Bio - Physiology Exam 1 Terms

physiology

how the body works to sustain life

structure-function

things in your body are shaped a certain way because of what they do

homeostasis

your body keeping conditions of internal environment stable

pathophysiology

what occurs when normal body processes break (sickness, injury, diseases, aging, cancer) → failed homeostasis

nervous system

fast electrical signals → movement, sensation, memory, thinking

endocrine system

slow chemical signals (hormones) → growth, metabolism, reproduction

respiratory system

brings in O2, removes CO2, helps controls blood PH

digestive system

break food → nutrients → sends to blood

circulatory system

blood transports O2, CO2, nutrients, hormones, waste

urinary system

filters blood → removes waste → controls water + electrolytes

immune system

defends against bacteria, viruses, and cancer cells

muscular + skeletal system

movement, posture, protection, calcium storage

integumentary system (skin)

barrier, temperature regulation, sweat

reproductive system

production of sperm/eggs → create a new human

Level of Organization

atoms (tiny particles - C,H,O,N)

→ molecules (water, glucose protein)

→ cells (smallest living units)

→ tissues (groups of similar cells)

→ organs (heart, lung, kidney)

→ body systems (groups of organs = function)

→ total body

(AMCTOBT)

purpose of cells

create energy, remove waste, respond to signals, reproduce, move materials, control exchange with the environment

primary tissue types

epithelial, connective, muscle, nerve

epithelial tissue

covers the surfaces, lines organs, forms glands functions: absorption, secretion, protection

• structural types: simple (single), stratified (multiple)

• types: squamous (flat), cuboidal (cube-like), columnar (column-like)

• glands: exocrine + ducts (OUTSIDE), endocrine + no ducts (INSIDE)

connective tissue

supports and binds → includes blood, bone, adipose (fat), cartilage

• an extracellular matrix with embedded cells = collagen fibers which are resistant to stretch

muscle tissue

contracts (shortens as its excited) → creates movement

• types: skeletal (voluntary), cardiac (involuntary), smooth (involuntary)

• characteristics:

• skeletal → large, striated (striped)

• cardiac → branched, striated (striped)

• smooth → tapered, NOT striated

nervous tissue

sends electrical signals → communication

• cell types:

• neurons/nerve cells → generate and conduct electrical impulses with action potentials

• glial cells (gila) → structure and function support neurons

negative feedback loop

when a variable moves away from the setpoint, your body pushes it back (the “fix it” loop)

ex: body temperature, blood pressure, blood glucose, CO2 levels, hormone levels

• components:

• sensors (receptors) → detects changes

• integrating center (control center)

• effector → makes correction

positive feedback loop

makes a process stronger until it’s finished (the “AMPLIFY it” loop)

ex: childbirth (cervical stretch → oxytocin → concentrations → more stretch → more oxytocin → cycle stops when the baby is delivered

feedforward

your body predicts a change before it happens (involuntary)

ex: bracing before lift, preparing muscles before jumping, sweating due to being nervous

setpoint of body temperature

37°C

temperature level that is considered dangerous, convulsions, death

41–43°C

intracellular fluid (ICF)

inside cells

• 28 L, 2/3 of total body water

extracellular fluid (ECF)

outside cells

• plasma (in blood) → 3 L, 20% of ECF

• interstitial fluid (between cells) → 11L, 80% of ECF

phase 1 trial

toxicity and metabolism tested in healthy human volunteers

(if effective and safe, clinical trials performed)

phase 2 trial

effectiveness and toxicity tested in target population

phase 3 trial

widespread test of a drug in diverse populations (ethinicity)

phase 4 trial

drug is tested for other uses

(ex: Viagra)

organic molecules

carbon-based molecules that make up life (ANYTHING WITH CARBON)

• special as they form strong covalent bonds and make chains, rings, and complex shapes

covalent bonds

formed by sharing electrons between 2 or more atoms → STRONGEST + STABLE

• “carbon forms stable covalent bonds with itself”

ionic bonds

electrostatic attraction between oppositely charged ions, occurs when 1 atom transfers an electron to another atom resulting in IONs

• weaker in water

• Na⁺ → becomes excessively positive charged, LOSES 1 electron

• Cl⁻ → becomes negatively charged, MANY electrons, based on atomic number

• 
  

• “lons interact weakly, easily dissociate in water”

hydrogen bonds

weakest association between an electronegative acceptor atom and a hydrogen covalently bonded to another atom

• attraction between partial charges

• holds DNA strands together

• give water surface tension

• positively charged (H+)

• negatively charged (OH-)

“hydrogrn bonds stabilize proteins & DNA”

hydrophilic

molecules that form spheres are soluble in water (dissolve in water)

hydrophobic

those which do not dissolve in water

polar covalent bond

unequal sharing of electrons between dissimilar atoms

• 1 atom has stronger attraction to electrons, and accumulates negative charge (FAVORS)

• ex: H2O

non-polar covalent bond

equal sharing of electrons between similar atoms

• neither atom accumulates a partial charge

• ex: O2 and hydrocarbon

hydrocarbon

carbon (covalent) + hydrocarbons

• can be straight chains

• can be rings

• double bonds create kinks

• non-polar + hydrophobic

pre-mRNA

synthesized by DNA and must be modified by introns being spelled out (CUT OUT - to stay in the nucleus)

mRNA - messenger RNA

carries DNAs genetic coding

tRNA - transfer RNA

carries amino acid and anticodon to the ribosome (where mRNA is waiting)

rRNA - ribosome RNA

component of the ribosome that helps make peptide bonds between amino acids

functional groups

“special attachments” that change how molecules behave

• adding these makes molecules polar, reactive, and able to FORM hydrogen bonds

—OH or HO— (hydroxyl)

alcohol

PO₃^2- (phosphate)

organic phosphates

NH₂ (amino)

amines

—SH (sulfhydryl)

thiol

carbohydrates

they are polar, hydrophilic, and dissolve in water

carbs = sugar

monosaccharides

triose → glyceraldehyde

pentose → ribose, deoxyribose

hexose → glucose, fructose, galactose

disaccharides

lactose = glucose + galactose

maltose = glucose + glucose

sucrose = glucose + fructose

polysaccharides

starch → plant energy

glycogen → animal energy storage

cellulose → plant structure

glucosamine → chitin

galactosamine → cartilage

amino sugars

glucosamine

galactosamines

polymers

big molecules made of repeating small units

dehydration synthesis

water comes out → monomers join → forms glycosidic linkage (carbs) → forms peptide bonds

hydrolysis

water added BACK → break polymers apart

macromolecules

M=most large organic molecules called polymers are produced by the linking of smaller organic molecules called monomers

saturated fats

no double bond

straight

solid in room temp

ex: BUTTER/ stearic acid

unsaturated fats

double bonds

cis double bond causes bending

liquid at room temp

ex: OIL/ oleic acid

triglycerides

glycerol + 3 fatty acids

connected by an ester linkage

used for energy storage

phospholipids

hydrophilic head

hydrophobic tails

amphipathic

form cell membrane

ketones

made from fat, can be used for energy

consequences: fasting → increased ketone body formation (ketosis) → altered blood pH (ketoacidosis) → contributes to the cause of diabetes (DEADLY)

nucleic acids

DNA, RNA, ATP, ADP, AMP

nucleotide

base + phosphate + sugar

purines (base)

A → adenine
G → guanine

• 2 rings

• “pure As Gold

pyrimidines (base)

C → cytosine
U (in RNAA) → uracil
T → thymine

• 1 ring

• “pyramids CUT”

DNA

sugar → deoxyribose

purpose → genetic information

strands → double stranded

RNA

sugar → ribose

purpose → protein synthesis

strands → single stranded

proteins

polymers of amino acids

essential

must be consumed to retrieve the amino acids

nonessential

our body can produce the amino acid (no eat)

protein structure levels

1. primary → amino acid sequence + polypeptide strand

2. secondary → alpha helices, beta sheets (hydrogen bonds)

3. tertiary → 3D folding (ionic bonds, hydrogen bonds, disulfide bridges, heme groups)

4. quaternary → multiple chains together (hemoglobin - 4 different)

• 2 or more polypeptides

codons

3 letter mRNA for amino acids

AUG

start (methionine)

conjugated proteins (quaternary)

these proteins which have some type of molecule attached to them

• glycoproteins (carbohydrates) → many in cell membranes

• lipoproteins (lipids) → plasma & cell membranes

• chromoproteins (pigment) → hemoglobin/cytochrome

metabolism

all the chemical reactions that allow our body to…

1. make ATP

2. build molecules

3. break down molecules

4. maintain homeostasis

our body gets energy from?

1. carbohydrates (glucose)

2. fats (fatty acids/ adipose)

3. proteins (amino acids)

glycolysis

occurs in the cytoplasm and splits up sugars/glucose that are to big