Tissue Architecture Flashcards

1
Q

Why are cytoskeletons dynamic and adaptable?

A

Can disassemble, diffuse, and reassemble elsewhere

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2
Q

What forms of cytoskeleton filaments are thermally stable?

A

Multiple protofilaments

Single protofilament are not thermally stable

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3
Q

What filaments are resistant to stretching forces?

A

Intermediate filaments

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4
Q

What are the main components of cytoskeletal filaments?

A

Intermediate filaments

Microtubules

Microfilaments

Associated proteins

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5
Q

Mesh-like structure made up of intermediate filaments.

A

Nuclear lamina

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6
Q

Fuctions of intermediate filaments

A

Form a network throughout the cytoplasm and surround the nucleus

Rope-like properties give high tensile strength

Often further stabilized by accessory proteins

– Cross-link filaments into bundles

– Link to microtubules, actin filaments, and cell-junctions

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7
Q

What intermediate filament is found in epithelial cells?

A

Keratin filaments

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8
Q

What intermediate filament is found in connective tissue cells, muscle cells, and glial cells?

A

Vimentin and vimentin-related filaments

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9
Q

What intermediate filament is found in nerve cells?

A

Neurofilaments

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10
Q

What is the nuclear intermediate filament?

A

Nuclear lamins

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11
Q

Functions of microtubules

A

Provide tracks for transport vesicles

Mitotic Spindle formation

Cilia and Flagella

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12
Q

Binds and stabilizes microtubules

A

taxol

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13
Q

Binds tubulin dimers and prevents polymerization.

A

Colchicine, colcemid, vinblastine, vincristine

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14
Q

What is F actin composed of?

A

Twisted polymer of G-actin (globular) that has structural polarity

Many must be in association with other proteins to be stable

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15
Q

Binds and stabilizes actin filaments

A

Phalliodin

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16
Q

Caps actin filament plus end, preventing polymerization there

A

Cytochaslin

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17
Q

Binds actin monomoers and prevents polymerization

A

Latrunculin

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18
Q

How can actin filaments be modified when bonded to other proteins?

A

Stabilize

Strengthened

Cross-linked

Organizes

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19
Q

What are some extracellular proteins?

A

Perlecan

Sheet formin collagen (IV)

Fibrillar collagen (I,II,III)

Lamninin

Fibronectin

Nidogen/entactin

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20
Q

Main structural protein in ECM/connective tissue and basal laminae.

A

Collagen

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21
Q

How do collagen types differ?

A

28 types

Homotrimers

Heterotrimers

Form collagenous triple helix

Can be fibers, sheets, or transmembrane structures

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22
Q

Where is the precollagen prepared for secretion

A

Secretory Vesicles

23
Q

Scurvy is caused by loss of what cofactors

A

Ascorbate or Iron

24
Q

Disease caused by defects in collagen or enzymes contributing to synthesis.

A

Ehlers-Danlos Syndrom

Weakens connective tissue in the skin, bones, blood vessels, and organs

25
Q

Links cells to extracellular matrix, or basil lamina

A

Focal Contacts

26
Q

What are the four classes of Cell Adhesion Molecules

A

Cadherins (e-cadherins)

Ig-superfamily CAMs (NCAM)

Integrins (avB3)

Selectins (P-selectins

27
Q

What are the common aspects of cadherins?

A

Ca2+ dependent adhesion molecule – Important in formation of junctions between cells (epithelial “sheets”) such as desmosomes and adherens junctions

– Homophilic interactions (extracelluar)

– Interact with cytoskeleton (actin)

28
Q

What are classic cadherins?

A

Cytoplasmic domain interacts with beta-catenin, alpha-catenin, and p120

Linked to the actin cytoskeleton

Associated with adherens junctions

29
Q

What are the classic cadherin examples listed?

A

E-cadherin (epitheilial)

VE-cadherin- (vascular-endothial)

N-cadherin- (neural)

30
Q

What are atypical cadherins?

A

Function without interaction with catenins or a link to the actin cytoskeleton.

31
Q

Example of an atypical cadherin.

A

LI-cadherin - liver-intestine cadherin

32
Q

How can Cadherin serve in the detection of metastatic tumors?

A

Epithelial to mesenchymal transition (EMT)

In bladder cancer, a decreased E-cadherin and increased N-cadherin can mark metastasis.

33
Q

Family of more than 25 Calcium-independent transmembrane glycoproteins that are involved in immune cell interactions.

A

Ig Superfamily CAMS

34
Q

What type of bonding does the Ig Superfamily participate in?

What is the function of this binding?

A

Homophilic and heterophilic binding

Involved in recognition, binding, or adhesion processes of cells

35
Q

Contain a variable number of immunoglobulin-like domains.

Expressed on vascular endothelial cells and bind to various integrin molecules.

A

ICAM, VCAM-1, PECAM-1, NCAM

the NP does IV

36
Q

Contain Ig-like and mucin-like domains

Expressed on mucosal endothelium to direct lymphocyte entry into mucosa.

A

MAdCAM-1

37
Q

What are selectins and what are their roles?

A

Family of calcium-dependent glycoproteins

Bind to extracellular carbohydrates

Play important roles in host defense mechanism

38
Q

How do selectins play a role in the host defense mechanism?

A

Increased presentation during local inflammatory response

WBC surface markers include carbohydrates which act as ligands for selectins

Low-affinity of selectins to ligands allows for leukocyte “rolling” during leukocyte adhesion cascade

39
Q

What are the types of selectins?

A

Endothelial (E)-selectin

Leukocyte (L)-selectin

Platelet (P)-selectin

40
Q

How many integrins are there?

A

15 α and 8β subunits form over 20 heterodimeric integrins

41
Q

Functions of integrins

A

Couple the extracellular matrix to cell cytoskeleton

Can activate signaling pathways

Cell-Cell interactions via β2 family

42
Q

How do integrins activate signaling pathways

A

Interactions with receptor tyrosine kinase

Take part in regulating growth, division, survival, differentiation, apoptosis

43
Q

B2 Integrins are important for cell-to-cell interactions for what?

A

On leukocytes they allow for adhesion and transmigration to sites of infection.

44
Q

What important molecule is synthesized in the RER for collagen production?

A

RER = Synthesis of precollagen

45
Q

Where does hydroxylation of proline and lysine, glycosylation of select hydroxylysine residues of precollagen occur?

A

The Endoplasmic Reticulum

46
Q

Where does self-assembly of the trimeric molecule of precollagen occur?

A

Golgi Apparatus and ER

47
Q

How does self-assembly of the trimeric molecule of collagen occur?

A

With sulfide bonds initiating it in the c-terminus.

48
Q

Where is precollagen cleaved to collagen?

A

In the extracellular environment

49
Q

Describe the movement of microfilaments.

A

Faster movement on the postive end. dissociation or slower growing of the negative end

50
Q

What role does gamma tubulin play in microtubules?

A

Nucleation of the minus end provides area from which microtubules can grown

51
Q

What three chains make up collagen?

A

3 alpha chains total

2 alpha1

1 alpha2

52
Q

Vitamin C is a cofactor of what?

A

Prolyl hydroxylase, which hydroxylates collegen

53
Q

4 cell connections and junctions

A

Anchoring

Occlluding - maintain cell polarity

Channel-forming

Signal-relaying

54
Q

4 types of Anchoring junctions

A

Adherens junctions

Desmosomes

Hemidesmosomes

Focal, fibrillar, and Ad adhesions