BSC 215 Exam 1 Study Guide
BSC 215 Exam 1 Study Guide BSC 215
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This 22 page Study Guide was uploaded by Jordana Baraad on Sunday September 18, 2016. The Study Guide belongs to BSC 215 at University of Alabama - Tuscaloosa taught by Dr. Jason Pienaar in Fall 2016. Since its upload, it has received 124 views. For similar materials see Human Anatomy & Physiology I in Biological Sciences at University of Alabama - Tuscaloosa.
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Date Created: 09/18/16
*** BSC 215 Exam 1 Study Guide SQ3R method of studying: survey, question, read, recite, review Learning styles Visual / Verbal: learns best when words in written language format Visual / nonverbal: learns best when info in pic/ design format Auditory / Verbal: learns best when info presented in oral language format (i.e. lecture/ discussion) Tactile / Kinesthetic: learns best in “hands on” environment (also helped by working in groups) characteristics of life 1. Homeostasis: creation and maintenance of a relatively stable internal environment to facilitate the numerous physiological processes that cells undergo 2. Organization Truism: if something is alive, has cells Truism: if something is alive, has organization ex. biomolecules cells tissues organs 3. Metabolism anabolism + catabolism = metabolism Breakdown + synthesis Essential property of cells Reason why viruses not considered alive Generally do not have metabolisms Parasitic, use host metabolism; can’t exist isolation 4. Growth maturation; increased size 5. Adaptation Response to stimuli Reproduction DNA evolves; Structure always evolving toward desired function 6. Responds to stimuli: Humans complex—language v. bacteria move toward sugar 7. Reproduction For something to be determined alive, must rep ALL 7 CHAR Ex. viruses reproduce but don’t metabolize—not alive! histology: study of tissues anatomy: study of body structures and internal workings physiology: study of body’s structures, as they relate to function anatomical position: body is upright, directly facing the observer, feet flat and directed forward. The upper limbs are at the body's sides with the palms facing forward anatomical directions anterior: toward front posterior: toward back superior: toward head inferior: toward tail proximal: closer to point of origin (typ to the trunk) distal: farther from the point of origin medial: closer to the midline of the part of a body part; on the inner side lateral: farther away from midline of the body; on the outer side superficial: closer to the surface deep: farther below the surface feedback loops—BOTH positive and negative required to maintain homeostasis positive: Increase / reinforce initial stimulus on regulated variable in same direction of initial stimulus embedded w/n neg feedback loop to maintain homeostasis ex. platelets recruiting more platelets to cite of injury negative: Return regulated variables to within “normal” range of values in opposite direction of initial stimulus ex. maintaining body temperature when enviro temp changes stimulus: event that triggers physiological response/ feedback loop oftentimes, in physio, the regulated variable receptor: measure regulated variable; sends signal to control center control center: receives stimulus; makes decision to activate response oftentimes, the brain effector: puts into effect response indicated by control center direct response to stimulus unusual ex. platelets act as both control center and effector cell signaling: chemical autocrine: closerange; signals to self juxtacrine: closerange; cell produces messenger to adjacent (touching) cell paracrine: semilong distance; Chem messenger travels across ECM (not touching; but not separarated by bloodstream) until finds cell w/ receptor BOTH messenger and receptor necessary endocrine: longdistance signaling; released into bloodstream electrical within nervous system (along neurons only; chemical btwn them) biological hierarchy (smallest to largest) chemical level/ biomolecules cells tissues organs organ systems organisms variables: factor liable to change; physiological variables affect cell chemistry regulated variables: can be affected by physio mechanism(s) Temperature pH blood glucose concentration rate dissolved O2/ CO2 in blood unregulated variables: environmentally determined solely ex. Vit D synth—dep on how much time spent in sun gradients: increase/ decrease in magnitude of property; passively move high low temperature heat dissipates from its source pressure gas and liq molecules diffuse to lower conc. areas regulated by Brownian motion concentration particles move from areas with high to low concentration 2. subatomic particles: proton: pos charge loc in nucleus determines element’s ID, know proton # of H, O, N, C neutron: neutral charge loc in nucleus electron: neg charge loc in orbitals; valence (outermost) electrons responsible for reactivity how many electrons can shell hold? n she l holds 2(n ) electrons octet rule: need 8 valence electrons in valence (outer) shell to be stable ALL chem bonding (or lack thereof) to satisfy this rule duet rule: modification—need 2 val electrons in smaller atoms (H, He) atomic categorization atomic #: # protons atomic mass: # protons + # neutrons –whole number decimal on periodic table is average of diff isotypes—called atomic weight isotope: diff forms of same element (same # protons, varying # neutrons) radioactive isotopes decay physical v. biological half life physical: how long til ½ remains (ex. carbondating) biological: how long to get rid of radioactive ion depends on what it’s incorporated into low penetrance (α & β particles) high penetrance (γ rays = high energy photons) can mutate genes metabolism = sum anabolic (building rxns) + catabolic (breakdown rxns) (endergonic rxn) (exergonic rxns) types energy Chemical energy: Potential energy stored in chemical bonds (covalent bonds) When break those bonds, energy released that can do work Ex. glucose has lots potential chem energy—molecule of choice for biorxns Electrical energy: Flow of ions Discussed more with respect to nerves Mechanical energy: Energy directly transferred from one object to another Types chem rxns Reactants Products Decomposition: AB A + B o Reactants more complex/ larger than products o Nature of bonds doesn’t matter Synthesis: A + B AB o Opposite of decomp o Products larger/ more complex than reactants Exchange: AB + CD AC + BD o NO change in size/ complexity o AB/ CD have “swapped” partners Reversible: AB ⇌ A + B o ALL the above rxns are reversible o Typ faster rate in one direction reaction kinetics endergonic: Products have higher energy than reactants Need to put energy into system Exergonic reactions: Reactants have higher energy than products Get energy out of rxn Think… digestion/ breakdown to release energy so orgs can use it Endothermic: absorb heat energy Exothermic: give off heat energy enzyme: increases rxn rate by lowering activation energy not permanently altered by rxn 2 factors increasing reaction rate 1. reactants must come into physical contact with one another a. dep on phys proximity at same time b. cell mechanisms work to bring molecs in concentration @ same place/ time 2. reactants must overcome the repulsive forces of their electrons get electrons over barrier to be attracted to other nuclei make 1 and/or 2 happen thru… Concentration: higher concentration = more molecules in given space more likely to collide if more particles Temperature: more kinetic energy higher speed more collision likelihood Reactant properties: ex. state/ phase of matter increased molecular motion increased collision likelihood Ex. liquid Catalysts: “master builders/ breakers” bring molecules together or put tension on bonds (only a little excess energy req to break) active site where desired reactant molecules fit together so they can interact Law of mass action: rxn rate directly proportional to [ ] reactants Bonds Ionic: bond via transfer of electrons btwn oppositely charged molecules Charged particles via unequal number of protons & electrons Ionization by octet rule Atoms with < 4 valence electrons… give them up Cations (+) pos charge • Atoms > 3 & < 8 valence electrons… tend to gain more Anions () neg charge electrolytes: dissolve in water; conduct electricity Covalent: bond via sharing of electrons Polar: shared electrons spend unequal time around atoms polarity Side w/ more electron density more (); other side more (+) regardless of what the polar molecules are otw to ionic bonds (Hbonds—partial charge; ionic—full charge) Ex. hydrogen bonding in H2O: attractions between polar molecs O is electronegative; H’s carry partial pos charge Nonpolar: shared electrons spend equal time around all atoms STRONGEST type of bond Strength: triple covalent >> double >> single >> other type bonds Ex. CH 4 O 2(double), N 2 riple) Van der Waals: brief attractions between temporarily polar molecules sim to Hbonds and ionic bonds, but TEMPORARY Hbonding water’s unique properties: 1. Universal solvent Doesn’t dissolve everything—but most biomolecules o Ionic and polar 2. High heat of vaporization. Why sweating helps cooling the body! 3. High heat capacity. Absorb or release large amounts of heat while T changes only slightly 4. Reactivity. Participate in many chemical reactions. 5. Adhesion/cohesion. e.g, surface tension. Cohesion: sticking to self o Ex. forming a puddle o Reduced by surfactant in lungs Adhesion: sticking to other surfaces o Moving up xylem and down phloem in plants pH scale: 1 (most acidic / highest [H+]) – 14 (most basic / highest [OH]) Logarithmic (e.g. pH 2 is 100x more acidic than pH 4) 42 = 2 ; 10 = 100fold increase Measure of the concentration of hydrogen ions • pH= log[H+] • ex. pH = 7 [H+] = 1 x 10 M7 • –KNOW HOW TO CALCULATE THIS & BYO CALCULATOR Water breaks into H+ and OH ions Neutralization rxn: Acid + Base salt + water • acids: release H+ ions increasing [H+] of the solution • bases: accept H+ ions decreasing [H+] of the solution • salts: when acids and bases mix • contain cations (+)other than H+ and anions () other than OH ex. NaCl, KCl, etc. buffers: act as acid or base to stabilize pH when pH drops, binds H+ to make solution more basic when pH rises, releases H+ to make solution more acidic 4 biomolecules polymer: carbohydrates (polysaccharides) compostion: (CH O)2n – KNOW THE 1:2:1 C:H:O RATIO (if given 1, predict other 2) polysaccharides linked by glycosidic bonds monomer: monosaccharides common monosaccharides: glucose, fructose, galactose polymer: lipids nd Fatty acid: Energy molecules (2 best) & building blocks for polymers Potential energy stored in covalent bonds Steroid Storage: Cholesterol, testosterone, estrogen Help muscle growth Promote membrane rigidity Triglyceride: Storage of fatty acid, building block of phospholipids Equivalent of glycogen for lipids Phospholipid: Major cell membrane component Take one fatty acid (FA) away from glycerol Amphiphilic Phosphate: hydrophic; charged—outsidefacing heads Lipid: hydrophobic; uncharged—inward facing tails monomer: fatty acids ~(1C:2H)n:2O = eg (C H C15H31 same components of carbohydrate, different ratio polymer: nucleic acids (DNA (deoxyribonucleic acids) & RNA (ribonucleic acids)) Contain C, H, O, N, P (sim to proteins; diff ratio) DNA missing –OH on 2’ Carbon RNA has high energy bond on 2’ carbon—can act as enzyme Held together by peptide bonds monomer: nucleotides (ATP, GTP, CTP, TTP (DNA only), UTP (RNA only)) 3 basic components 1. Ribose sugar (deoxy or oxy sugar) 2. 1 of 4 diff nitrogenous bases (covalently linked to 1’ Carbon) (Adenine A, Cytosine C, Guanine G, Thymine T/ Uracil U) purines: large, 2 rings, A/G pyrimidines: small, 1 ring, C/U/T 3. triphosphate group (XTP) polymer: proteins Each level dictates higher order structure 4 levels protein structure Primary: Sequence of amino acids Secondary: Amino acid chains arranged in α helices or β sheets (hydrogen bonds) Tertiary: Folding into fibrous or globular shapes (Hydrophobic interactions, disulfide bridges & VdW force) Quaternary: 2+ polypeptide chains (Hydrophobic interactions & ionic bonds) monomer: amino acids KNOW general structure: central carbon, amino group (NH ), car2oxylic acid OOH), R group(radical) group = placeholder for 1 of 20 side chains Side chains versatility of proteins —don’t need to know all 20 3. Cell theory—3 tenets 1. All living organisms are composed of cells 2. The cell is the most basic unit of life everything above cell level is life; everything below is not cellular processes 3. All cells come from preexisting cells Cell theory contributors Robert Hook 1 tenet of life/ cell theory: all living things have cells Anton Van Leeuwenhoek Discovered bacteria Louis Pasteur Spontaneous generation of life nd 2 tenet of life: all life comes fr life; all cells come from cells cell components plasma membrane – Surrounds cell, defines boundaries – Made of proteins and lipids – Selectively permeable phospholipid bilayer membrane proteins integral (hydrophobic segments, membranespanning) peripheral (hydrophilic; embedded in 1 side of membrane) cytosol + organelles/ cytoskeleton Ribosome: protein synthesis, using mRNA and tRNA Large and small protein subunits Free in cytosol or bound to rough ER and nuclear membranes ER fixation impmRNA knows “fixed address” to go RER: protein synthesis/ transport; “rough” bc studded with ribosomes (italicized comp to SER) Protein folding Continuous w/ nuclear membrane “Membrane factory” Combines integral proteins and lipids in “prefabricated” cell membrane sections function constant despite cell type SER: lipid synthesis; detoxification (italicized comp to RER) Continuous w/ RER (and nucleus, before) Ribosomes lost along the way main job: Calcium ion storage function varies dep on cell type Calcium ion storage (e.g. muscles) Detoxification reactions (e.g. liver) Lipid synthesis (phospholipids, cholesterols) Golgi apparatus: protein modification/ packaging Small system of cisternae job: Synthesizes carbohydrates Adds carbohydrates to proteins from ER (glycoproteins) enclose proteins in transport vesicles lipidderived membrane fr membrane enclosing protein Mitochondrion: ATP synthesis Most ATP made btwn inner and outer membrane Folds: cristae (NOT cisternae like Golgi body) Lysosome: enzymatic brkdwn of wornout organelles and other substances entering cell (italicized comp to peroxisome) Produced by Golgi apparatus acid hydrolases to digest bacteria / worn out cell components Relatively large—breaks down larger things Peroxisome: detoxifies toxic substances Produced by RER Contains oxygen free radicals Dangerous to cell; OK in enclosed organelle Oxidizes toxic substances (like ethanol) to hydrogen peroxide Breaks down fatty acids recycles products into phospholipids Synthesizes some phospholipids Breaks down smaller things Centrosomes: organizes mitotic spindle dur cell division/ replication Cytosekeleton Microfilaments (protein: Actin) Form terminal web Extend into microvilli (support & “milking”) can pull microvilli and whatever’s attached into cell Intermediate filaments (Various proteins) Give cell shape (stiff); Purely structural role Microtubules (protein: Tubulin) Radiate from centrosomes, hold organelles in place centrosomes controlle microtubules’ movements Act as “railway tracks” for organelle movement Axonemes (motors) of cilia & flagella, mitotic spindles (special instance of microtubules) Some remodel (spindles dragging chromosomes) some don’t (axonemes for beating flagella) Cellular Extensions Microvilli: Smaller, Increase SA Find actin Cilia: bigger, more mobile Find tubulin protein microcilia for primary cilia Cell sensory function “Monitors” surrounding ring of 9 microtubule triplets (9 +0) axoneme Secondary cilia (motile cilia) Restricted to cells of respiratory tract, uterine tubes, brain ventricles, and testes Motile cilia Beat in wavespropel mucous, egg cells & cerebrospinal fluid Axoneme (in both) • 2 central, 9 peripheral microtubules (9+2 structure) • Peripheral microtubules extend as basal body into cell • Dynein arms: use ATP to crawl up adjacent microtubule arms causes bending & power stroke if no dynein, you’re in trouble req saline solution; can’t move in mucus lack of saline solution CF Flagellum (only in sperm cell) Structure almost exactly like cilia axoneme (9+2 axoneme) • Beats in an undulating motion unlike propellerlike flagellum in bacteria Pseudopodia: Cytoplasm filled extensions of cell surface Used by macrophages Constantly appearing / retracting *** Assembling / disassembling Actin protein scaffolds Directed by tubulin nucleus Nuclear envelope Double membrane (4 phospholipid layers) Inner membrane rests on intermediate filament scaffold (lamina) Nuclear pores facilitate active transport of RNA (mostly mRNA out), proteins (in) & chemical messengers (in & out) Nucleoplasm: Salts, Nutrients, Nucleotides & Enzymes nucleotides = “building blocks” Nucleolus (darker staining region) • Ribosomal factory (Ribosomal RNA (rRNA)) constantly need to make proteins constantly need rRNA, so constant transcription in nucleolus stains dark bc highly active • Chromatin: 30% DNA, 60% Histone protein, 10% RNA chromosomes are NOT the same thing as chromatincondensed DNA is negatively charged RNA transcribed from DNA **chromosomes only made when need to move DNA to other cellsmitosis/ meiosis Morphology: shape and size Shape variation (affects function) Skin cells—no cell wall Bacterial cells –no nucleus Nerve cells –no cell wall; axons/ dendrites as projections Egg cell large Plant cells—cell wall Size variation Egg cell (100 μm diameter) –big, not microscopic Most human cells 1015 μm diameter Some nerve cells (>1m long) PM & endomembrane syst structured to increase surface area to volume ratio (SA/V) higher S/V ratio ideal bc lots rxns happen on surface want smaller size (diameter) smaller vol rel to SA low SA/ V ratio cannot sustain chemistry endosymbiant theory: ribosomes and mitochondria were initially freeliving microorganisms that were symbiotically endocytosized long ago evidence: 1. Outer membrane has lipids sim to eurkaryotes Inner membrane has lipids sim to bacteria Tells us that ancient endocytosis Inner = orig; Outer = remnant of vesicle 2. Mitochondrial DNAremnants of bacterial genome 3. mitochondrial ribosomes 4. in genetic sequencing—don’t need to know Much more like bact cell transport Passive: substances cross the membrane without the cell expending any energy Down concentration energy via kinetic energy of random motion • Less particles to bump into at lower concentration, travel further • Cell membrane’s selective permeability based on: • Size: lipid soluble but can’t fit btwn molecules • Charge: small enough, but charge repels • Membrane protein specificity Diffusion Simple: unassisted net movement of particles down concentration gradient Facilitated: channel protein assist above process Filtration: substances thru semipermeable membrane via hydrostatic pressure osmosis: Special type of diffusion across a selectively permeable membrane • Movement of a solvent from an area of higher water concentration (lower solute concentration) to an area of lower water concentration (higher solute concentration) Active: requires the cell to expend energy (ATP) Primary active transport: Membrane protein uses ATP energy directly to “pump” against concentration gradient Na/K pump All animal cells have them for … nerve cell signaling, Skeletal (skinetal)muscle contraction, Heartbeat, Osmotic balance Antiporterlike activity—but actually primary transport **MANTRA: 2 K’s into, 3 Na’s leave Secondary active transport: Membrane protein uses concentration gradient energy created by a different ATP dependent “pump” Uniport: moves one substance one way Cotransport: Symport: 2 substances in same direction ex. w/ glucose Antiport: 2 substances in opposite direction • Vesicular transport: Membrane vesicles bud off membrane to transport molecules wholesale 4. Nucleus and genetics 2 arms of identical DNA sequence (sister chromatids) • Result of DNA replication • Chromatids joined at centromere • Each chromatid has a kinetochore at the centromere (on either side) kinetochores interact w/ microtubules; Pt of attachment for microtubules microtubules pull chromatids apart Human Karyotype: quickest way to look at genome—partic abnormalities **23 pairs 46 chromosomes (only nonpair = sex chromosomes: X/Y) i.e. trisomy 21 Down’s syndrome (extra copy of chrom 21) banding patterns: dark patches = condensed DNA, not being transcribed light patches = looser DNA, highly active, so must always be transcribed Each nt has 3 basic components Ribose sugar (deoxy or oxy sugar) 1 of 4 diff bases (Adenine, Cytosine, Guanine, Thymine/ Uracil) oxygen on 2’ carbon is more imp distinction btwn DNA/ RNA than T/U purines: large, 2 rings, A/G pyrimidines: small, 1 ring, C/U/T Nitrogenous base (covalently linked to 1’ Carbon) 3’ carbon results in polarity of sugar 5’ carbon participates on phosphodiester bond process = dehydration synthesis Rules of genetics 1. purine on one side of DNA, means always linked to pyrimidine on other side 2. GC3 rule a. Guanine (purine) forms 3 Hbonds w/ Cytosine (pyrimidine) b. Adenine forms 2 Hbonds w/ thymine (AT2) Hbond baseparing rules 5’3’ rules antiparallel rules If given… 3’AGCTTTCG5’ Need to grow in 5’ 3’ direction Put down at left (true for DNA or RNA) 5’TCGAAAGC3’ *OR* 1 base = U for RNA Look at #bonds btwn bases to det G/C v. A/T Then look at ring structure to figure out which in bond is purine/ pyrimidine Cellular DNA long polymers of nucleotides connected by phosphodiester bonds Each polymer assoc w/ a partner based on specific hbonding patterns in an antiparallel orientation 1 Purine :1 Pyrimidine G ≡C A = T DNA occurs as a double helix in cells • 2 strands twist around each other held by phosphodiester bonds • Most thermodynamically stable conformation Mutation happens mostly dur replicaion Central dogma of molecular biology: Watson’s model DNA RNA protein Stored in nt’s transcription stored in nt’s translation Proteins are NOT genetic material—can’t pass it on DNA Replication DNA polymerase can only add nt’s when hydroxyl group hanging off 3’ end True for DNA RNA polymerase can put down nt on template; doesn’t need existing –OH on 3’ end Always start w/ RNA primer to provide hydroxyl group for DNA Polymerase Both DNA and RNA can only grow 5’ 3’ end Each individual nt has 5’ and 3’ end Last one will have 5’ end free; 1 one will have 3’ end free DNA opened at A/T seq, not C/G, bc 3 Hbonds stronger than 2 (2 in A/T) Steps in writing nt sequence; describing replication 1. Form and open replication bubble a. write polarity: typ 5’ on top left (where phosphate hangs off) 3’ on top right (where –OH hangs) b. rule of antiparallel strands (true for DNADNA or DNARNA coming together 2. RNA polymerase puts down 3’ –OH that DNA polymerase can use a. RNA polym responsible for first phosphodiester bond b. DNA polymerase “cements” it 3. 2 template strands of replication—semiconservative replication a. top: top strand is from original molec; bottom strand is new (from RNA) b. bottom: bottom strand is from orig molec; top strand is new c. EACH STRAND IS 50/50 old/new 4. polymerases can only add at 3’ end a. smooth transcription on one side of bubble (leading strand) b. fragmented in opp direction (lagging strand) i. lagging strands have Okazaki fragments c. one of each, per template **KNOW ALL ENZYMES AND STEPS FOR TEST!! DNA Transcription Promoter (aka. TATA box): indicates where replication should start (which strand serves as template) *** Recognized by RNA polymerase RNA polymerase: protein catalyzes DNA replication Acts slightly downstream from promoter Lays down complementary nt’s –antiparallel Until reaches termination sequence Termination sequence on opp strand to promoter DNA opening continues L R Once DNA Polymerase “fixes” nt’s, mRNA falls of template DNA closes behind it; meanwhile, other side of bubble keeps opening • Many different types of RNA • Usually single stranded sometimes folds back on itself to form partial double strands (complimentary base paring) forms stemloop structure of tRNA • Messenger RNA (mRNA) carries genetic information between nucleus and ribosomes stays long string of instruction; no folding • Ribosomal RNA (rRNA) component of ribosomes, enzymatic and mRNA orientation activity made in nucleolus—reason for dark stains proteins for laying down aa’s catalyzed by rRNA—enzymelike activity in sequencing • Transfer RNA (tRNA) transfers specific amino acids to specific mRNA sequences during translation one of loops in stemloop structure forms 3nt sequence called anticodon enzyme recognizes it and covalently links appropriate 1 of 20 aa’s 1:1 unique enzyme to anticodon ratio anticodon responsible for recognizing codons • MicroRNAs gene regulatory & defense functions don’t need to know DNA Translation codon table refers to triplet codons on mRNA **will be given this table on exam—KNOW how to use; DON’T memorize don’t need to know about degeneracy KNOW 3 letter code to predict, NOT what 3 letter code means in full First aa in seq is Met: start codon AUG First step find 5’ end; 2 step find AUG Count in 3’s from there On ribosome, 3 sites E: Ejection siteWhere tRNA’s that have been used are ejected P: peptide site Contains growing aa chain at any given time A: amino siteWhere tRNA comes in w/ aa every time mRNA and tRNA pulled thru ribosome process continues until reaches 1 of 3 stop codons (UAA, UAG, UGA) no tRNA recognizes it; stops translation 5. histology 4 basic types of tissues: –Epithelial –Connective – Muscular – Nervous All have 2 main components: 1. Cells (unique to tissue type) 2. Extracellular matrix (ECM) (contains ground substance) Epithelial tissues structure – Supported by connective tissue beneath the basement membrane – Avascular: no blood supply – Regeneration – a lot of friction, need to regenerate if well nourished Function: cover and line surfaces Protection, absorption, filtration, excretion, secretion Classification – By thickness – Simple: One layer of cells attached to basement membrane – Stratified: 2+ layers of cells – By shape – Squamous – Flat and scalelike – Cuboidal – Cube shaped or squared – Columnar – Column shaped and tall Structure/ function/ location (only need to know one per CT type) Structure Function Location Simple squamous elliptically shaped cells filtration and diffusion Kidneys—Bowman’s with flattened nuclei capsules, glomerulus Lungs—alveoli Circulatory system— endothelium Simple cuboidal Cubeshaped protection (against Excretory ducts Large, central nucleus abrasion, foreign Misc. organs/ glands particles, bacteria, and Kidneys—tubules excessive water loss); Ovarian surface absorption; transport Lungsbronchioles Simple columnar Cells longer than wide Absorption, protection Most prolific cells in the Large, circular nucleus, constant regeneration body oriented closer to basement membrane, Digestive tract, female sometimes innervated reproductive organs, nasal passage. Stratified squamous Flat, compact, scalylike Protection against Epidermis, esophagus cells. mechanical and physical Can be keratinized or damage, chemical nonkeratinized. damage in the esophagus Stratified cuboidal or Commonly twolayered Protection; secretion Rare columnar (but can be Linings of large ducts multilayered) (salivary, mammary, Circular nuclei that sweat glands) appear stacked. Transitional Stretchy Distension to allow for Walls of ureter, bladder, Constriction dome water filling cavity urethra shape Stretching flat shape Pseudostratified Typ covered in cilia Secretion, absorption, Trachea, vas deferens 1 row of misaligned movement (thru ciliary and epididymis, cells action) endometrium in females can tell it’s not multiple rows bc all touch basement membrane Connective tissue Function • Protects, supports, and binds together other tissues of the body, i.e. bone, cartilage, etc. Structure • With the exception of cartilage, connective tissue is highly vascularized • Typically have few cells extensive nonliving material (matrix) between cells of connective tissue 3 main components o 1) Elastic and/or collagenous fibers (3 main types) 1. Collagen fibers provides tensile strength 2. Elastic fibers gives tissues distensible properties (stretch, compress) 3. Reticular fibers Network for support o 2) Ground substance (gellike substance with extracellular matrix) o 3) Cells (specific to cell type Classification • Connective tissue proper o Widely distributed throughout body o fibroblasts secrete ECM o many fiber types (collagen, elastic, reticular) o Highly vascularized o 4 subtypes – Loose (areolar) – Structure: – Cell type: fibroblasts – Fiber type: – thinelastic fibers – thicker collagen fibers Primarily ground substance. – Location: (most widespread) walls of hollow organs Surrounds blood vessels, nerves, and muscles Part of lamina of digestive and respiratory tract – Dense – Regular CT – Structure: – Fiber type: Primarily parallel collagen fibers – Thin nuclei run along fibers – Good for Resisting unidirectional stress – Function: Resists tension and pulling from a single direction – Location: Tendons and ligaments – Dense Irregular CT: – Structure: – Fiber type: collagen (closely packed) – Randomly arranged – Resist stress from every direction Location: Deep layer of thick skin (dermis), around joints, submucosa of digestive tract – Reticular Structure: Cell type: fibroblast Fiber type: reticular fiber (type III collagen) Function: gives support to soft organs – Location: Spleen, lymph nodes, bone, liver – Adipose – Cell type: Adipocytes consisting of fat (lipid) droplets – Nuclei at point of adipocytes – Location: Deep to the skin; surrounding heart and abdominal organs – Adaptation: consist of primarily adipocytes • Cartilage o Tough, flexible tissue resistant to tension, twisting and compressive forces o Cell type: Chondrocytes; housed in in lacunae o Avascular • 3 subtypes 1. Hyaline structure: fiber type: collagen (Large amount) Cell type: chondrocytes; found with the lacunae of ECM Chondrocytes are often found in pairs, location: Tissues in the ear, nose, trachea, larynx, and small respiratory tubules Synovial joints. Rib connection to sternum 2. Fibrocartilage structure: fiber type: collagen (spongier) cell type: chondrocytes; found in lacunae (often aligning) function: shock absorption location: ligaments, intervertebral disks, pubic symphysis, knee disks 3. Elastic Cartilage structure: fiber type: elastic (tightly packed) cell type: chondrocytes embedded in ground substance function: great dispensability/ flexibility to withstand bending location: Pinna (outer ear) and epiglottis • Bone o structure: o Hard calcified matrix o many collagen fibers o rocklike o very vascularized o cell type: osteocytes; lie in lacunae o Location: bones throughout body (obviously) o function: Supports and protects, calcium storage, rbc / wbc formation, mech movement • Blood o structure: o cell type: Red blood cells (erythrocytes) & white blood cells (leukocytes) ECM called plasma contains platelets, fat globules, gases, proteins, and hormones Red blood cells: donutlike, smaller than WBC’s White blood cells: larger, filled in o Function: Transport of respiratory gases, nutrients, waste, and other substances; immune response Clicker Question Recap Groups of cells working together to form common function: D) tissue T/F All living orgs composed of 1 or more cells? True (one of simplest defs of life) Which false? C. Pos feedback loops triggered by deviation from norm range; work to decrease val of var as it increases to maintain var w/n norm range TRUE: A. Structure and funct related at ALL levels of org B. homeostasis: creation and maintenance of dynamic equilib Gradient exists when… D)all of the above a. heat conc in one area body b. given subst more conc in 1 region than other c. higher P in one place than other What kind of chemical signaling occurs at the neuromuscular junction? Chemical signaling Atom w/ atomic #8, and mass number 17? 8 protons, 9 neutrns, 8 electrons (if neutral) Which of following contains polar covalent bonds? H2O (H2 and CH4: polar covalent; NaCl: ionic) Chem energy stored in bonds is: potential energy Digestion exergonic bc chemical bonds are broken and energy is released? T/F True Enzymes bind w/ substrates at active sites and are permanently altered by binding process. T/F? False—enzymes are reusable; once product formed and release; enzymes move on unchanged Cmpd has 120 carbons, 240 hydrogens, 2 oxygens. It is most likely a… Lipid (C, H, O) NOT protein/ nucleic acid, bc no N, or carbohydrates bc no 1:2:1 ratio monomers of proteins are… d. amino acids Cell 1 has 10um width; cell 2 has 50 um width. Which cell has larger S/V ratio? A) cell 1 Which of following factors affect diffusion rates of small hydrophobic molecules? b. temperature, conc. gradient NOT ATP, bc then energy required 3 main components cell: B. plasma membrane, cytoplasm, nucleus Diff btwn active and passive transport is active uses proteins; passive doesn’t False—facilitated diffusion uses carrier proteins; is type of passive transport i. Not about protein use; about energy use Na/K pump? b. 2 K ions in for 3 Na out reason: membrane almost impermeable to Na; only way in w/ channel not part of endomembrane system b. cilia (ribosomes part of RER) Which is secondary active transport? b. glucose symporter NOT Na/K pump—has secondarytransporterlike activity (but not secondary transport) Happens to antiport, but primary transport bc transport pump directly uses ATP
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