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Sarcoidosis

 Sarcoidosis is a disease in which inflammation occurs in the lymph nodes, lungs, liver, eyes, skin or other tissues.

I. Causes, Incidence and Risk Factors

    Generally the cause of the disease is unknown. In sarcoidosis, tiny clumps of abnormal tissue (granulomas) form in certain organs of the body. Granulomas are clusters of immune cells.

     The disease can affect almost any organ of the body but it most commonly affects the lungs. 

Possible Causes:

extreme immune response to infection

high sensitivity to environmental factors

genetic factors.

    The condition is more common in African Americans than Caucasions, especially in Caucasions of Scandinavian heritage. Females are usually affected more often than males.

    Disease typically begins between ages 20 and 40. It's very rare in young children.

    A person with a close blood relative who has sarcoidosis is nearly five times as likely to develop the condition.

II. Symptoms

There may be no symptoms. When symptoms do occur, they can involve almost any body part or organ system in your body. Almost all patients have lung or chest symptoms:

Chest pain (most often behind the breast bone)

dry cough

shortness of breath.

Symptoms of general discomfort or uneasiness often occur:

fatigue (most common symptoms of chidlren)

fever

joint achiness or pain (arthralgia)

overall feeling of discomfort, illness or lack of well-being

weight loss (common symptom in children)

    2. Skin Symptoms

hair loss

raised, red, firm skin sores (erythema nodosum) almost always on the front part of the lower legs

rash

scars that have become raised or inflamed

    3. Nervous System Symptoms may include:

headache

seizures

weakness on one side of the face

    4. Eye Symptoms:

burning

discharge from the eye

dry eyes

itching

pain

vision loss

    5. Other Symptoms

Dry mouth

fainting spells if the heart is involved

nosebleeds

swelling in the upper part of the abdomen

III. Signs and Tests

A physical exam may show the following:

abnormal breath sounds (such as rales)

enlarged liver

enlarged lymph glands

enlarged spleen

rash

Often, the disease is found in patients with visible physical signs who have an abnormal chest x-ray.

Different imaging tests may help diagnose sarcoidosis:

chest x-ray: check to see if the lungs are involved or lymph nodes are enlarged.

CT scan of the chest

Lung gallium scan

To diagnose this condition, a biopsy is required. Biopsy of the lung using bronchoscopy is usually done. Biopsies of other body tissues may be needed.

The disease may affect the results of the following lab tests:

Calcium levels (urine, ionized, serum)

CBC

immunoelectrophoresis - serum

liver function tests

quantitative immunoglobulin (nephelometry)

serum phosphorus

IV. Treatment

Sarcoidosis symptoms will often get better on their own slowly without treatment.

Patients whose eyes, heart, nervous system or lungs are involved may need to be treated with corticosteroids (prednisone or methylprednisolone). Therapy may continue for 1 to 2 years. The mostseverely affected patients may need lifelong therapy.

Drugs that suppress the immune system (immunosuppressive medicines) are sometimes also needed:

Drug used most often is methotrexate, but azathioprine and cyclophosphamide are also sometimes recommended.

Hydroxychloroquine is useful for skin sarcoidosis.

Rarely, some people with end stage heart or lung damage may need an organ transplant.

V. Expectations (prognosis)

Many people with sarcoidosis are not seriously ill, and the disease may get better without treatment. About 30-50% of cases get better without treatment in 3 years. About 20% of people whose lungs are involved will develop lung damage.

The overall death rate from sarcoidosis is less than 5%. Causes of death include:

bleeding from lung tissue

heart damage, leading to heart failure and abnormal heart rhythms

lung scarring (pulmonary fibrosis)

VI. Complications

fungal lung infections (aspergilloma)

Glaucoma and blindness from uveitis (rare)

Kidney stones from high calcium levels in blood or urine

Osteoporosis and other complications of taking corticosteroids for long periods of time

Pulmonary hypertension

VII. Calling a Health Care Provider

Notify your health care provider if:

difficulty breathing

palpitations

vision changes

other symptoms of this disorder

[anatomyhelp-blog]

The Cellular Level of Organization

I. Parts of a Cell

plasma membrane: cell's flexible outer surface, separating the cell's internal environment from external. regulates flow of material in and out with selectivity.

cytoplasm: all cellular contents between membrane and the nucleus. two compartments:

        - cytosol: fluid portion containing H2O, dissolved solutes and suspended particles.

        - organelles: little organs; each has a characteristic shape/function. ie cytoskeleton, Golgi complex, lysosomes. 

II. The Plasma Membrane

flexible yet sturdy barrier that surrounds and contains the cytoplasm of the cell; fluid mosaic model

   A. The Lipid Bilayer

Two back-to-back layers made up of phospholipids, cholesterol and glycolipids

Phospholipids: 75% of the bilayer. Contain phosphate groups.

cholesterol: 20% of the bilayer. Steroid with a -OH group.

glycolipids: 5% of the bilayer. lipids with attached carbohydrate groups.

amphipathic: ie lipids. Have polar and nonpolar parts. In phospholipids, head is polar (hydrophilic), tail is nonpolar (-phobic). orient themselves so heads face interstitial liquid and cytosol.

cholesterol is weakly amphipathic. -OH group forms H bonds with the polar parts of phosphilipids and glycolipids.

glycolipids appear in only the layer facing the extracellular fluid.

   B. Arrangement of Membrane Proteins

Integral Proteins: extend into or through the lipid bilayer among fatty acid tails and firmly embedded in it

transmembrane proteins: span entire lipid bilayer and protrude in both cytosol and extracellular; attached by covalent bonds

amphipathic

    2. peripheral proteins: associate with polar heads of membrane lipids or with integral proteins at inner or outer surface of the membrane

    3. glycoproteins: proteins with carbohydrate groups attached to ends protruding into the extracellular fluid.

oligosaccharides: chains of 2-60 monosaccharides; straight or branched 

glycocalyx: carbohydrate parts of ylcolipids and glycoproteins form an extensive sugary coat. molecular signature that lets cells recognize each other.

   C. Functions of Membrane Proteins

ion channels: formed by integral membrane proteins. holes which ions ie K+ can flow in and out of a cell. most channels are selective.

transporters: selectively moving polar subsgtance or ion.

receptors: cellular recognition sites.

ligands: specific molecule that binds to a receptor.

    4. enzymes: catalyze specific chemical reactions at inside or outside of cell

    5. linkers: anchor proteins in membranes of other cells or to protein filaments. Peripheral proteins can also do this.

    6. Cell-identity markers: glycoproteins and glycolipids. enable cell to recognize other cells; ie blood transfusion.

    7. Membrane Fluidity

dependent on the number of double bonds in fatty acid tails and amount of cholesterol present.

allows interactions to occur within membrane.

allows for easy fix of tears and punctures of the membrane.

seldom flip flop because of hydrophilic parts adversity to hydrophobic area.

at normal body temperature, lipid bilayer is less fluid because of cholesterol. the opposite is true at lower temperature.

    8. Membrane Permeability

selective permeability: membranes allow some substances more readily than others.

permeable to nonpolar, uncharged molecules ie oxygen, carbon dioxide, steroids, slightly permeable to water and urea. Impermeable to large uncharged polar molecules and ions.

channels and transporters increase permeability to ions but are very selective. 

    9. Gradients Across the Plasma Membrane

difference in concentration of chemical from one place to another; ie concentration of oxygen and sodium in extracellular fluid; cytosol -> potassium ions and carbon dioxide

electrical gradient: difference in charges between two regions

        - membrane potential

substance moves down its concentration gradient -> equilibrium

electrochemical gradient: combined influence of concentration gradient and membrane potential on movement.

   D. Transport Across the PLasma Membrane

passive transport: substance moves down concentration/electric gradient using only its kinetic energy. No input of energy from the cell.

active transport: cellular energy drives substance uphill against gradient. uses ATP.

Kinetic energy intrinsic to moving particles ie diffusion, osmosis.

Kinetic Energy Transport

diffusion: passive process in which random mixing of particles occur because of their kinetic energy. moves down gradient.

factors influencing diffusion rate:

        - steepness of concentration gradient: greater difference in concentration increases rate of diffusion especially with charged particles.

        - temperature: high temperature = high rate of diffusion

        - mass of diffusing substance: high mass = lower rate of diffusion

        - surface area: high surface area available for diffusion = high rate of diffusion

        - diffusion distance: high distance decreases rate of diffusion

Diffusion Through the Lipid Bilayer

        - nonpolar hydrophobic molecules diffuse freely ie O2, CO2, N2, fatty acids, steroids, fat soluble vitamins, small alcohols and ammonia, sometimes H2O and urea.

Diffusion Through Membrane Ion Channels

        - integral transmembrane proteins allowing passage of small inorganic ions too hydrophilic to get through.

        - generally slower because less surface area.

        - different permeabilities

osmosis: net movement of solvent through selectively permeable membrane, passive.

        - area from high concentration to low concentration

        - aquaporin: integral membrane proteins acting as water channels

        - occurs only when membrane permeable to water but not certain solutes

        - hydrostatic pressure: pressure exerted by liquid. The higher the concentration is, it forces water back into the left side. Equilibrium when molecules move at equal rates.

        - osmotic pressure: proportional to concentration of solute particles that can't cross the membrane. Increase the concentration of the solute -> increase of osmotic pressure. The amount of pressure needed to prevent water movement.

tonicity: measure of solution's ability to change volumes of cells by altering water content.

        - isotonic solution: any solution where cell maintains normal shape and volume. concentration of solute that can't cross plasma membrane are equal.

           * normal saline solution: red blood cells maintain shape

        - hypotonic solution: solution with lower concentration of solute than red blood cell cytosol. Water molecules -> red blood cells -> swell and burst

           * hemolysis: rupture of red blood cells

           * lysis

           * cells in distilled H2O.

        - hypertonic solution: solution with greater concentration of solute than cytosol, ie 2% NaCl brackish water.

           * crenation: H2O leaves cell causing shrinkage.

    2. Medical Uses of Isotonic, Hypertonic, Hypotonic

intravenous (IV) solutions: liquids infused into blood; isotonic

relieves fluid overload by causing osmosis of water

hypotonic solutions: move from blood to interstitial fluid to rehydrate them

    3. Transport by Transporter Proteins

Facilitated Diffusion

        - a solute binds to a specific transporter on one side of the membrane and released after transporter undergoes a change in shape. 

           * too polar or highly charged to diffuse.

        - passive; down a concentration gradient.

        - rate determined by steepness of concentration gradient across membrane

        - transport maximum: the upper limit on rate at which faciliated diffusion occurs; once all transporters occupied, maximum is reached.

        - exhibits saturation

        - selective permeability regulated to achieve homeostasis

           * ie insulin raises transport max for facilitated diffusion; inability to use insulin is called diabetes mellitus.

Active Transport

        - particles that must enter/leave cells go against concentration gradient

        - energy required for transport proteins to move solutes across membrane across concentration gradient.

           * energy from hydrolysis of ATP; primary active transport

           * energy stored in ionic concentration gradient; secondary active transport

        - transport maximum and saturation

        - Na+, K+, Ca2+, I-, Cl-, amino acids, monosaccharides

Primary Active Transport

        - ATP changes shape of transporter protein; pumps substance across membrane against concentration gradient

        - pumps: transporter proteins that carry out primary active transport

        - 40% of ATP used on primary active transport

        - Na-K pump: expels Na+ and pumps K+ in. Another name is Na+/K+ ATPase.

           * maintain low concentration of Na+ by pumping against gradient. Pumps K+ into cytosol.

        - Three Na+ in the cytosol bind to the pump protein

           * binding of Na+ triggers hydrolysis of ATP -> ADP. attaches a phosphate group to pump protein changing shape of the protein.

           * Expels Na+, now new shape binds 2 K+ in EC fluid to protein.

           * K+ binding releases phosphate group from protein causing another shape change in the pump protein.

           * pump reverts back to original shape -> K+ in cytosol. repeats.

        - Na+ improtant for tonicity in EC fluid and cytosol.

Secondary Active Transport

        - Energy stored in a Na+ or H= concentration gradient drives other substances against their own gradients indirectly using energy from ATP

        - Na+/K+ pump maintains step gradient of Na+ therefore has potential energy.

        - symporters: move two substances in opposite directions across the membrane.

Digitalis Increases Ca2+ in Heart Muscle Cells

        - slows Na+/K+ pump allowing Na+ to accumulate

        - More Ca+ stays inside the heart and strengthens heartbeat

    4. Transport in Vesicles

vesicle: small spherical sacs that import and move materials into EC fluid.

endocytosis: materials move into a cell in a vesicle formed from plasma membrane.

exocytosis: materials move out by fusion with the plasma membrane. both endocytosis and exocytosis are active processes.

Endocytosis:

        - receptor-mediated endocytosis: highly selective type of endoccytosis by which cells take up specific ligands ie. LDL, antibodies, vitamins.

           * binding: particle binds to protein receptor to form a complex. Then, a protein forms around it on the cytoplasmic side to fold the membrane inwards. 

           * vesicle formation: edges of membrane pinch off.

           * uncoating: right after formation, vesicle loses its protein coat

           * fusion with endosome. Particle separates from its receptors

           * regraduation in lysosomes: lysosomes break it down.

        - phagocytosis: form of endocytosis. Cells engulf large particles

        - pseudopods: projection of cytosol to plasma membrane binding. Individual cases of undigested material but remain undisposed indefinitely in a vesicle. (residual body)

        - pinocytes: tiny droplets of EC fluid taken up. All solutes dissolved. aka bulk phase endocytosis. movement of liquid.

Exocytosis: releases materials from the cell; all cells carry this out.

        - secretory cells: liberate digestive enzymes; hormones, mucus

        - nerve cells: release transmitters

        - membrane enclosed vesicles (secretory) fuse with membrane and release into the EC fluid

Transcytosis: active; vesicles undergo endocytosis on one side of the cell and undergo exocytosis on the opposite side. Most common in endothelial cells, move between blood plasma and interstitial fluid.

   E. Cytoplasm

cytosol: intracellular fluid that surrounds organelles. 65% of total volume. 75-90% composed of water.

lipid droplets and glycogen granules aggregate for storage.

site for chemical reactions; catalyze glycolysis.

    2. organelles: specialized structures with specific functions.

Cytoskeleton: network of protein filaments extend through cytosol.

        - microfilaments: thinnest; made of actin. Most prevalent at periphery. generate movement and mechanical support, cell division, locomotion. anchor the cytoskeleton.

           * microvilli: cell extensions; tufts, nonmotile projections that increase surface area to facilitate absorption.

        - intermediate filaments: second thinnest; exceptionally strong, found in areas subject to mechanical stress, stabilize position of organelles.

        - microtubules: largest component, unbranched hollow tubes; tubulin. Begins in the centrosome. Helps determine cell shape.

Centrosome: consists of a pair of centrioles and pericentriolar material

        - centrioles: composed of nine clusters of microtubules in a circular pattern.

        - pericentriolar: surround centrioles. Have complexes made of tubulin. organizing centers for growth of mitotic spindle; critical for cell division.

        - replicate so future cells can replicate.

Cilia and Flagella

        - cilia: short projections extending from surface of the cell. anchored to a basal body; ie respiratory tract

        - flagella: longer than cilia. Move an entire cell; ie sperm cell

ribosomes

        - sites of protein synthesis

        - ribosomal RNA: more than 50 proteins; destined for organelles

Endoplasmic Reticulum: network of membranes in the form of flattened sacs or tubules

        - Rough ER: continuous with nuclear membrane and flattened sacs. contain many ribosomes therefore produces many proteins.

        - Smooth ER: network of membrane tubules. no ribosomes but enzymes make it structurally and functionally more diverse.

            * prolonged drug use alters smooth ER; creates a tolerance for drug.

Golgi Complex

        - consists of 3 to 20 cisternae; small flattened membranous sacs

           * entry/cis face: cisterna that faces the rough ER; convex

           * exit/trans face: cisterna facing plasma membrane; concave

           * medial cisternae: sacs between entry and exit faces

        - transport vesicles: proteins synthesized on rough ER bud.

           * moves toward entry face of Golgi complex

           * several transport vesicles create entry face and release proteins

           *proteins move from entry face into medial cisternae 

           * transfer vesicles move specific enzyme back toward cis face and move some towards trans face

           * in trans face, products are further modified, sorted and packaged

        - secretory vesicles: deliver proteins to plasma membrane; discharged into EC fluid

         - membrane vesicles: deliver contents into plasma membrane. adds new segments.

Lysosomes

        - membrane enclosed vesicles that form from Golgi complex

        - pH of 5 in interior

        - helps recycle worn out cell structure

        - autophagy: organelle is digested; enclosed by ER membrane and binds into lysosome

        - autolysis: pathological conditions; lysosomal enzymes destroy entire cell

        - Tay-Sachs Disease: absence of single lysosomal enzyme called Hex A. usually breaks Gm2; excess accumulates and causes nerve cells to defect

Peroxisomes

        - contain oxidases, enzymes that can oxidize organic substances

        - abundant in liver; detox alcohol and other substances

        - catalase decomposes byproduct H2O2.

Proteasomes

        - cytosilic proteins require continuous destruction of unneeded, damaged or faulty proteins

        - contain proteases: enzymes that cut proteins into small peptides

Mitochondria

        - generate most ATP via respiration; powerhouses of the cell

        - found in areas of the cell where O2 enters or high amounts of ATP

        - outer and inner mitochondrial membrane: inner consists of cristae; series of folds

        - matrix: enclosed by inner membrane

        - enzymes located in cristae and create ATP

   F. Nucleus

nucleus: spherical or oval shaped structure usually most promninent in a cell

nuclear envelope: separates nucleus from cytoplasm. lipid bilayers.

nuclear pores: openings extending through envelope; control movement between nucleus and cytoplasm. 

nucleoli: spherical bodies that produce ribosomes. cluster of protein; DNA and RNA without membrane. Sites of ribosome production.

genes: hereditary units; control cellular structure and activities.

chromosomes: genes are arranged in these coils. Somatic cells have 46.

chromatin: complex of DNA proteins and RNA coiled tightly together.

genome: total genetic information carried in a cell or an organism.

nucleosome: a "head" on the "string" of chromatin in electron micrographs.

histones: a cone of 8 proteins that help to organize DNA folding.

Linker DNA: "string" between bonds holding nucleosomes together.

chromatin fiber: large-diameter that folds into large loops

chromatids: fibers replicate causing loops to condense thus forming chromatids.

   G. Protein Synthesis

proteome: all of an organism's protein

gene expression: DNA is used as a template for synthesis of a specific protein

base triplet: sequence of three nucleotides in DNA

codon: complementary to base triplet; specifies a particular amino acid

genetic code: set of rules relating base triplet to its codon and corresponding amino acid

Transcription: occurs in the nucleus; genetic information serves as a template for copying into complementing codons.

messenger RNA (mRNA): directs synthesis of a protein

ribosomal RNA (rRNA): joins both ribosomal proteins to make ribosomes

transfer RNA (tRNA): binds to amino acid and holds it in place on a ribosome until incorporated into a protein during translation.

        - opposite end has an anticodon. attaches to mRNA codon.

RNA polymerase: catalyzes transcription of DAN.

promoter: special nucleotide sequence located near the beginning of a gene.

terminator: transcription ends at this nucleotide sequence.

introns v. exons: introns do not code for proteins; exons do.

pre-mRNA: transcript including information from both introns and exons

small nuclear ribonoucleo proteins: remove introns from pre-mRNA . enzymes that cut out introns and splice together exons to create functional mRNA.

alternative splicing: process in which pre-mRNA transcribed from a gene and spliced so that it creates several mRNA

    7. Translation: nucleotide sequence in mRNA specifies amino acid sequence of a protein; ribosomes carry out in cytoplasm. 

mRNA binds to ribosomal subunit. tRNA (initiator) binds to start codon (AUG) where translation starts.

large ribosomal subunits attaches to smaller one; mRNA complex creating functional ribosome, fits into "P site". 

anticodon of another tRNA with attached amino acid pairs with second mRNA at A site. 

large ribosomal thing catalyzes formation of peptide bond between AUG which separates from tRNA at P site and amino acid at A site.

after peptide bond is formed, tRNA at the P site detaches from ribosome and shifts the mRNA strand by one codon. New sequences are then exposed to the A site; steps 3 to 5 occur repeatedly.

protein synthesis ends when ribosomes reach a stop codon causing it to detach from final tRNA.

polyribosome: ribosomes attached to the same mRNA

recombinants: organisms whose cell's DNA is altered to produce proteins not regularly produced.

   H. Cell Division

process by which cells reproduce themselves. (somatic, reproductive)

somatic cell: any cell other than a germ cell, a gamete or any precursor of gamete.

mitosis: nuclear division

cytokinesis: cytoplasmic division

somatic division: replaces dead or injured cells and adds new ones.

reproductive: produces gametes via meiosis.

Somatic Cell Division

cell cycle: somatic cells duplicate contents and divide into two. 

homologous chromosomes: two chromosomes that make up a pair.

sex chromosomes: X, Y

diploid cells: 2n; 2 sets of chromosomes.

Interphase:

        - cell replicates DNA through phases G, S and G2.

        - G1 phase: interval between mitotic phase and S phase. cell is metabolically active; replicates most organelles and cytosolic components but not DNA.

        - G0: cells remaining in G1 phase for a very long time; ie brain cells.

        - S phase: interval between G1 and G2; DNA replication occurs

        - G2: interval between S and mitotic phase; enzymes and proteins are synthesized.

Mitotic Phase: distribution of two sets of chromosomes into two nuclei.

        - prophase:

           * centromeres hold chromatid pair together. contain protein complex; kinetochore.

        - mitotic spindle: microtubules that attach to the kinetochore. metaphase            * microtubules align centromeres at the exact center called metaphase plate         - anaphase: centromeres split, pushing chromatid pairs toward opposite ends.         - telophase: nuclear envelopes and nucleoli reappear; chromatin form; mitotic spindle disappears.

Cytokinesis

        - division of cytoplasm and organelles

        - cleavage furrow: contractile ring (actin microfilaments) divide cytoplasm.

    2. Control of Cell Destiny

cyclin-dependent protein kinases: enzymes that can transfer a phosphate group from ATP to a protein to activate it. crucial in regulation of DNA replication.

cyclins: levels rise and fall during cell cycle. Turns cyclin dependent kinases on and off. Timing transitions from G2 to S to G2 phase.

apoptosis: an orderly genetically programmed cell death. cell shrinks by producing destructive enzymes; phagocytosis finishes up.

necrosis: pathological cell death resulting from tissue injury. stimulates an inflammatory response in immune system. 

tumor-suppressor genes: produce proteins that normally inhibit cell division; ie p53 in chromosome 17. 

    3. Reproductive Cell Division

Meiosis: reproductive cell division creating haploid (n) gametes.

Meiosis I

        - Prophase I: chromosomes shorten and thicken; nuclear envelope and nucleoli disappear. mitotic spindle form.

            * synapsis: doesn't occur in mitosis. sister chromatids of each homologous chromosomes pair off.

           * tetrad: resulting structure of four chromatids.

           * crossing-over: exchange between parts of nonsister chromatids resulting in genetic recombination.

        - metaphase I: tetrads line along metaphase plate.

        - anaphase I: homologous pair separate. pair chromatids stay together.

        - net result: each cell contains haploid because only one member of each pair present.

Meiosis II

        - two haploid cells from Meiosis I divide to form 4 haploid gametes.

   I. Cellular Diversity

200 different cell types.

may be round, oval, cuboidal, columnar, elongated, star shaped, cylindrical

variations in structure facilitate function.

III. Aging and Cells

aging: normal process accompanied by a progressive alteration of the body's homeostatic and adaptive responses. increases vulnerability to environment.

geriatrics: specialized branch of medicine dealing with medical problems and care of the elderly.

gerontology: scientific study of processes and problems associated with aging.

telomeres: specific DNA sequences found only at the tips of each chromosomes; protect from erosion. Division shortens telomeres.

Glucose forms irreversible cross links causing loss of elasticity.

Free radicals produce oxidatives

Progeria and Werner Syndrome

        - Progeria: disease characterized by normal development in the first year of life followed by rapid aging.

        - Werner Syndrome: rare, inherited disease causing rapid acceleration of aging while in 20s. 

[anatomyhelp-blog]

The Chemical Level of Organization

I. How Matter Is Organized

   A. Chemical Elements

chemical elements: all forms of matter are made up of these number of building blocks that cannot be simpler substances by ordinary chemical means.

chemical symbol: one or two letters in English/Latin designating an element.

chemistry: science of structure and interactions of matter.

matter: anything that takes up space and has mass.

    4. mass: amount of matter in any subject.

weight: force of gravity acting on matter.

    5. 26 elements are present in the body but 4 major elements make up 96%

oxygen, nitrogen, carbon, hydrogen

    6. Lesser Elements: Calcium, Phosphorus, Potassium, Sulfur, Sodium, Chlorine, Magnesium, Iron

   B. Structure of Atoms

atoms: smallest units of matter that retain properties and characteristics of the elements.

subatomic particles: compose an atom; protons, neutrons, electrons

nucleus: dense central core of an atom

protons: positively charged subatomic particles in the nucleus

neutrons: uncharged subatomic particles in the nucleus

electrons: negatively charged cloud enveloping nucleus

        - electron shells: the path of motion within certain regions around nucleus

           * first shell: 2 electrons

           * second shell: 8 electrons

           * third shell: 18 electrons

   C. Atomic Number and Mass Number

atomic number: the number of protons in the nucleus of an atom

mass number: the sum of its protons and neutrons

isotopes: atoms of an element that have different numbers of neutrons and therefore different mass numbers

radioactive isotopes: unstable; nuclei decay into a stable configuration by emitting subatomic particles

half-life: of an isotope is time required for half of the radioactive atoms in an isotope to decay into a more stable form

tracers: follow movement of certain substances through the body.

   D. Atomic Mass

dalton: standard unit of mass of atoms and their subatomic particle; amu.

atomic mass: of an element, is the average of mass of all naturally occurring isotopes.

    E. Ions, Molecules, and Compounds

ion: an atom that has a positive or negative charge because it has an unequal number of protons and electrons

cation: positively charged ion

anion: negatively charged ion

ionic compounds generally exist as solids with repeating arrangement of ions

electrolyte: an ionic compound that breaks apart into positive and negative ions in solution. These solutions can conduct an electric current.

   B. Covalent Bonds

When two or more atoms share electrons rather than gaining or losing

single covalent: when two or more atoms share an electron pair

double covalent: when two or more atoms share two pairs of electrons.

triple covalent: when two or more atoms share three pairs of electrons

nonpolar covalent bond: when electrons are shared equally between two atoms.

polar covalent bond: sharing of electrons between two atoms is unequal- the nucleus of one atom attracts the shared atom more strongly.

electronegativity: the power to attract electrons to itself.

   C. Hydrogen Bonds

hydrogen bond: forms when a H atom with a partial positive charge of neighboring electronegative atoms. Weaker than ionic and covalent bonds.

cohesion: tendency of like particles to stay together.

surface tension: created by cohesion of water molecules; measure of difficulty of stretching/breaking the surface of a liquid.

III. Chemical Reactions

occurs when new bonds form or old bonds break between atoms.

reactants: starting substances of a reaction

products: final substances of a reaction

mass of substances = mass of products

metabolism: all chemical reactions occurring in the body

   A. Forms of Energy and Chemical Reactions

energy: capacity to do work

potential energy: energy stored by matter due to its position

kinetic energy: energy associated with matter in motion.

chemical energy: form of potential energy stored in bonds of compounds and molecules.

law of conservation of energy: energy can't be created or destroyed; only converted. 

   B. Energy Transfer in Chemical Reaitons

exergonic reactions: release more energy than absorbed

endergonic reactions: absorb more energy than released

Activation Energy: collision energy needed to brea kthe chemical bonds of the reactants.

concentration: more particles of matter present, therefore increases the chance of collision

temperature: as temperature increases, speed of particles increases, therefore more collisions occur.

   C. Catalysts

chemical compounds that speed up chemical reactions by lowering the activation energy needed for a reaction to occur.

does not alter difference in potential energy between reactants and products.

lowers energy needed to start a reaction

orients collision paths.

   D. Types of Chemical Reactions

Synthesis Reactions - Anabolism

synthesis reaction: when two or more atoms, ions, molecules combine to form new and larger molecules.

anabolism: all synthesis reactions occurring in the body.

endergonic because it uses energy.

    2. Decomposition Reations - Catabolism

decomposition reaction: split up large molecules into smaller atoms, ions, molecules

catabolism: all decomposition reactions

exergonic: release more energy than absorbed

    3. Exchange Reaction

exchange reation: consist of both synthesis and decomposition

HCl + NaHCO3 -> NaCl + H2CO3

    4. Reversible REactions

reversible reaction: when the product can revert to original reactants

many require catalysts

IV. Inorganic Compounds and Solutions

inorganic: usually lack carbon; structurally simple. H2O, salts, H+, OH-, 55-60% of the body

organic: contain carbon and usually hydrogen. always covalently bonded. has a complex structure. 38-43% of the body.

   A. Water

most important and abundant inorganic compound.

Water as a Solvent

solution: a medium in which substances dissolve in together.

solvent: substance that dissolves solutes. In solution, there is more solvent than solute.

solute: being dissolved by solvent; ie. salts in sweat. 

hydrophilic: solutes charged or contain polar covalent bonds. dissolve easily in water.

hydrophobic: nonpolar covalent bonds. not water soluble. ie animal fats, vegetable oils.

water is ideal for metabolic reactions and washing out wastes.

    2. Water in Chemical Reactions

water serves as medium for mos reactions, sometimes reactant or product.

hydroloysis: breakdown of larger molecules by addition of water.

dehydration synthesis: removal of water molecule to join together smaller molecules.

    3. Thermal Properties Of Water

heat capacity: high because it can absorb and release large amounts of heat with little change in its own.

heat of vaporization: water requires a large amount of heat to change from liquid to gas.

    4. Water As A Lubricant:

major component of mucus and lubricating fluids to reduce friction between muscles, organs, bones.

   B. Solutions, Colloids, and Suspensions

mixture: combination of elements/compounds physically blended together but not chemical bonds.

colloid: differs from a solution because of the size of the particles

large enough to scatter light, transparent and opaque

ie. milk

    3. suspension: suspended material will eventually settle out.

blood

    4. concentration: of a solution may be shown as:

mass/volume percentage: relative solute mass in given volume of a solution

moles/L: total number of molecules in a given solution

        - mole: amount of any substance with mass in grams equal to the sum of -         atomic mass

        - Avogadro's Number: 6.023 x 10^23

   C. Inorganic Acids, Bases, and Salts

dissociate: when inorganic acids, bases, salts separate into ions and surrounded by water molecules. 

acid: substance that dissociates into one or more H+

also a proton donor

    3. base: removes H+ from a solution. Many dissociates into one or more OH-

proton acceptor

    4. salt: when dissolved in H2O, dissociates into cations and anions

acids and bases react with one another to form salts

HCl + KOH -> H+ + Cl- + K+ + OH- -> KCl + H2O

does not give off H+ or OH-

   D. Acid-Base Balance: Concept of pH

pH scale: measure of acidity/alkalinity of a solution. Scale of 0-14.

pH 7 = 1x10^-7 H+; pH 4 = 1x10^-4 H+

    2. acidic solution: more H+ than OH- pH < 7

    3. alkaline: less H+ than OH-. pH > 7

   E. Maintaining pH: Buffer Systems.

Normal Body pH between 7.35 and 7.45

excess H+ < 7.35 -> acidosis

excess OH- > 7.45 -> alkalosis 

    2. buffer systems: function to convert strong acids or bases into weak acids

        or bases

    3. buffers: chemical compounds that convert strong acids/bases by               -       removing/adding H+

    4. carbonic acid-bicarbonate buffer system

excess H+ -> H+ + HCO3 -> H2CO3

excess OH- -> H2CO3 -> H+ + HCO3

V. Organic Compounds

   A. Carbon And Its Functional Groups

Carbon has four electrons in its valence shell; most commonly binds with nitrogen, oxygen or hydrogen

carbon skeleton: chain of carbon atoms in an organic molecules

hydrocarbon: carbons bonded with hydrogen

    3. functional groups: atoms or molecules bound to a hydrocarbon skeleton

each confer a specific characteristic trait of that group

Hydroxyl: R-O-H; occurs in alcohols. dissolves easily in H2O because of    -OH group

Sulfhydryl: R-S-H; in thiols, certain amino acids; helps stabilize the shape of a protein, ie cysteine

carbonyl: R-C=O-R or R-C=O-H; ketones contain a carbonyl group in the carbon skeleton. Polar and hydrophilic. Aldehydes contain carbonyl group at the end of the skeleton.

Carboxyl: R-C=O-OH or R-C=O-O, carboxylic acids contain this group at the end of the carbon skeleton. all amino acids have -COOH at one end.

Ester: R-C=O-O-R. predominate in dietary fats and oils and also occur in body triglycerides. Aspirin is ester of salicyclic acid.

Phosphate: R-O-P=O-O-O (PO4^2-) very hydrophilic because of the two negative charges. ie ATP

amino: R-N-H-H or R-N-H-H-H; amines have a -NH2 which can act as a base and pick up a H+ ion. Gives amino group a positive charge. Most amino groups have a +1 charge.

    4. macromolecules: small organic molecules can combine into these large       -      molecules

    5. polymer: large molecule formed by covalent bonding of many identical or  -       similar small building block molecules called monomers. 

dehydration synthesis

    6. isomers: molecules with the same molecular formula but different                 -      structures.

   B. Carbohydrates

include sugars, glycogen, starches and cellulose. 2-3% of total body mass. function as a source of energy to generate ATP, ie DNA.

Monosaccharides and Disaccharides

simple sugars

monosaccharides: monomers containing 3-7 carbon atoms. designated by suffix -ose. ie glucose, fructose, galactose, deoxyribose and ribose.

disaccharides: formed by dehydration synthesis of two monosaccharides, ie sucrose (glucose + fructose), lactose (galactose + glucose) and maltose (glucose + glucose).

artificial sweeteners: hydrolyzed disaccharides

    2. Polysaccharides

contains tens to hundreds of joined monosacchardies. insoluble in water.

glycogen: entirely of linked glucose monomers. stored form of carbohydrates in animals; liver

starches: polysaccharides from glucose by plants. major carbohydrates in a diet.

cellulose: found in plants but can't be digested by humans. help in bowel movement. 

   C. Lipids

make up 18-25% of body mass.

Fewer covalent bonds because of proportion of oxygen is smaller in soluble in polar solvents (water); hydrophilic

lipoproteins: lipid molecules join with hydrophilic protein molecules soluble in water.

   3. Triglycerides

most plentiful, aka triglycerols. solid or liquid at room temperature.

provide twice as much energy as carbohydrates; stored in adipose

glycerol: 3-carbon; forms backbone of the triglyceride molecule

fatty acids: attached by dehydration synthesis; one to each carbon in covalent chemical bond is called an ester linkage

saturated fats: single covalent bonds between fatty acid carbon atoms. saturated with H atoms are solid at room temperature.

monounsaturated fats: contain fatty acids with one double covalent bond between fatty carbon atoms, ie oleic acid. decrease heart risk.

polyunsaturated fats: contain more than one double covalent bond between fatty acid atoms, ie sunflower oil. Also decreases heart risk.

    4. Fatty Acids in Health and Disease

essential fatty acids: fatty acids essential to human health not produced naturally in the human body

omega-3, fatty acids, omega-6 and as fatty acids

overall promotion of health

    5. Phospholipids

glycerol backbone and two fatty acid chains attached to the first carbon

hydrophilic head and hyrophobic tail

amphipathic

    6. Steroids

four rings of carbon

cholesterol: minor component in cell membranes

bile salts: digestion and absorption of dietary lipids

adrenocortical hormones: regulates metabolism, resistance to stress and salt and water balance.

sex hormones: stimulate reproductive functions and sexual traits.

    7. Other Lipids

eicosanoids: lipids derived from a 20-carbon fatty acid called arachidonic acid.

        - prostaglandins: modify responses to hormones ie. inflammatory              -         response to prevent ulcers, regulate body temperature and blood clots.

        - leukotrienes: allergic and inflammatory responses

fatty acids: catabolized to generate ATP or synthesize triglycerides and phospholipids

carotenes: synthesis of vitamin A; make visual pigments in the eyes, antioxidants.

Vitamin E: promotes wound healing, prevents tissue scarring, contributes to normal structure and function of nervous system. antioxidant.

Vitamin K: synthesis of blood-clotting proteins.

lipoproteins: transport lipids in blood, carry triglycerides and removes excess cholesterol.

   D. Proteins

macromolecules containing carbon, hydrogen, oxygen and nitrogen. some have sulfur. 

Functions of Proteins

Structural: structural framework of various parts of the body, ie collagen

Regulatory: hormones regulate processes, control growth and development. function as neurotransmitters ie. insulin.

Contractile: allow shortening of muscle cells causing movement. ie myosin and actin.

Immunological: responses that protect body against foreign substances.

Transport: carries vital substances throughout the body

Catalytic: enzymes regulate biochemical reactions.

    2. Amino Acids and Polypeptides

amino acids: monomers of proteins

        - 3 functional groups: amino (-NH2), acidic carboxyl (-COOH) and side        -         chain (R)

peptide bond: covalent bond joining amino acids. formed by dehyration synthesis.

dipeptide: when two amino acids combine.

tripeptide: when another amino acid is added to dipeptide.

peptide: 4-9 amino acids or polypeptide (10-2000 amino acids)

    3. Levels of Structural Organization in Proteins

primary structure: unique sequence of amino acids linked covalently to form polypeptide.

        - sickle-cell disorder: nonpolar amino acid (valine) replaces polar amino     -         acid (glutamate) through two mutations in hemoglobin thus decreasing   -         solubility of hemoglobin. 

secondary structure: repeated twisting or folding of neighboring amino acids in the polypeptide chain. Stabilized by hydrogen bonds; form at regular intervals.

        - alpha helixes

        - beta pleated sheets

tertiary structure: 3D shape of polypeptide chain. determines how protein will function. some parts are hydrophobic or hydrophilic.

        - disulfide bridges: S-S; strongest but least common between cysteine

        - chaperones: helper molecules aiding folding process

quaternary structure: arrangement of individual polypeptide chains relative to one another. Variation in structure and shape directly related to function.

denaturation: when proteins unravel in an altered environment ie high pH or high temperatures

    3. Enzymes

enzymes: protein molecules are catalysts

        - apoenzyme: protein portion of enzyme

        - cofactor: nonprotein portion. may be derived from metal ion or                -         coenzyme aka vitamin. 

highly specific

        - each enzyme binds only to specific substrates; reactant.

        - active site: part of the enzyme thought to 'fit' the substrate.

           * change shape to fit substrate is induced fit

enzymes are very efficient. many reactions in a cell.

subject to variety 

How it works:

        - temporary intermediate compound when substrates make compound

        - substrate molecules transformed by rearrangement of existing atoms

        - breakdown of substrate molecule or combination -> products of a              -         reaction

        - After reaction, enzyme is free to attach to other substrate molecules

        - Sometimes a reaction can be reversible depending on quantity of           -         substrates and products.

    4. DNA and RNA

nucleic acids: organic molecules contain carbon, hydrogen, oxygen and nitrogen.

DNA: forms inherited genetic material inside each human

        - gene: segment of DNA molecule controlling protein synthesis                   -        determining physical traits. 

RNA: second nucleic acid relays information from genes to guide protein synthesis

nucleotides: monomers making up nucleic acids; three types:

        - nitrogenous base: contain carbon, hydrogen, oxygen and nitrogen

        - adenine and guanine: larger, double-ringed; purines

        - cytosine and thymine: smaller, single-ringed bases; pyrimidines

pentose sugar: 5-carbon sugar called deoxyribose attached to each base in DNA

phosphate: (PO4^3-) alternate with pentose sugars to form DNA backbone

double helix model: Crick & Watson; ladder of alternating phosphate and pentose sugars.

        - mutation: change in base sequence of DNA strand; can result in cell        -         death, cancer or genetic defects. 

ribose: pentose sugar in RNA nucleotide, contains pyrimidine uracil instead of thymine. three different kinds: ribosomal, messenger and transfer.

    5. DNA Fingerprinting

used in research and law to determine whether suspect's DNA matches sampled DNA.

    6. Adenosine Triphosphate

ATP: "energy currency" of the living, transfers energy liberated in exergonic catabolic reactions to power cellular activities that require energy. 

3 phosphate groups and 5 carbon sugar ribose attached to adenine

ADP: adenosine diphosphates, enzyme is ATPase. ATP synthase synthesizes to create ATP.

Anaerobic Respiration: doesn't need O2 to run. glucose is broken down to pyruvic acid. Yields 2 ATP

Aerobic: with O2. glucose broken down completely into CO2 and water. yields heat and 36 or 38 ATP. 

[anatomyhelp-blog]

An Introduction To The Human Body

I. Anatomy and Physiology Defined

Anatomy: science of body structures and relationship among them.

        - dissection: careful cutting apart of body structures to study relationship.

Physiology: science of body functions; how the body works.

II. Levels of Structural Organization

   A. Levels

Chemical Level

atoms: smallest unit of matter

molecules: 2 or more atoms joined together

Carbon, Hydrogen, Oxygen, Nitrogen, Phosphorus, Calcium, Sulfur; important elements of the body.

    2. Cellular Level

cells: basis structural and functional units of an organism.

    3. Tissue Level

tissues: groups of cells and materials surrounding them that work together to perform a particular function.

Epithelial, connective, muscular, nervous

    4. Organ Level

organs: composed of 2 or more different types of tissues; specific functions and recognizable shape.

skin, bones, stomach, heart, liver, lungs, brain

    5. System (Organ-System) Level

system: related organs with a common function

digestive system: mouth, salivary glands, pharynx, esophagus, stomach, etc.

    6. Organismal Level

organism: any living individual. All parts of the human body functioning together.

   B. Noninvasive Diagnostic Techniques

Inspection: the examiner observes the body for abnormal changes.

Palpation: feeling body surface with hands. To detect enlarged/tender internal organs or abnormal masses.

Auscultation: listening to body sounds to evaluate functioning of certain organs. Crackling sounds in the chest may signal abnormal fluid accumulation. 

Percussion: tapping of body surface with fingertips and listening to echo.

III. Characteristics of Living Human Organism

   A. Basic Life Processes

Metabolism: sum of all chemical processes in the body.

catabolism: breakdown of complex chemical substances into simpler components.

anabolism: building up of complex chemical substances from smaller, simpler components. 

Food catabolized, proteins -> amino acids. Anabolizing proteins; amino acids -> new proteins.

    2. Responsiveness: body's ability to detect and respond to changes.

    3. Movement: motion of the whole body; individual organs, single cells

    4. Growth: increase in body size resulting from increase in size of existing cells number of cells or both.

    5. Differentiation: development of a cell from an unspecialized to a specialized state. 

stem cells: precursor cells that can divide and make cells to differentiate into specialized cells.

    6. Reproduction: formation of new cells for tissue growth repair or replacement or to the production of a new individual.

   B. Homeostasis

condition of equilibrium in the body's internal environment due to ceaseless interplay of body's many regulatory processes.

   C. Body Fluids

dilute, watery solutions containing dissolved chemicals found inside and surrounding cells. 

        - intracellular fluid (ICF): fluid within cells

        - extracellular fluid (ECF): fluid outside body cells

           * interstitial fluid: ECF that fills narrow spaces between cells of tissues

           * blood plasma: ECF within blood vessels

           * lymph: ECF within lymphatic vessels

           * cerebrospinal fluid: in and around the brain and spinal cord

           * synovial fluid: ECF in joints

           * aqueous humor and vitreous body: ECF of the eyes.

interstitial fluid = internal environment

Exchanges between interstitial fluid and blood plasma removes waste and provides glucose and oxygen.

IV. Control of Homeostasis

Nerve Impulses: action potential or electronic signals sent to organs then correct deviations from the balanced state. [Nervous System]

Hormones: messenger molecules work slower than nerve impulses. Regulation. [Endocrine System]

   A. Feedback Systems

cycle of events where the body, system, is constantly watched, fixed, evaluated and repeat.

controlled condition: a monitored variable; body temp, blood pressure

stimulus: disruption that changes a controlled condition

receptor: monitors changes in a controlled condition and sends input to a control center. THese inputs are in the form of chemical signals/nerve impulses.

Control Center

brain; sets a range of values the controlled condition should be, evaluates input and creates output in the form of commands

output is nerve impulse, hormones or chemical signals

    3. Effector

Receives output and produces response to change controlled condition.

    4. Negative Feedback Systems

reverses a change in a controlled condition

blood pressure: 

        - stimulus disrupts homeostasis

        - Increases blood pressure

        - baroreceptors send input to control center (the brain)

        - the brain interprets the input and sends impulses to the heart (effector)

        - The effector negates the stimulus by decreasing blood pressure

    5. Positive Feedback 

strengthen/reinforce change of a controlled condition

only difference from negative: effector adds/reinforce initial change

continues until interrupted by some mechanism

birth:

        - contractions of wall of uterus force baby's head/body into cervix

        - increase stretching of the cervix

        - receptors send stretch-sensitive nerve cells in the cervix

        - nerve impulses sent to the control center

        - brain interprets and releases output (oxytocin)

        - effectors: uterus muscles contract more forcefully

        - baby's body stretches cervix more

        - Interruption: birth decreases stretching cervix; breaks feedback cycle

    6. Difference

positive systems reinforce conditions that do not occur often; negative system regulate conditions that remain stable over long periods.

   B. Homeostatic Imbalances

disorder: any abnormality of structure or function

disease: illness characterized by recognizable set of signs and symptoms

local disease: affects 1 part or limited region of the body

systemic disease: affects entire body or several parts of it

symptoms: subjective changes in body functions not externally apparent

signs: objective changes that are observable; rash, swelling

    3. Epidemiology: science that deals with why, when and where diseases occur and how they're passed between people in a community

    4. Pharmacology: science that deals with effects abd use of drugs in treatment

    5. Diagnosis of Disease

science and skill of distinguishing one disorder/disease from another

medical history: collecting information about events related to a patient's illness.

physical examination: orderly evaluation of the body and its functions.

V. Anatomical Terminology

   A. Body Positions

anatomical position

when any region or part of the body assume a specific stance

body is upright

    2. prone: body is lying face down

    3. supine: body is lying face up

   B. Regional Names

Head:

skull: encloses andprotects the brain

face: front portion of head including eyes, nose, mouth, forehead, cheeks and chin

    2. neck: supports head and attaches it to the trunk

    3. trunk: chest, abdomen and pelvis

    4. upper limb: attaches to the trunk; shoulder, armpit, arm, forearm, wrist, hand

    5. lower limb: attaches to trunk, buttock, thigh, leg, ankle, and foot.

       * groin: area marked by a crease on each side, where trunk attaches to thighs.

   C. Directional Terms

words that describe the position of one body part relative to another.

superior (cephalic or cranial): toward the head or upper part of a structure.

Inferior (caudal): away from head, lower part of structure.

Anterior (ventral): nearer to or at the front of the body.

Posterior (dorsal): nearer to or at the back of the body.

Medial: nearer to midline.

Lateral: farther from midline.

Intermediate: between two structures.

Ipsilateral: on the same side of the body as another structure. 

Contralateral: opposite side of the body from another structure.

Proximal: nearer to the attachment of a limb to trunk; nearer to origination of structure.

Distal: farther from attachment of limb to trunk

Superficial: toward or on the surface of the body

Deep: Away from surface of the body

   D. Planes and Sections

Planes: imaginary flat surfaces that pass through the body parts

sagittal plane: vertical plane that divides the body/organ into right/left sides

misagittal/median plane: when the body/organ is divided into equal right/left sides

parasagittal plane: when body/organ divided into unequal right/left sides

frontal/coronal plane: divides body into anterior (front) and posterior (back). 

transverse plane: divides body into superior (upper) and inferior (lower)

        - can be known as cross-sectional or horizontal plane

oblique plane: passes through body/organ at an angle between transverse and sagittal or frontal plane

section: 1 flat surface of a 30 structure or a cut along a plane

   E. Body Cavities

Body Cavities: spaces within body that help protect, separate and support internal organs. Bones, muscles, ligaments and other structures also help.

cranial cavity: formed by cranial bones. Contains brain.

vertebral (spinal) cavity: formed by vertebral column. contains spinal cord.

        - 3 layers of protective tissue line cranial and vertebral cavities called meninges.

thoracic cavity: chest, formed by ribs, chest muscles, sternum, and thoracic part of the vertebral column.

        - pericardial cavity: fluid-filled space surrounding the heart

        - pleural cavities: two located inside thoracic c. Each contain lung and a small amount of fluid

        - mediastinum: central part of thoracic cavity between lungs; from sternum to vertebral column and from neck to the diaphragm. Contains all organs but the lungs.

            * diaphragm: dome shaped muscle that separates thoracic cavity from  -             abdominopelvic cavity.

abdominopelvic cavity: extends from diaphragm to groin and encircled by abdominal wall and bones and pelvic muscles. divided into two portions.

        - abdominal cavity: superior part containing stomach, spleen, liver, gall      -        bladder and intestine.

        - pelvic cavity: inferior part, contains urinary bladder, parts of large              -         intestine and internal organs of the reproductive system.

        - viscera: organs located inside thoracic and abdominopelvic cavity.

    2. Thoracic and Abdominal Cavity Membranes

Serous Membrane: thin, slippery double layered membrane covering the viscera within thoracic and abdominal cavities and lines the walls of thorax and abdomen.

        - parietal layer: lines walls of cavities.

        - visceral layer: covers and adheres to the viscera within the cavities.

        - serous fluid: between layers to reduce friction allowing viscera to slide - -         around.

        - pleura: serous membrane of pleural cavities

           * visceral: clings to the surface of the lungs.

           * parietal: anterior part. lines chest wall covering superior surface of      -             the diaphragm.

        - pericardium: serous membrane of pericardial cavity. 

           * visceral: covers surface of the heart.

           * parietal: lines chest wall. Between these layers is pericardial cavity.

        - peritoneum: serous membrane of abdominal cavity.

           * visceral: covers abdominal viscera.

           * parietal: lines abdominal wall; covers inferior diaphragm. Between      -             parietal cavity. 

           * most abdominal organs located in peritoneal cavity.

        - retroperitoneal: located between parietal peritoneum posterior              -         abdominal wall; ie. pancreas, kidneys, duodenum of small intestine.

        - Other Cavities

           * oral (tongue and teeth)

           * nasal (nose)

           * orbital (eyeballs)

           * middle ear (small bones)

           * synovial (freely movable joints with synovial fluid)

   F. Abdominopelvic Regions and Quadrants

Abdominopelvic Regions: two horizontal and teo vvertical lines; tic-tac-toe pattern

subcostal line: top horizontal line; inferior to rib cage, across the inferior stomach

transtubercular line: bottom horizontal; inferior to tops of hip bones

left/right midclavicular lines: vertical lines. thorugh mid-points of clavicles, medical to nipples.

nine regions: [of the tic tac toe] right-hypochondriac, epigastric, left hypochondriac, right lumbar, umbilical, left lumbar, right invuinal (iliac) hypogastric (pubic), left inguinal (iliac)

quadrants: vertical and horizontal line passed through the umilicus (belly button)

        - right upper, right lower, left upper, left lower

    2. Uses

Regions used for anatomical studies

quadrants used for describing site of abdominopelvic pain, tumor abnormality

   G. Medical Imaging

allow visualization of structures inside our body and helps for diagnosis of anatomical and physiological disorders.

Radiography

X rays pass through body producing image of interior structures.

Mammogram, bone desmiometry, angiography (blood vessels), urinary system (intravenous), gastrointestinal tract (barium contrast)

necessary to use contrast medium to make hollow/fluid filled structures visible

    2. Magnetic Resonance Imaging (MRI)

exposure to high energy magnetic field causing protons in fluids to arrange themselves in the field

fine details for soft tissue, not for bone

detects tumors, artery-clogging fatty plaques, reveal brain abnormalities, etc.

Relatively safe, can't be used on patients with metal in their bodies. 

    3. Computed Tomography (CT)

X-ray traces an arc at multiple angles around a section

soft tissues and organs with much more detail than conventional radiographs.

Differing tissue densities show up as various shades of gray. 

Screening for lung cancers, coronary artery disease and kidney cancers

    4. Ultrasound Scanning

High-frequency sound waves produced by a handheld device reflect off body tissues and are detected by the same instrument. Image is called a sonogram.

Safe, noninvasive, painless and uses no dyes. Used to visualize the fetus during pregnancy.

Doppler Ultrasound: observe the size, location and actions of organs and blood flow through blood vessels.

    5. Positron Emission Tomography (PET)

Substance emitting positrons (positively charged particles) injected into the body where it's absorbed by tissues.

Collision of positrons with electrons produces gamma rays. Computer receiving signals constructs a PET image.

Darker colors signal minimal activity, lighter colors are greater activity

Used to study the physiology of body structures such as metabolism in the heart or brain.

    6. Radionuclide Scanning:

Radionuclide (radioactive substance) is introduced intravenously into the body and carried by blood to desired tissue

Gamma rays emitted by the radionuclide detected by the computer where an image is constructed.

Areas of intense color take up a lot of the raidonuclide and represent high activity

Single Photo Emission Computerized Tomography Scanning (SPECT): specialized type scanning useful for studying the brain, heart, lungs and liver.

Used to study the activity of a tissue or organ

    7. Endoscopy

visual examination of the inside of body organs or cavities using a lighted instrument with lenses called an endoscope.

Colonscopy, laparoscopy, arthroscopy. Colonoscopy is used to examine the interior of the colon (part of the large intestine) .

Laparascopy: used to examine the organs within the abdominopelvic cavity.

Arthroscopy: used to examine the interior of a joint, usually the knee.