MCM 2-10: Tissue Organization, Cell Junctions, and Extracellular Matrix Flashcards Preview

MSI Unit II > MCM 2-10: Tissue Organization, Cell Junctions, and Extracellular Matrix > Flashcards

Flashcards in MCM 2-10: Tissue Organization, Cell Junctions, and Extracellular Matrix Deck (36)
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1
Q

General organization and function of major tissue types

A

Cellular - tissue composed mainly of cells. integrity and properties are derived from cell junctions (epithelium)

Connective - tissue composed mainly of ECM with a few cells that synthesize, remodel, and bind the ECM. Physical properties of tissue is provided by organization of ECM (loose CT, cartilage, bone, tendon)

2
Q

what are anchoring/adhering junctions?

A

junctions whose primary purpose is to maintain tissue integrity under mechanical stress.

can be cell-cell or Cell-ECM junctions

3
Q

Three components of anchoring/adhering junctions

A

transmembrane glycoprotein - anchoring portion

complex of linker proteins on cytosolic face - regulates assembly and connects to cytoskeleton

cytoskeleton - connection can be to intermediate filaments or microfilaments (actin). Distributes force due to mechanical stress over a large area, allow the glycoprotein to stay attached.

4
Q

Four types of anchoring junctions

A
  1. adherens junctions/zonula adherens
  2. Focal Adhesions/Focal Contacts -
  3. Desmosomes -
  4. hemidesmosomes
5
Q

Tight Junctions/Zona Occludes (5 features)

A
  1. provide permeability layer across epithelial sheets like in small intestine - This allows regulated transport of nutrients through the cells (Transcellular transport). Na+2 dependant uptake occurs at apical membranes, faciliatated diffusion occurs at basolateral membranes
  2. maintain cell polarity by keeping membrane trasnport proteins in correct locations
  3. claudin and occludin are major proteins of tight juncctions
  4. strings of transmembrane proteins interact with each other on adjacent cells via homophilic interactions
  5. cytoskeleton not needed for integrity
6
Q

Gap Junctions ( 3 features)

A
  1. Provide means of communication between neighboring cells (such as electrical conduction in cardiac cells). Also known for passage of small molecules such as amino acids and vitamins
  2. made of single protein called connexin. six connexin molecules associate in PM to form connexon (hemi channel). connexons on adjacent cells associate to form gap junctions
  3. regulated by intracellular Ca+2 concentration or pH

high Ca+2 or low pH = gap junction close
low ca+2 or high pH = gap junction opens

7
Q

three major families of extracellular matrix proteins

A

fibrous proteins, bulky space filling proteins, cross linking proteins

8
Q

fibrous proteins

describe each type.

A

includes collagens (fibrillar, and type IV) and elastin

Fibrillar collagen provide tensil strength; resist stretching.
the pro-collagen triple helix is secreted from golgi and collagenases cleave the pro-peptides forming true collagen helices which then self associate into fibrils and fibers like tendons.

type IV collagen does not follow same pathway - when excreted into ECM it is not acted upon by collagenases, it forms mesh which is compoenet of basal lamina

Elastin provides elasticitiy. undergoes extensive cross linking following secretion via coalent linking of serine residues. elastic character is derived mostly from the many random coils in the polypeptide chain due to high proline content. The Glycoprotein fibrillin forms a sheath around the elastin fibers, preventing overstretching.

9
Q

bulky space filling proteins

includes what?

does what?

A

including proteoglycans.

Resist compression forces and allow for rapid diffusion of soluble molecule like growth factors.

also permit cell migration

the GAGS on proteoglycans have many sulfate and carboxyl groups, giving them negative charges making them hydrophilic. they can bind noncovalently many water molecules

a hydrated gel is only 10% proteoglycan.

Using linker proteins, proteoglycans can complex with hyalauronic acid and resist compression forces

in loose CT, primary role of proteoglycan molecules is structure and space filling, permitting free movement of water soluble molecules as well as cells in the matrix

10
Q

cross linking proteins

A

includes fibronectin and laminin.

Fibronectin - heterodimer that can assemble higher order structures. Many alternative-splice variants have modified functions. They have multiple binding sites giving them their functionality as crosslinking molecules. Fibronectin can bind :integrins, heparin, syndecan, types I,2,3 collagen, and fibrin

Laminin - a three chain polypeptide, forms component of basal lamina along with type 4 collagen and proteoglycan.
Laminin binds integrins on cell surface, heparin, TYPE 4 COLLAGEN

11
Q

Anchoring junction diseases

A

result in loss of tissue binding and blistering, can be fatal
-pemphigus - autoimmune, antibodies generated against cadherins, disrupt cell-cell junctiojns

-epidermylosis bullosa simplex - defect in keratin assembly

12
Q

Extracellular matrix protein diseases

A

ehlers-danlos - various fibirllar collagen defects, hyperextensible skin and joints

marfan syndrom - mutation in fibrillin gene, makes aorta prone to rupture

DMD - basal lamina plays role, as it surrounds and supports muscle cells

13
Q

adherens junctions/zonula adherens

A
  • cell-cell anchoring junctions
  • transmembrane glycoproteins are cadherins which require Ca+2 to interact with another cadherin on adjacent cell (homophilic).
  • linker proteins interact with actin filaments
14
Q

Focal Contacts

A
  • cell to ECM anchoring junctions
  • TM glycoproteins are integrins (formed from alpha-beta subunit heterodimer) require Ca+2 to interact with fibronectin in the ECM (heterophilic)
  • linker proteins interact with actin filaments
15
Q

desmosomes

A

Cell:Cell anchoring junctions

  • tm glycoproetins are caherins (like adherins junctions)
  • linker proteins interact with IF like keratins
  • they connect IF filaments across epithelial sheet
16
Q

hemidesmosomes

A

cell: ECM anchoring junctions
- TM glycoproteins are integrin a6/b4 - attatch the of basal lamina
- linker proteins interact with IF
- connect intermediate filaments across an epithelial sheet

17
Q

The two Cell:Cell Adhering/anchoring junctions and what they have in common

A

Adherens junctions and Desmosomes

  • cadherin glycoprotein
  • homophilic interaction (cell to cell)

cell:cell are homophilic interactions with cadherin glycoproteins

18
Q

The two cell:ECM adhering/anchoring junctions and common features

A

Focal adhesions and Hemidesmosomes

  • integrin glycoprotein
  • heterophilic (cell:ECM)

Cell:ECM are heterophilic interactions with integrin glycoproteins

19
Q

the cytoskeleton of the 4 anchoring junctions

A

Adherens and Focal = Actin

Desmosomes and Hemidesmosomes - Intermediate filaments

20
Q

what do adherens junctions do?

A

provide strength and are important in development

21
Q

what do focal adhesions do?

A

orient contracts, important in developmental processes

22
Q

what do desmosomes do?

A

maintain cellular tissue integrity

23
Q

what do hemidesmosomes do?

A

maintain cellular tissue integrity

24
Q

describe the ECM

A

major component of CT, giving CT strength and integrity

-generated by fibroblasts, Chondroblasts(cartilage) or osteoblasts (bone)

25
Q

three major families of ECM proteins

A

fibrous proteins, bulky space filling proteins, cross-linking proteins

26
Q

fibrillin?

A

a glycoprotein which surrounds the fibrous protein elastin to prevent overstretching

27
Q

the crosslinking proteins fibronectin and laminin bind what?

A

fibronectin bind integrins (focal adhesions and desmosomes), heparin (GAG), syndecan (proteoglycan), 1/2/3 collagen, fibrin (blood clotting)

laminin - integrins on cell surface, heparin (GAG), type 4 collagen

28
Q

pemphigus

disease type?

A

Anchoring Junction Disease - An autoimmune disease in which antibodies are generated against cadherins, disrupting cell-cell junctions leading to a loss of tissue integrity/blistering

29
Q

Epidermolysis Bullosa Simplex –

disease type?

A

Defect in keratin assembly. anchoring junction disease

30
Q

Ehlers-Danlos syndrome

disease type?

A

– Various fibrillar collagen defects. Causes hyper extensible skin and joints.
– Mutation in the fibrillin gene. Makes the aorta prone to rupture.

ECM protein disease

31
Q

DMD?

disease type?

A

The basal lamina plays a role in DMD, as it surrounds and supports muscle cells.

ECM protein disease

32
Q

describe the basal lamina

makeup?

function?

A

proteogylcan + laminin + Type 4 collagen

Basal lamina is specialized ECM that

  1. forms a dense meshwork that surrounds/supports muscle cells
  2. links muscle to tendon
  3. provides support for epithelial sheets
  4. acts as molecular filter for the kidney
  5. is involved in guidance pathways (neural crest cells).
33
Q

Which of the following junctions
DO NOT utilize interactions with the cytoskeleton in fulfilling their primary function?

A. Tight junctions only
B. Adherens junctions only
C. Gap junctions only
D. Gap junctions and adherens junctions
E. Gap junctions and tight junctions
A

E. Gap junctions and tight junctions

34
Q

loss of blood proteins into the urine is prevented primarily by?

A. The barrier function of the endothelial cell layer of the capillaries.
B. The basal lamina between the endothelium of the blood vessel and the glomerulus epithelium.
C. The glomerulus epithelium.
D. The connective tissue surrounding the capillary bed.
E. Adhesio
n of blood prot
eins to circulating platelets.

A

the basal lamina between the endothelium of bv and the glomerulus epithelium (Choice B)

35
Q
(2 pts) Which of the following extracellular matrix molecules is primarily responsible 
for the 
“shock absorbing” properties of cartilage?
A. Fibronectin
B. Proteoglycan
C. Type IV collagen
D. Laminin
E. Elastin
A

Proteoglycan - has gags with - residues. can bond water and form gel.

36
Q

Cleavage of the pro-peptides from type I collagen molecules occurs in the Golgi apparatus and is necessary for fibril formation.
TF

A

False - post translational modifications occur in the golgi forming a pro-collagen triple helix. When it is excreted, collagenases in the ECM cleave its pro peptides to form a true helical collagen

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