Cells to Tissues Flashcards

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1
Q

adhesive structures

A

tight junction, adherens junction, spot desmosome, hemidesmosome, gap junction

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2
Q

tight junction (adhesive proteins, substrate, & function)

A

adhesive proteins: occludin, claudin, JAMs
bind to: actin filaments
function: prevents materials from moving in between cells (can also serve as receptor and entryway for viruses - especially in the intestine)

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3
Q

adherens junction (adhesive proteins, substrate, & function)

A

adhesive proteins: cadherens
bind to: actin filament
function: form part of the circumferential belt to give structure/stability to the cell

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4
Q

spot desmosome (adhesive proteins, substrate, & function)

A

adhesive proteins: desmosomal cadherens
bind to: intermediate filaments
function: attach to intermediate filaments
* made of cytoplasmic plaque associated with desmoglein and desmocollin

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5
Q

hemidesmosome (adhesive proteins, substrate, & function)

A

adhesive proteins: integrin α6ß4
bind to: intermediate filaments
function: attaches cell to basal lamina (keeps cells in position & associated with ECM in order to survive)

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6
Q

gap junction (adhesive proteins, substrate, & function)

A

adhesive proteins: connexins, innexins, & pannexins
bind to: indirect connection to cytoskeleton
function: communication - allows diffusion of small molecules between cells

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7
Q

two types of cadherens

A

E-Cadherins & desmosomal cadherin

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8
Q

E-Cadherins

A

found in adherens junctions
homophillic interaction: associate with another cadherin on extracellular side / interact with catenins that attach to circumferential belt

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9
Q

desmosomal cadherin

A

made up of desmoglein and desmocollin;

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10
Q

different regions of a polarized cell in a tissue

A

apical
lateral
basal

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11
Q

apical domain

A

interacts with surface

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12
Q

lateral domain

A

nteracts with/ is connected to adjacent cells

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13
Q

basal domain

A

interacts with the basal lamina

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14
Q

integrin

A

multi adhesive protein; transmembrane heterodimers (α & ß chains) that interact with ECM; can have outside-in & inside-out signaling

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15
Q

outside-in signaling

A

integrin responds to outer ligand binding, conformation change passes through the molecule, across the plasma membrane, and induces change on the cytoplasmic side

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16
Q

inside-out signaling

A

growth factor receptors (GFRs) can activate the integrin tail and induce conformation change on the outside of cell that alters ligand affinity

17
Q

basal lamina

A

region directly under the cell (generally in polarized epithelial cells); specialized form of ECM

18
Q

components common to all basal lamina

A

Type IV Collagens
Perlecan
Entactin
Laminin

19
Q

How is basal lamina formed?

A

Generated / secreted by the cells

20
Q

What are collagens?

A

Trimeric helix structures that form a network in the basal lamina & can interact with other proteins. Have unique synthesis process that begins in the rough ER and is completed outside the cell.

21
Q

How do the collagen isoforms differ?

A

size & structure, associations, function, & tissue

22
Q

notable collagen isoforms

A

Types IV, I, & II

23
Q

Type IV collagen

A

found in the basal lamina - makes up the framework

24
Q

Type I collagen

A

found in tendons - gives strength

25
Q

Type II collagen

A

found in cartilage - absorbs shock and gives strength

26
Q

general structure of collagen

A

C-terminal globular head
Trimeric helix
Small N-terminal globular domain

27
Q

What makes collagen unique?

A

it’s synthesis

28
Q

How is collagen synthesized and secreted?

A

Formation begins in the Rough ER; Propeptide (has additional peptides to prevent premature folding); Procollagen forms triple helices; Moves through the Golgi Apparatus; Lateral association begins; Excreted out of the cell by golgi dependent vesicles; Propeptides are cleaved; Assembly & crosslinking of fibrils

29
Q

proteoglycans

A

Molecule with a protein backbone and very large sugar dimers

30
Q

GAGs

A

glycosaminoglycans - large sugar dimers found in proteoglycans

31
Q

proteoglycan function

A

crosslinking & cushioning/buffer between molecules

32
Q

What are laminin and fibronectin?

A

Multiadhesive proteins: They have domains that act as binding sites for many different molecules. They are important in development because they form a cell substrate or highways for cells to migrate along.