A&P Unit 1 - homeostasis, lipids, proteins

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55 Terms

1

Anatomy

the study of form and structure of the body

-WHAT is body part

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2

Physiology

the study of how organism functions

-HOW and WHY it works

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3

Microscopic anatomy (2 subtypes)

can’t see with naked eye

-cytology = study of cells

-histology = study of tissues

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gross/macroscopic anatomy (5 subtypes)

can see with naked eye

-systemic = of each body system

-regional = focus on one area of body

-surface = only on surfaces

-comparative = compare across species

-embryology = how develops from conception to birth

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5

types of physiology (5 types)

**studying how and why these systems work

-cardiovascular

-neurophysiology

-respiratory

-reproductive

-pathophysiology (disease)

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6

6 characteristics of living things

Organization

Metabolism

Growth

Responsiveness

Reproduction

Regulation

(OMGRRR)

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-organization

complex structure and order of organism’s parts

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-metabolism

organism uses nutrients

anabolism = build nutrients, use energy

catabolism = break nutrients, release energy

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-growth & development

organism uses materials from environment to grow

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-responsiveness

organism sense & react to environment stimuli

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-reproduction

organism make new cells for growth & repair (mitosis) OR make sex cells (meiosis)

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-regulation

organism ability to maintain homeostasis

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homeostasis

maintain consistent internal environm. even with external environm. changing

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interstitial fluid

fluid that fills space btwn cells

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internal v external environment

internal = interstitial fluid → temp, pH, etc

external = outside env. of organism (ex. my dorm)

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what are the ways of internal env. regulation?

conformity = ‘cold-blooded’ organism IE matches EXE

regulation = ‘warm-blooded’ organism maintain stable IE despite change in EXE

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What factors are homeostatically regulated?

-nutrients/blood sugar → energy

-O2 & CO2 → need for respiration & pH

-concentration of waste products

-electrolyte/water balance

-pH → enzyme function

-temp → cell & enzyme function

-vol & (blood) pressure → for transportation

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18

what are the components of homeostatic systems?

  1. RECEPTOR detects changes from the STIMULUS

  2. CONTROL CENTER interprets & initiate change

→ nervous system = quicker response. endocrine = slower response

  1. EFFECTOR is structure that brings changes

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negative feedback

move toward homeostasis by minimizing impact of stimulus

Ex. shivering to stay warm in winter

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positive feedback

move away from homeostasis by amplifying stimulus

→ until climactic event occurs, then goes back to homeostasis

Ex. blood clot, childbirth, breastfeeding

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Individual response

individual organism alter own physiology in response to smth

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population/evolutionary response

change in gene pool over generations

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what are the types of individual response?

acute = short period (min-hours) change. modify existing cells

chronic = long period (days-month) change. restructure/build new parts

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acclimation

chronic response changes in one way (usually in lab w/ controlled variables)

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acclimatization

chronic response changed in many ways (happens naturally instead of in lab)

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hydrogen bond

weak bond btwn H & O in water.

can form up to 4 H bonds for 1 water molecule (2 from O and 1 each from H)

<p><u>weak</u> bond btwn H &amp; O in water.</p><p>can form up to <u>4</u> H bonds for 1 water molecule (2 from O and 1 each from H)</p>
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functions of water

-body temp regulation

-transportation

-lubricant

-spinal fluid

-solvent for hydrophilic molecules

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solvent vs solute

solvent = dissolving agent

solute = gets dissolved

forms solution

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electrolytes

-ionic compounds

-completely dissolve

-can conduct current

-salts or acid/bases

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nonelectrolytes

-polar compounds

-dissolve in water but remain intact

-can’t conduct current

-ex. glucose

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31

water surrounds ions in a _____________

hydration shell

<p>hydration shell</p>
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hydrophobic exclusion & hydrophobic interaction

when water molecules “force out” nonpolar molecules → NP molecules need a protein carrier in the body

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amphipathic

partially dissolves in water. part P and part NP

ex. phospholipid

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34

functions of lipids

-store energy

-cell membrane components

-make steroids

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35

what are the classes of lipids?

P.E.T.S.

Phospholipids

Eicosanoids

Triglycerides

Steroids

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fatty acid

chain of lipid made of C and H. nonpolar

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Triglyceride

-most common lipid

-hydrophobic, NP

-1 glycerol + 3 fatty acid tail

-created by joining glycerol via lipogenesis

<p>-most common lipid</p><p>-hydrophobic, NP</p><p>-1 glycerol + 3 fatty acid tail</p><p>-created by joining glycerol via <u>lipogenesis</u></p>
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unsaturated, saturated, polyunsaturated triglyceride

unsat = no double bonds. solid @ room temp

sat = 1 double bond. liquid @ RT

polyunsat = 2+ double bond

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Phospholipid

-cell membrane bilayer

-amphipathic

-polar phosphate group in head with 2 NP fatty acid tails

<p>-cell membrane bilayer</p><p>-amphipathic</p><p>-polar phosphate group in head with 2 NP fatty acid tails</p>
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Steroid

-nonpolar

-4 carbon ring structure

-side chains make them unique

-ex. cholesterol, estrogen, testosterone, bile salts

<p>-nonpolar</p><p>-4 carbon ring structure</p><p>-side chains make them unique</p><p>-ex. cholesterol, estrogen, testosterone, bile salts</p>
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cholesterol

-type of steroid

-plasma membrane flexibility

-precursor to other steroid synthesis

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Eicosanoids

-20 carbon chain fatty acid

-signal molecules

-inflammatory response & nervous system communicators (think back to pain response in microbio)

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classes of eicosanoids

prostaglandin

prostacyclin

thromboxane

leukotriene

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44

a protein is _______

a polymer made from monomers of amino acids

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amino acid overview

-1 amine group, 1 carboxyl group, side R chains

-20 types of amino acids

-peptide bond created by dehydration synthesis

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lengths of peptides

oligopeptide = 3-20 AAs

polypeptide = 21-199 AAs

protein = 200+ AA’s

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four types of AAs

-nonpolar

-polar

-charged

-AAs with special function

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Nonpolar AAs

-has only H-C bonds

-group with other NP AAs → hydrophobic exclusion

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polar AA’s

-R grp has more than H-C (usually O or N)

-interact with water and other polar AAs

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charged AAs

-R grp has +/- charge

-forms ionic bond btwn other charged AAs

-hydrophilic

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AAs with special function

-proline - cause bend in protein chain

-cysteine - can form disulfide bond

-methionine - MET. start marker, first AA during protein synthesis

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1° Primary Structure

sequence of AA’s

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2° Secondary Structure

H-bonds → coiling of peptide chain

-a-helix

-b-pleated sheet

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3° Tertiary Structure

3D shape of protein as it folds→ affected by H-phobic or philic interactions of peptides

-fibrous protein = skinnier and straighter. insoluble in water. structural support in body (ex. muscle)

-globular protein = like a blob. soluble in water. chemical process/metabolism (ex. enzymes)

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4° Quaternary Structure

more folding. only appears if protein is made of 2+ polypeptides

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