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Human Form & Function > Quiz 1 > Flashcards

Quiz 1 Flashcards

1
Q

Histology

A
  1. Microscopic anatomy linked to functions – cell biology, physiology, genetics, biochemistry, etc.

2.Study of tissues of the body
Structure, Arrangement,
How structure and arrangement optimize functions specific to each organ

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2
Q

whole mounts

A

entire organism/structure is placed directly onto a microscope slide;
preserves structural relationships

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3
Q

squash preparations

A

where cells are intentionally squashed/crushed onto a slide

to reveal their contents; allows counting of cell numbers and individual cell details

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4
Q

smears

A

cells suspended in a fluid=
(blood, semen, cerebro-spinal fluid);individual cells scraped, brushed or aspirated
from a surface or from within an organ (exfoliative cytology).
“Pap test”

allows counting of cell numbers and individual cell detail

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5
Q

Sections

A

slices are cut from specimens, mounted on slides, and stained
preserves structural relationships

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6
Q

Axial vs Appendicular

A

Axial – head, vertebrae, ribs, sternum

Appendicular – everything else (arms, legs)

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7
Q

Planes and directions

A

Median, sagittal (parallel to it), transverse (axial), oblique, coronal (anterior separate posterior),medial (toward median), lateral (away from median), proximal, distal, anterior (ventral), posterior (dorsal) superior (cranial or rostral ), inferior (caudal), longitudinal (parallel to long axis), horizontal, vertical, peripheral, superficial, deep, external, internal, apical, basal, frontal, basilar

A-P (anterior – posterior) can also refer to superior/inferior direction depending on context

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8
Q

Thoracic skeletal elements

A

Manubrium, body, xiphoid process [ these 3 make up the sternum] ribs (true (1-7),false (8-10) floating(11-12)) costal cartilage, vertebral body, intervertebral discs

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9
Q

Shoulder Osteology

A

Clavicle, scapula, coracoid process, superior angle, inferior angle, lateral angle, scapular spine, infraspinous fossa, medial border, supraspinous fossa, acromion

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10
Q

pelvic osteology

A 
Os Coxae (hip bone) – 3 bones, fuse to form the pelvis
Intervertebral disc, pubis, ischium, ilium, pubic symphysis, sacrum (fused vertebrae), coccyx
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11
Q

Joint types

A

Synarthroses (immovable joints) ex. suture (skull only; fibrous tissue is continuous with periosteum) or gomphoses (teeth; ligament is periodontal ligament)

Diarthroses (freely movable; all synovial)

movement at joints has limits due to bones, muscles, ligaments, other tissues

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12
Q

Muscles

A

smooth, cardiac, skeletal

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13
Q

Connective tissue around muscles

A

Connective tissue surrounds fibers, bundles, muscles, muscle groups, neurovascular bundles

Connective tissue partitions the body – implications for muscle function, infections, surgery

Endomysium (surround individual fibers), perimysium (surrounds fiber bundles, or fasiculi), epimysium (surrounds entire muscle)

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14
Q

Superficial back muscles

A

trapezius, levator scapulae, rhomboid major, rhomboid minor, latissimus dorsi; together with serratus posterior these are NOT innervated by dorsal rami, are innervated by ventral rami (part of branchial plexus) except trapezius which is done by cranial nerve

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15
Q

Trapezius

A

Innervated by spinal accessory nerve; 3 different fiber angles (different movements); elevation, inward rotation of scapula, tilts head towards and rotates head away from unilateral contraction

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16
Q

Levator Scapulae

A

innervated by dorsal scapular nerve (C5), elevates scapula; unilateral contraction- tilts neck to same side

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17
Q

Rhomboid major/minor

A

innervated by dorsal scapular nerve (C5); retracts/ adducts scapula (closer to midline/central point)

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18
Q

Latissimus dorsi

A

innervated by thoracodorsal nerve (C6-8); adduction, medial rotation of shoulder

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19
Q

Deep Back muscles (paraspinal, intrinsic, epaxial)

A

All innervated by dorsal rami of spinal nerves;

Function: postural support, extension of spine/trunk/neck, unilateral contraction (bending and some rotation)

Splenius, erector spinae, transversospinalis, suboccipital groups

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20
Q

Splenius

A

superficial deep back muscles; splenius capitus, splenius cervicis

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21
Q

Erector spinae

A

Iliocostalis, longissimus, spinalis (I Love Sluts)

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22
Q

Transversospinalis

A

semispinalis, rotatores, multifidus

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23
Q

Suboccipital

A

Under semispinalis (part of transversospinalis group) rectus capitis posterior minor, rectus capitis posterior major,[ medial] obliquus capitis inferior, obliquus capitis superior [lateral]

suboccipital nerve (C1- dorsal ramus); bilateral (extends head/neck), unilateral (rotates head to same side), EXCEPT OCSM (tilts head to same side, rotates to opposite; cute dog tilting head)

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24
Q

Shoulder muscles

A

Innervated by brachial plexus; ex. deltoid (innervated by upper and lower subscapular nerve C5-6) subscapularis (inner surface), while these are outer surface (suprascapular nerve; C4-6): infraspinatus, supraspinatus

thorax, deep back muscles (segmental body plan make innervation easy)

Arms, shoulders, superficial back (not segmented)

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25
Q

Brachial plexus

A

(C5-T1) Ventral rami, Trunks (axons mix, no longer separated by level), divisions (no nerves emerge here), cords (2 anterior [lateral and medial] and 1 posterior)

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26
Q

Dorsal Scapular Nerve

A

C5; levator scapulae, rhomboid major, rhomboid minor

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27
Q

Long thoracic nerve

A

C5-7; serratus anterior

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28
Q

Subclavius nerve

A

C5-6; subclavius muscle

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29
Q

Suprascapularis nerve

A

C4-C6; supraspinatus, infraspinatus

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30
Q

Thoracodorsal Nerve

A

C6-8 innervates latissimus dorsi

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31
Q

Upper and Lower Subscapular Nerve

A

C5-6; innervates subscapularis, teres major

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32
Q

Epithelial Tissue

A

Aggregated Polyhedral cells that are strongly attached to one another, small amount of ECM; Protective lining, glandular secretions, and transport

Primary functions:

  1. Covering, lining, and protective surfaces (ex. epidermis)
  2. Absorption (ex. intestinal lining)
  3. Secretion (ex. Parenchymal cells of the gut) from inside to outside

formation of cell sheets that coat outer surface of body (GI) and line various organ surfaces, form glands and other secretory tissues and linings, undergo mitosis and is typically avascular (relies on the diffusion from blood vessels in adjacent CT) and is a POLAR tissue (apical pole that faces lumen/space and basal pole which faces CT)

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33
Q

Connective Tissue

A

All sorts of different cell types. Some fixed, some forever voyaging. Generally quite a bit of ECM. Functions: Support and protect body structures ex. tends to attach epithelial tissues etc. Ex. blood

Cells are generally separated by ECM, generally not linked together. It is generally holding some other tissue in place and not at a free surface (outside)

Consists of cells, ECM fibers (collagen), and ECM ground substance

Derived from mesoderm (primarily), contains multipotent mesenchymal progenitor cells

Function:

  1. Mechanical/protective support of other tissues. Often found as stroma in organs, surrounds blood vessels, lymphatics, and nerves
  2. Stores interstitial fluid, water, electrolytes
  3. involved in early repair of damaged organs, if repairs not complete, can lead to permanent scar formation/ fibrosis (big injury, pump collagen in a non ordered way)
  4. contains immune system cells and presents a physical barrier so provides defense and protection
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34
Q

Muscle

A

Contractile tissue. A muscle contains CT, but muscle tissue is distinct. Has a moderate amount of ECM

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35
Q

Nervous

A

Conducts nerve impulses. Very little ECM.

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36
Q

Relationship between Epithelial and CT

A

Epithelium lines various surfaces and generally anchored by underlying CT; tissues often joined by a basement membrane which is a thin sheet of ECM anchoring the epithelium to underlying CT. Both epithelium and CT contribute to it; Sometimes called the basal lamina (electron microscopy)/ structure seen by light microscopy is basement membrane

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37
Q

Basement Membrane

A

ECM sheet attaching epithelium to CT; Cells anchored to basement membrane via HEMIDESMOSOMES; 50-100 nm thick with 3 zones: lamina lucida (has hemidesmosomes, laminin, entactin, integrins), lamina densa (Collagen IV), lamina fibroreticularis (Col III)

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38
Q

Simple squamous

A

Lining blood/lymph vessels, kidney glomeruli, lung alveoli, or any surface that has a lot of diffusion happening

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39
Q

Simple cuboidal

A

Secretory cells lining glands and ducts, kidney tubules. Anywhere secretion of proteins is actively happening

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40
Q

Simple Columnar

A

Mucus secreting absorptive surfaces, notably much of the GI tract (stomach to anus), can be ciliated as in bronchi of lungs and uterine tubes

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41
Q

Pseudostratified ciliated columnar

A

Mucosal surfaces, where they secrete mucus. Ciliated to push mucus along, as in various sperm carrying ducts and ducts of large glands. Also lining the trachea and upper respiratory tract

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42
Q

stratisfied squamous

A

Keratinized: skin and attached gingiva

Non Keratinized: lining mucosa of mouth, esophagus, and vagina.

Anything that might encounter abrasive forces on a regular basis

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43
Q

Urothelium

A

Bladder lining. Stretchy and irregular

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44
Q

Stratisfied cuboidal

A

Somewhat rare. Ducts of large sweat glands, salivary glands, and mammary glands

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45
Q

Stratisfied columnar

A

Fairly rare; found in the male urethra and associated with salivary glands. Sometimes transitional between simply columar and stratisfied squamous. Looks a bit like cuboidal cells with columnar cells stacked atop

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46
Q

Microfilaments

A

Cytoskeletal component; made of actin, 6-8nm diameter, structural function, microvilli, filopodia, gives shape to the cells, forms tracks for myosin, giving contractibility

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47
Q

Intermediate filaments

A

Cytoskeletal component; different in various tissues (vimentin, cytokeratin); around 10nm diameter, anchors, structural, non contractile

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48
Q

Microtubules

A

Cytoskeletal component; made of tubulin, around 25nm diameter, monorail system (kinesins, motor protein complex), cilia and flagella (dynein)

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49
Q

Tight Junctions (Zonula Occludins)

A

Cell attachment type; homotypical interactions between transmembrane proteins (proteins that are identical and stick tightly together); very narrow gaps between cells, control movement of stuff between cells, maintains cell polarization, bind to ACTIN MICROFILAMENTS (inside of cell), claudins, occludins, JAM, roles in various cell signaling pathways

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50
Q

Cell to cell Adhesive Junctions (Zonula Adherins)

A

Cell attachment type; Hold cells together,cadherins (outside; Ca2+ dependent) and catinins (inside) complexes, Nectin-Afadin complexes, vinculin and actinin attachments to ACTIN FILAMENTS, gaps of 20 nm so small stuff can get through

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51
Q

Focal Adhesion Junction

A

Cell attachments type; hold cells to ECM, similar to cell to cell adhesion, integrins replace cadherins as transmembrane component and they interact with many ECM proteins ex. collagen, fibronectin; integrin receptors (role in cell signaling); vinculin, actinin, and talin attachments to ACTIN FILAMENTS

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52
Q

Desmosomes

A

Cell attachment type; more cell to cell adhesion, cadherins (outsides) are called desmogleins and desmocollin; catinins (inside) are called desmoplakin, plakoglobin, and plakophilin; form lines externally, and plaques internally visible as dark bands (electron dense); attach to INTERMEDIATE FILAMENTS; Heterotypical interaction of desmoglein and desmocollin; gaps of 25 nm, help resist shearing forces- flat force across the surface

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53
Q

Hemidesmosomes

A

Cell attachment type; more cell- matrix adhesion, similar appearance to desmosomes (intracellular plaque visible), attach to INTERMEDIATE FILAMENTS; integrin transmembrane protein, tightly attach to basal lamina by integrin-laminin and collagen XVII; resist shear

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54
Q

Gap Junctions

A

Cell attachment type; cell to cell aqueous pores; 6x connexins= 1x connexon; forms a 2nm pore, 2-3 nms between cells; ions and small water soluble molecules may pass; nucleic acids, sugars, and proteins are too large; propagation of electrical signal

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55
Q

Cell attachments

A

All types of cell attachments function together to provide both cell to cell adhesion and anchoring, forming tissues;

Junctional Complex (tight junctions, zonula adherins, desmosomes, and gap junctions)

Terminal bar (group of junctional complexes which attach cells on their lateral surfaces. appear as a sort of band under a light microscope

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56
Q

Epithelial turnover and maintenance

A

Epithelial cells turnover, from several days to months, and are replaced by the divisions of progenitor cells (adult stem cells), which are pluripotent

Ex. small intestine; in epithelia, mitosis occurs on basal lamina, so stem cells and transit amplifying cells are normally in basal layer; stem cells in “niche” division rates and developmental choices are influenced by cytokines

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57
Q

Epithelial Function: Protection

A

Provides a physical barrier due to junctions; augmented by various secretions: mucus + cilia to trap and move things along, defensins in some cases ; provides a zone for antigen detection;

Ex. of primary protective epithelia: skin, upper respiratory tract, oral mucosa, gut, urinary system

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58
Q

Epithelial Function: Transport

A

Epithelium controls the passage of selective stuff; active or passive transport, can secrete (mucus or fluid) and can absorb (GI tract); blood gases passively diffuse across an epithelial barrier, most interactions with the outside world occur across an epithelial barrier

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59
Q

CT Cell Types

A

Permanent: Fibroblasts, adipocytes, macrophages, mast cells

Transient: Plasma cells, lymphocytes, neutrophils, eosinophils

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60
Q

Fibroblasts

A

Main cell of CT, highly motile, involved in ECM production and therefore tissue repair and renew; rarely have cell to cell connections (exception: perio ligaments); often have cytoskeletal (actin) connections from integrin to fibronectin in the ECM (fibronexus); many subtypes in many different tissues(pulp, PDL, oral mucosa); fibroblasts age- slower healing with age; incredible diversity of secretory products

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61
Q

Collagen

A 
triple helical structure, most abundant protein in the body (28 types), major synthetic product of cells derived from the mesenchyme; rich in proline and lysine (H bond allows triple helical assembly), fibrillar collagen and many other types, dentine (mostly type I, some III)
pulp (mixture of type I and III)
cartilage (Type II)
basement membrane ( Type IV chicken wire meshwork)

5 ‘microfibrils’ with a 1/4 stagger (overlap) align in a parallel fashion; banded structure of fibrils, stagger in microfibrils; bone/dentin (mineral deposition in gap regions) ; many diseases result from malformation of collagen (OI, epidermolysis bullosa) s
Scurvy (vitamin C deficiency; prolyhydroxylase and lysyl hydroxylase- assembly of collagen much less stable)

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62
Q

Elastin

A

Fibroblast product, assembled into sheets or fibers, glycoproteins fibrillin 1 and 2 (and others) form a microfibril scaffold onto which elastin fibers accumulate; final result is a fiber with an elastin core, supported by a glycoprotein scaffold

Marfan’s syndrome- fibrillin 1 mutation

63
Q

Adipocytes and adipose tissue

A

Adipocytes are single lipid droplet with thin rim of cytoplasm; flattened nucleus, each adipocyte is surrounded by basal lamina

Adipose tissue function: store lipid (energy), insulate, cushion, make hormones

64
Q

CT ground substance

A

made up of all sorts of things, mainly proteoglycans and glycoproteins; it is the non fibrillar stuff that makes up CT ECM (fills in the left spaces by the fibrils), gel like (highly hydrated), sequesters fluid, gives compressive strength to tissue (cartilage), keeps what should be squidgy, squidgy

65
Q

Proteoglycan

A

main component of ground substance made by fibroblasts; they are protein core with glycosaminoglycan chains (GAGs- aggregation and fluid sequestration ex. hyaluronic acid, chondroitin sulfate, keratin sulfate etc.) [carb with protein backbone that will sequester water and give it is squidginess] Ex. versican, perlecan, syndecan, and many others; have relatively strong negative charge and are hydrophilic; Non aggregating proteoglycans (many; perlecan, found in basal laminae, syndecan); CAN SERVE TO SEQUESTER GROWTH FACTORS IN ECM AND CAN HELP ACTIVATE GF RECEPTORS

66
Q

Glycoprotein

A

Proteins with carbohydrate side chains attached; found everywhere but also in ground substance; huge category but notable examples (fibronectin (cell migration/wound healing), tenascin (directs migration), thrombospondin (attachment, migration, collagen alignment)

Difference between glycoproteins and proteoglycans (proteoglycans are specialized glycoproteins and have a larger carbohydrate component than protein)

67
Q

Growth factors

A

Many; these can be secreted by a wide array of cells for immediate use (development) or can be sequestered into the ECM for later use (repair)

68
Q

Matrix digestion

A

Extracellular vs Intracellular; MMPs (matrix metallo proteases) are very significant in operative dentistry; kept tightly controlled in ECM because it can break it down; implications for tissue remodeling and disease states

69
Q

Loose CT

A

Most abundant type of CT; more cells and ground substance; fewer fibers, most cell types are present; location (underlies epithelia, forms stroma, fills spaces between tissues and organs, sheathes lymphatic and blood vessels); provides support and form, but not as much structure as dense CT

70
Q

Dense Irregular CT

A

more fibers, fewer cells, little ground substance; fibers arranged randomly, location (deeper dermis, organ capsules, submucosa of intestine) provide multidirectional structure

71
Q

Dense regular CT

A

Fibers arranged in same direction; few cells, mostly fibroblasts; location: tendons and ligaments, provides directional structure

72
Q

Skin

A

Epidermis (keratinized stratisfied squamous)

Dermis (loose CT) –> dense irregular CT

73
Q

Lipids and Fatty Acids Function **

A

store energy (Triglycerides especially), form membranes, carry info and signal (inflammation), perform diverse additional services ( vitamins, enzyme cofactors, colorants [absorb light at different wavelengths]) surfactants (like a detergent)

74
Q

Fatty Acids **

A

carboxylic acid with a long hydrocarbon chain

ex. saturated, unsaturated (cis vs trans), polyunsaturated

75
Q

Fatty acid nomenclature

A

18:1 (Δ9) cis- 9 octadecenoic acid; 18 C, 1 double bond at 9 , cis, 18 long chain
omega 3 FA- omega is carbon at tail end so omega 3 has a double bond off the 3rd C

76
Q

Fatty acid physical characteristics **

A

A mixture of saturated and unsaturated FA makes a membrane more mobile than just saturated FA; as the number of C increases, melting point increases; saturated FA have a higher melting point (from solid –> liquid)

77
Q

lipids **

A

one or more FA connected to a linker molecule

Common linkers: glycerol, sphingosine, glycerophosphate

Ex. triglycerides

78
Q

Storage Lipids (Triacylglycerides)**

A

Contain a glycerol linker with 3 FA; saturated, unsaturated, polyunsaturated; nonpolar, stable and relatively inert in aqueous solutions, not found in biological membranes, energy dense (have highly reduced long chains of carbon), primary storage molecules, primary source of energy for many organ systems

79
Q

Lipids are key metabolic constituents **

A

movement of energy through body; Organism metabolism (anabolism/catabolism[break down and release energy to do work/make more complex structures])

80
Q

Dietary Sources of lipids and FA

A

Dietary sources form triglycerides (fats, carbs, proteins)
Albumin (protein) transfers bloodstream free FA
Lipoproteins transfer triglycerides from adipose tissue to other cells

Dietary sources are ingested–> gallbladder–> bile emulsifies dietary fats in small intestine, forming mixed micelles–> interact with ApoC-11–> form chylomicron (lipoprotein)–> go into vasculature and lipoprotein lipase breaks it and releases lipids and deliver lipids to different cells and storage

81
Q

Lipids form membranes

A

Form micelles (individual lipid is wedge shaped; one tail) , vesicles, bilayer (individual lipid is cylindrical; 2 tails) because entropy is increased; allows water to be more disordered by causing lipid to be ordered

82
Q

Plasma membrane lipids and FA

A

3 major lipids: phospholipids, sphingolipids, and glycolipids; sterols (FA, cholestrol; sit in bilayer and change fluidity in membrane)

83
Q

Membrane Lipids: Phospholipids **

A

phosphate group, glycerol or sphingosine linker, FA, major constituent of most animal plasma membranes

84
Q

Membrane Lipids: Sphingolipids **

A

one shingosine, one FA, phosphate, glucose or polysaccharide head group components; membrane components, direct signaling activity

85
Q

Membrane Lipids: Glycolipids **

A

Anchor proteins to membrane, involved in cellular identification, tied to many diseases ex. lipopolysaccharides to tell if its a bacteria; Ceramide, sphingosine, FA

86
Q

Membrane FA: Sterols **

A

major membrane components, increases membrane rigidity, reduces membrane permeability, lipid raft constituent, needed for endocytosis ex. Cholestrol

87
Q

Lipids carry info and signal

A

Hormones, cell surface markers, inflammatory mediators (drive it and also resolution of it)

88
Q

Lipid Signaling Drives and Resolves Inflammation **

A

Injury and infection drive the release of inflammatory lipids (vasodilators, increase temp of region, increase rate of metabolism, sensitize nerve cells that innervate these periphery cells)

Ex. prostaglandins, thromboxanes, and leukotrienes

The enzymes cyclooxygenase 1 and 2 (COX 1/2) produce prostaglandins and thromboxanes from arachidonic acid

Non-steroidal anti- inflammatory drugs (NSAIDs) block COX 1/2 function (Aspirin, Ibuprofen, Naproxen)

89
Q

Lipids and FA perform diverse functions

A

Cell surface markers (blood type, cellular identity), antibiotics, vitamins and cofactors (compulsory, biochemically relevant)

90
Q

Essential FA

A

Essential- the human body requires but can’t produce the FA so must be obtained through the diet ex. Linoleic acid and alpha linolenic acid

91
Q

Nucleotide**

A

A molecule with a pentose (5 C ring), phosphate (1-3; if none= nucleoside), purine or pyrimidine base; foundational molecule of all life

92
Q

Nucleic acid**

A

Nucleotides connected by phosphodiester bonds;

93
Q

Importance of Nucleotides and Nucleic acids **

A

Information transfer (DNA [genetic], RNA [proteomic])

Energy transfer (ATP, GTP, NAD/NADH)

Signal transduction (cAMP, cGMP)

94
Q

Nucleic acids regulate cellular function **

A

DNA–>RNA–> Protein

Replication, Transcription, Translation
plus RNA replication and reverse transcription

basis for the cell hypothesis- cell is a recurrent organism; has blueprint of its function

95
Q

Purine**

A

A (Adenine) G (Guanine)

2 rings

96
Q

Pyrimidines**

A

C (Cytosine) U (uracil) T (thymine)

1 ring

97
Q

DNA vs RNA **

A

DNA (Deoxyribonucleotide polymer)
RNA (ribonucleotide polymer)

Key differences: 2’ ribonucleotide oxidation, reactivity, Thymidine vs Uridine, DNA confined to nucleus, RNA found throughout the cell

98
Q

Nucleic Acids form complex structures

A

Primary (nucleic acid chain), secondary (anti- parallel chains that bind to one another- H bond between bases), tertiary ( 3D right hand alpha helix)
quaternary (DNA bound on histone–> nucleosome–> chromosome)

99
Q

DNA Primary Structure

A

Phosphodiester bonds form nucleic acids

RNA is less stable (2’ OH can attack chain and break it)

Read DNA 5’–> 3’

100
Q

DNA Secondary Structure

A

Base H bonding forms strand (purine to pyrimidine)

Adenine- Thymine (Uracil)
Guanine to Cytosine

Antiparallel; stable in aqueous environments

Base bonding is not uniform- palindrome (sequence if separates from adjacent strand, can bind to itself creating cruciform structures or hairpins - form physical structures in which different proteins can target and bind to

101
Q

DNA Tertiary Structure

A

Strands form double helix; taking sheets of DNA, put in aqueous solution and forms a rightward helix

Different compressions: A form (more compressed), B form (regular), Z form (least compressed)

102
Q

DNA Quaternary Structure

A

Strands and Proteins create complex structures;

DNA–> Nucleosome (DNA wraps around histones)–> chromosome (copied, pulled apart for translation and replication)

103
Q

RNA is functionally Diverse

A
  1. Messenger RNA (mRNA)- DNA transcript that encodes proteins for production
  2. Transfer RNA (tRNA)- RNA adapter molecule tethered to amino aicds that interact with mRNA and form polypeptide chains
  3. Ribosomal RNA (rRNA)- RNA that forms the structural and functional backbone of ribosomes

Regulatory RNAs (aRNA, shRNA, siRNA)- a large class of RNA that regulates translation, signal transduction, and prevent infection by viruses

104
Q

RNA Primary Structure

A

Single stranded (mostly), formed from DNA transcription by RNA polymerase, mirror of the DNA template sequence; DNA is read 3–> 5 (template) and made 5–>3 (identical to nontemplate)

105
Q

Nucleotides are energy substrates and coenzymes

A

Electron rich, phosphate groups high in free energy, phosphate hydrolysis moves electrons to perform work, ATP is the primary euk energy currency; ex. Coenzyme A –> Acetyl CoA; NAD+

106
Q

Nucleotides are signaling molecules

A

(cyclic) cAMP; cGMP,

107
Q

Electronegativity

A

measure of the tendency of an atom to attract a bonding pair of electrons
F is the most electronegative element and Cs and Fr are the least;

108
Q

Interatomic bonding

A

Ionic (metallic with non metallic; NaCl) transfer of electrons (cation-anion) STRONGEST

Molecular or Covalent (non-metals, SO2, H20, C2H4O2) sharing of electrons

Atomic or Metallic (metals Cu2) electrons surrounding the element (cation) WEAKEST

109
Q

Intermolecular Interactions

A

Ion dipole, H bond, dipole- dipole, ion-induced dipole, dipole-induced dipole, dispersion (weakest)

Van der Waals Forces: random variations in the positions of electrons around one nucleus may create a transient electric dipole, which induces a transient opposite electric dipole in the nearby atom

110
Q

Noncovalent (weak) interactions among biomolecules in aqueous solvent

A

H bonds (between neutral groups or peptide bonds), Ionic interactions (attraction/ repulsion), hydrophobic interactions, Van der Waals interactions (any 2 atoms in close proximity)

between OH and F, N, O bonded to H

111
Q

Structure of a water molecule

A

Repulsion of H but O is attracting electrons forming a partial neg. and pos.; water molecules can combine with up to 4 other molecules

Water has a high specific heat (Amount of heat required to raise the temperature of 1 gr of substance by 1 degree Celsius) because of the H bonds

112
Q

H bonding in ice

A

In ice a single molecule of water binds to 4 molecules of water to yield a regular lattice structure while in liquid only 3.4; As water is cooled down, however, the molecules have less energy and hydrogen bonding takes over. The molecules form an ordered crystal through hydrogen bonding that spaces the molecules farther apart than when they were in a liquid. This makes ice less dense than water allowing it to float.

113
Q

H bonds in biological systems

A

Between the OH of an alcohol and water; between the carbonyl group of a ketone and water, between peptide groups in polypeptides, between complementary bases of DNA

114
Q

Directionality of H bonds

A

strong H bond when bonded molecules are oriented to maximize electrostatic interaction (straight line)

All proteins can perform their functions better if they have a certain direction

115
Q

Water as a solvent

A

Entropy=ΔS=(degree of molecular disorder)
Enthalpy= ΔH
free energy= ΔG = ΔH- TΔS (where ΔG is negative, ΔH has a small positive value and TΔS is positive) spontaneous (lower the free energy of a system) ex. water interacts electrostatically with CHARGED solutes

116
Q

Amphipathic compounds in aqueous solutions

A

highly ordered water molecules

ΔG = ΔH- TΔS (where ΔG and ΔH are positive and TΔS is negative)non- spontaneous
ex. water interacts unfavorably with non polar compounds ; interfere with the H bonding among water molecules [decrease in entropy]

ex. lipids in water (soaps work by emulsifies the grease (lipids) binds to internal part of micelles and they transport it) ; ex. drug delivery; liposome, lipid bilayer; all minimize the number of ordered water molecules required to surround hydrophobic portion of the solute molecules

117
Q

Release of ordered water favors formation of enzyme substrate complex

A

Ordered water interacting with S and E–> disordered water displaced by E-S interaction (stabilized by H bonding, ionic, and hydrophobic interactions)

118
Q

Solutes affect colligative properties of a solution

A

Adding salt- boiling point elevation;
Pressure boiling point melting point and osmotic pressure, water as a conductor; The presence of a solute lowers the freezing point of a solution relative to that of the pure solvent

119
Q

Extracellular osmolarity on water movement

A

Aquaporins

Isotonic- no net water movement

Hypertonic- water moves out of cell and cell shrinks

Hypotonic-water moves in creating outward pressure, cell swells and may eventually burst

120
Q

Proton Hopping

A

water can be an acid or base; hydronium

121
Q

Pure water is slightly ionized

A

not likely to dissociate
Keq= [products]/[reactants]

Kw= 1E-14

122
Q

pH Scale

A 
pH= -log [H]
concentration= E^-# gives you a pH

Acidic-7; strong acids completely dissociate in water while weak acids only partially do

123
Q

Henderson Hasselback

A

weak acids

pH= pKa+ log [A-]/[HA]

Ka is the equilibrium of dissociation constant or ionization constant

pKa is analogous to pH the stronger the tendency to lose its proton the stronger is the acid and the lower PkA

124
Q

Conjugated bases

A

consist of a proton donor and a proton acceptor

ex. carbonic acid/ bicarbonate is the most important physiological buffer in body (ex. pH of saliva)
HCO3- (bicarbonate) H+–> H2CO3 (carbonic acid)–> CO2(d) (aqueous phase in blood in capillaries)–> Co2(g) (gas phase in lung air space)

125
Q

The titration curve of acetic acid

A

pka= pH when acid and base have equal concentrations

buffer- maintains pH
ex. acetic acid (CH3COOH); Acetate (CH3COO-)

pH of ammonium is higher than that of acetic acid but can still act as an acid

126
Q

optimal pH in enzymes

A

pH is critical for digestion, etc. each enzyme we have has an optimal pH (where they can optimally function)

127
Q

Saliva

A

Salivary flow rate, buffering capacity, pH, electrolytes, organic components, proteins

flow rate and buffer capacity are clinically useful diagnostic indicators; no evidence that other biological characteristics of saliva are useful in predicting an increased risk of caries

128
Q

pH of body is controlled by 3 systems

A
  1. The chemical acid-base buffering by the body fluids that immediately combine with acids or base to prevent excessive changes in pH ex. buffers in blood, urine, etc.
  2. The respiratory center which regulates removal of volatile CO2 as a gas in the expired air from the plasma and therefore also regulates bicarbonate from the body fluids via the pulmonary circulation. (occurs in min)
  3. The kidneys which can excrete either acid or alkaline urine, thereby adjusting the pH of the blood. This response takes place over hours or even days, but represent a more powerful regulatory system.
129
Q

Metabolic alkalosis

A

Abnormal loss of acid (as in vomiting gastric HCl) or addition of a weak base can lead to this. Increases pH above 7.4

130
Q

Metabolic acidosis

A

abnormal removal of HCO3- or another alkali or addition of acids other than CO2 or H2CO3 (renal failure) can lead to this. decrease pH below 7.4

Since the pH of a Co2/ HCO3- solution depends on the ratio of these 2, and becuase lungs control CO2, but kidney controls HCO3, the overall description of this= pH= K+ kidney/lung

131
Q

Respiratory acidosis

A

the inability of the lungs to eliminate CO2 efficiently so equilibrium shifts toward increased H+ and HCO3= and pH decreases

Normally, 1.2 M/L of CO2 is dissolved in plasma, which is a partial pressure or pCO2 of 40 mmHg.

132
Q

Respiratory alkalosis

A

Excessive loss of CO2 through ventilation driving the equilibrium to the left, away from H+ and increasing H+ and increasing pH

Normally, 1.2 M/L of CO2 is dissolved in plasma, which is a partial pressure or pCO2 of 40 mmHg.

133
Q

Modern Cell Theory

A
  1. Cells are the most fundamental unit of life
  2. All living organisms are composed of 1 or more cells
  3. Cells give rise to organ systems that coordinate function in a complex organism
  4. All cells within a given species have the same general structure and chemical composition
  5. Cells are formed by the division of pre-existing cells
  6. Hereditary info is encoded by DNA and is passed along (or recombined) as cells divide
  7. Metabolism (energy processing; anabolism and catabolism) occurs within cells
134
Q

Domains of life

A

Bacteria, Archae, Eurkarya

Use to be 5 kingdoms: animalia, plantae, protista, fungi, bacteria and later archae

135
Q

The constant transition of energy maintains life

A

2 real sources of energy on earth: light [phototrophs] and chemical [chemotrophs] (we depend on chemical)

136
Q

Proks vs Euk

A

Proks: 1-5µm scale, cell wall,no membrane bound organelles, cytoplasmic DNA, No cytoskeleton, 70S ribosome, replicate through binary fission, genetic diversity via mutation

Euks: 10-500µm, no cell wall, membrane bound organelles, nuclear DNA, cytoskeleton, 80S ribosome, replicate through mitosis, genetic diversity via meiosis/recombination

Both have plasma membrane

137
Q

Prok cells

A

gram positive (large peptidoglycan layer) and negative (LPS, sugar that sits on outside of cells targeted by our immune system) are different in their membranes; treated in different ways

Cell envelope differs, ribosome is smaller, nucleoid has one or several long circular DNA molecules, pili provide points of adhesion to surface of other cells, flagella propel cell through its surroundings

138
Q

Euk cell components **

A

Peroxisome (catabolism of lipids and fatty acids), cytoskeleton (structure, actin, IF, microtubules), lysosome (breaks down membrane associated organelles, proteins, fats), transport vesicle, golgi complex (structure that organizes movement of materials in membrane or material to be released or going to other organelles), smooth ER (lipid synthesis), nucleus (double membrane attachment to ER, nuclear membrane is continuous with it), nucleolus (make ribosome parts), rough ER (ribosomes embedded make proteins in cytoplasm), mitochondria (powerhouse of the cell), plasma membrane, nuclear membrane (outer and inner)

139
Q

Membrane segregate environments and function

A

Segregation is critical for biochemical reactions; can not have concentration gradients without it
Endosynic pathway

140
Q

The plasma membrane- boundary, interface, and information regulator

A

Fluid mosaic model (plasma membrane components move fluidly within the lipid bilayer)
Dynamic interface, heterogenous (different from one side to another), discrete domains (lipid rafts)

Too fluid; loss of barrier function
too rigid: restricted cell shape and transport capacity

141
Q

Lipid Rafts

A

Discrete plasma membrane domains; cholesterol and sphingolipid rich, limited fluidity, regulate signal transduction and endocytosis

142
Q

Endocytosis- Internalizing the external environment **

A

Internalization of the plasma membrane;

Phagocytosis, Macropinocytosis, Clathrin dependent, Caveolin dependent, Clathrin and caveolin independent

Functions: remodel the plasma membrane, alter the extracellular environments (ex. macrophages), provide necessary nutrients, regulate signal transduction, bring things in

occurs in all membrane domains

143
Q

Clathrin Mediated Endocytosis

A

Need dyamin to be present for this to occur

Recruitment of AP2 to attach to transmembrane proteins with ligand bound–> allows clathrin to interact–> dyamin fuses membrane–> clathrin coated vesicle into cell

Lattice- cause invagination of plasma membrane as lattice form

144
Q

The Endocytic pathway sorts internalized vesicles **

A

Vesicular fusion and excision, transport can occur between every compartment, Rab GTPase proteins critical; tells it which path to take (drives formation/fusion of vesicles), pH decreases along pathway; dissociation of binding of proteins together

145
Q

Golgi Network

A

Organizing import and export (from ER to outer)

cis–> trans side psorting[

146
Q

Cytoskeleton

A

Morphology (cellular form and shape), structure (backbone) and transport (movement of intracellular cargo)
Microfilaments (Actin- monomeric), microtubules (tubulin- dimer), Intermediate filaments (vary)

147
Q

Molecular motors

A

Transporting intracellular content along the cytoskeleton; directed process
vesicles tethered to Dynein or Kinesins

ex. Dynein (retrograde movement- toward nucleus)
ex. Kinesin (anterograde movement- away from nucleus to outside)

148
Q

Mitochondria

A

Cellular energy production; multifolded cisternae, inner membrane forms matrix, mitochondria is all throughout cell, glycolysis (cytoplasm) Krebs cycle (in matrix of mitochondria) and ETC (intermembrane space; formation of ATP)

149
Q

Nucleus

A

Director of Cellular function and hereditary transmission; where DNA resides, relaxed/spread out most of time but condenses toward nucleolus sometimes; accessible to transcription factors leads to the transcription for the production of RNA (template for protein production)

150
Q

Transcription**

A

DNA–> RNA; RNA polymerase reads 3–> 5 and RNA is produced 5–>3; RNA actively exported through nuclear pore complexes; requires ATP

151
Q

Ribosomes

A

80S; Polypeptide Chain production from mRNA; codons encode for specific amino acids–> put together in a chain; complex made of rRNA (structural role), appropriate tRNA (associated with codon of mRNA) will be recruited, bind, and peptides bind to each other and form polypeptide chain

152
Q

Translation

A

(from nucleus–> rER–>) RNA–> protein [proteins associated with membrane [bound polyribosome] or vesicular space [free in cytosol–> free polyribosome] that can be released to exterior]
(rER–> cis golgi–> trans–> lysosome, transport vesicle or secretory granule)

Activation of aa –>Initiation–> Elongation–> termination–> protein folding

153
Q

Cell Cycle**

A

INTERPHASE
G0= cell cycle arrest (no active division, chromatin dispersed throughout the nucleus)
G1 phase=Gap phase 1 (cellular contents are duplicated, chromosome not)
S= synthesis (chromosomal material duplicated)
G2 phase= Gap phase 2 (chromosomes cohere and proper duplication checked)

MITOSIS (cell division- replication of genetic material)
PMAT= prophase, metaphase, anaphase, telophase

154
Q

Euk cells divide by mitosis and meiosis **

A

Mitosis: Interphase–> PMAT–> cytokinesis (diploid cells with 46 chromosomes)

Meiosis: Interphase –> meiosis 1 (PMAT 1–> cytokinesis)–> meiosis 2 (PMAT 2–> cytokinesis) (haploid cells with 23 chromosomes ex. gametes)

Human Form & Function (6 decks)

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