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scientific method
hypothesis (testable), reproducible data, quantitative measures, control & experimental groups, peer reviewed
homeostasis
maintenance of relatively stable internal environment, includes sensor, integrating center, and effector
sensor
detects deviation from set point
integrating center
controls activity (effector) based on sensor
effector
adjustments to counter change happening (feedback loop)
negative feedback
most common, response COUNTERACTS change, back towards set point (temperature, blood glucose)
positive feedback
amplifies change, output of effector increases and furthers change from set point (childbirth)
antagonistic
opposing effectors on same factor, push-pull (hot=sweat, cold=shiver)
intrinsic homeostasis
cells within an organ sense change and signal to neighboring cells, all then act accordingly
extrinsic homeostasis
cells outside an organ like endocrine or nervous system responding to stimuli or change
body hierarchy
cell → tissue → organ → organ system → organism
nervous tissue
communication, regulate/integrate
neurons
high speed, electrical
neuroglia
support neurons
epithelial
covers and lines, absorb and secrete, barrier and protection - forms exocrine glands
connective tissue
structure and support, transportation, large extracellular matrix
specialized CT - adipose
large cells (adipocytes), most of their interior covered by a droplet of triglycerides
specialized CT - cartilage
cells found in small cavities (lacunae) in matrix
stem cells
creates highly specialized tissues
totipotent
embryonic stem cells, can form into all tissue
pluripotent
embryonic stem cells, can form most tissue, not placental or supporting tissue
multipotent
adult stem cells, undifferentiated cells in some organs, maintain and repair tissue
body fluid make up
60% H2O, 40% intracellular, 20% extracellular, separated by membranes and can exchange fluid
intracellular
cytoplasm
extracellular
interstitial fluid (80%) and plasma (20%)
covalent bond
two or more atoms share pairs of valance electrons, strongest bond, polar (equal share) or non-polar (not equal sharing)
ionic bonds
one atom gives electrons to another - fills both valance shells, strong electrostatic attraction (oppositely charged atoms), can dissociate in water
hydrogen bonds
weak attraction between polar molecules, - end to + end
acidic solution
releasing H+ ions when mixed with H2O (increase H+)
alkaline (basic) solution
solutes bind to H+ molecules when mixed with H2O (decreasing H+)
blood pH
between 7.4 ± 0.5
below normal blood pH
acidosis
above normal blood pH
alkalosis
carbohydrates
hydrogen (1), oxygen (2), carbon (1)
monosaccharides
one carbon ring
disaccharides
two carbon rings (by covalent bond)
polysaccharides
polymer of glucose, glycogen, starch/fiber
triglycerides
three fatty acids, backbone of glycerol
saturated triglycerides
single covalent bond, carbon binds 2 hydrogen
unsaturated triglycerides
double covalent bond, carbon binds one hydrogen
phosolipids
glycerol molecule attached to phosphate group (3 carbons), polar and non-polar so amphipathic, lowering surface tension on water and allows hydrophilic substances to suspend in polar solvents
prostaglandins
type of fatty acid, communication molecules, pro-inflammation, ovulation, uterine contractions, produced in almost all organs
primary protein
sequence of amino acids in polypeptide chain
secondary proteins
helix shape, hydrogen bonds between peptide chains
tertiary proteins
twisting/folding of polypeptide chains, chemical reaction of side chains
quaternary proteins
bonding/interacting of multiple polypeptides
glycoproteins
protein + carb (cell membranes)
lipoproteins
protein + lipid (carrier molecule in blood)
nucleotides
five carbon sugars, phosphate group, nitrogenous base
bulk transfer
large amounts of extracellular fluid and molecule exchange
plasma membrane
separates extracellular/intracellular and regulates movement (selective mechanical barrier), phospholipid bilayer
peripheral proteins
embedded on one face of membrane (structure, transport, receptors, self markers)
integral proteins
span across membrane (structure, transport, receptors, self markers)
peroxisomes
membranous sacs, H2O2, break down fatty acids, oxidative reactions (detoxification)
lysosomes
breakdown, digestive enzymes, bacteria, old organelles, food molecules
transcription
in nucleus, DNA → RNA, promoter region → transcription factor binds = RNA polymerase and copying
translation
in cytoplasm, RNA → protein, final sequence codes, ribosomes bind to mRNA and read codons, tRNA holds complementary sequences (anticodons), rRNA is structural component of ribosomes
necrosis
pathological cell death, damages adjacent cells
apoptosis
homeostatic cell death (programed/controlled), doesn’t damage other cells
effects of pH on reactions
changes shape of protein/active site
effects of substrate concentration on reactions
more substrate = rate of reaction increase until saturation
enzyme modulation
some enzymes produced as zymogens (need to be activated) by phosphorylation or dephosphorylation
coenzymes
additional small molecules to aid reaction, derived from water soluble vitamins, H+ atoms and others between enzymes
cofactors
covalently bonded - TEMPORARY, metal ions, attach to enzyme causing shape change to allow substrate/enzyme binding
endergonic reactions
reactions that need input of energy (i.g. photosynthesis)
exergonic reactions
reactions that produce energy (i.g. break down glucose into CO2 and water to produce energy)
ATP hydrolysis is an exergonic reaction driving endergonic reactions in the body
metabolism
chemical reactions in the body maintaining homeostasis
anabolism
requires the input of energy to synthesize large molecules (synthesize and store)
catabolism
releases energy by breaking down large molecules
cori cycle
lactic acid (produced in skeletal muscle) → liver (pyruvic acid and NADH, by LDH) → back to muscle (creates new glucose)
white adipose tissue
fat stored as triglycerides
lipolysis
breakdown of triglycerides to fatty acids (can enter blood for energy) and glycerol (taken up by liver) by lipase enzyme
beta (fats) oxidation
triglycerides to acetyl COA, mitochondrial matrix, 108 ATP
brown adipose tissue
thermogenesis, uncoupling proteins - H+ across w/out concentration gradient = more ATP
ketone bodies
lipolysis rate faster used than produced via beta oxidation, liver converts fatty acids to acetyl COA then ketone bodies (into blood/plasma = more acidic)
amino acid metabolism
amino acids from diet that body can’t reproduce, can be used to make ATP, excess amino acids = carb or fat storage
transamination
taking away amine group, amino acid → keto acid
osomolarity
high to low (WATER concentration) and low to high (SOLUTE concentration), solute concentration increases = osmotic pressure increases
isotonic
no net movement, same solute concentration
hypotonic
solute in cell is higher than outside so water goes into cell (swelling)
hypertonic
solute in cell lower than outside so water moves out of cell (shrink)
osomoreceptors
hypothalamus detects increase in osmolarity (solute concentration)
i.g. dehydration so thirst or ADH (less output in urine)
transcellular (epithelial)
across cell itself, cytoplasm
paracellular
between epithelial cells
tight junctions
seal between adjacent cells, limit passage
desmosomes
patches holding two cells together, intermediate filaments, resistant to stretch
adherins
“glued” together by special proteins, cadherin, i.g. heart muscle cells held together
just K+
-94 mv, equilibrium
just Na+
+60 mv
resting membrane potential
-70 mv, neurons and muscle tissue is highly excitable (rapid change in membrane potential)
gap junctions
adjacent cells passing ions and regulatory molecules through channels
paracrine signaling (local)
cells in organs secrete molecules that diffuses through extracellular matrix to target tissue/cell
autocrine signaling
cell acts on itself as target
synaptic signaling
neurons regulate/stimulate target cells through synapse (gap), releasing neurotransmitters
endocrine signaling
hormones enter blood to target receptors
second messengers
target cells with receptor proteins that binds to signaling molecules
G-proteins
alpha, beta, gamma - alpha subunit disassociates when signal molecule binds to receptor and travels to effector protein (enzyme or ion channel), GDP is released and hydrolyzed by alpha (alpha then moves back to beta and gamma)
cAMP
g-protein couple to enzyme, g-protein process but when binding to enzyme activates second messenger/response inside cell/adjacent cells, then open/close ion channel occurs