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Cell Bio > Lecture 3 - Quiz 1 > Flashcards

Lecture 3 - Quiz 1 Flashcards

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Biology 101 flashcards
1
Q

What is the ECM?

A

Extracellular matrix - any substance produced by cells and secreted to the extracellular space within the tissues - connective tissue

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2
Q

What are fibroblasts and their structure?

A

Fibroblasts have elongated nuclei and cytoplasms, and synthesize and maintain all the ECM components

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3
Q

What are tenocytes?

A

The fibroblasts of the tendons that maintain the ECM - principally collagen

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4
Q

What gives ECM tension and compression resistance?

A

Collagen crosslinks for resistance to tension and proteoglycans give resistance to compression

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5
Q

What are the roles of ECM?

A

Hold tissues together for structural support, comportmentalize tissues from one another and regulate intercellular communication by cell signaling - promotes and inhibits growth factor signals - essential for growth and wound healing

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6
Q

How does the ECM promote and inhibit GF signals?

A

Promotes by pericellular matrix (PCM) molecules binding and localizing GF close to cell surface to promote binding to receptor, in hibits when ECM/PCM molecules bind GF and sequester it away from the receptors

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7
Q

What is the structure of the PCM for chondrocytes?

A

PCM made up of hyaluronic acid with red blood cells kept at a distance from the chondrocytes

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8
Q

What are the components of the ECM?

A

Ground substance - like adhesive glycoproteins like laminin and fibronectin play a role in the adhesion of the cells and glycosaminoglycans (GAGs) give a hydrate gel for resistance to compressive forces and fibers - provide tensile strength and elasticity with collagens and elastins

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9
Q

What are the classifications of GAGs?

A

Heparin, chondroitin, keratan - all sulfates to give negative charge to bind a lot of water
Hyaluronic acid HA - non sulfated
Make up proteoglycans

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10
Q

What do GAGs do and what is their structure?

A

Provide a hydrate gel to resist compressive forces - polysaccharides composed of linear repeated disaccharide units and make up proteoglycans - GAGs are linked to core proteoglycan by linker proteins (GAG portion looks like bottle brushes off of backbone)

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11
Q

What gives proteoglycans their biological functions?

A

THe GAG chain and their linker proteins present with different protein ligands give different roles like coagulation, lipolysis, inflammation, etc.

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12
Q

Which type of GAG is non-sulfated?

A

Hyaluronic acid?

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13
Q

Where is hyaluronan found and what is it’s role?

A

Skin, umbilical cord, eye, synovial fluid of joints, gives lubricating and resistance to compression rles

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14
Q

What are some external uses of HA?

A

Lubrication for eye surgery, tumor marker for progression of breast and prostate cancer, wound healing scaffolding, reduce pain in osteoarthritis by lubrication, anti adhesive product, and fillers in ccosmetic applications

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15
Q

What gives ECM tensile strength and elasticity?

A

Fibrous protein - adhesive glycoproteins

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16
Q

What is the major fibrous protein in the ECM? and what do they do?

A

Collagen - give tensile strength and structural support

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17
Q

Where is Collagen I found and how abundant is it?

A

Skin, tendon, vasculatures, organs, BONE - most abundant >90%

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18
Q

Where is Collagen II found?

A

Cartilage

19
Q

Where is Collagen III found?

A

Reticulin - reticular fibers or blood vessels

20
Q

Where is Collagen IV found?

A

Forms bases of cell basement membrane

21
Q

What do most collagen related diseases arise from?

A

Genetic defects or nutritional deficiencies

22
Q

What does degradation of collagen lead to?

A

Wrinkles

23
Q

What is osteoporosis?

A

Not inherited genetically, brought on with age and gender (estrogen deficiency) - reduced levels of collagen in skin and bones

24
Q

What is osteogenesis imperfecta and what causes it?

A

Cause by a mutation in collagen type I in bone causes fragile bones - can also give scoliosis

25
Q

What is chondrodysplasias?

A

A skeletal disorder caused by a mutation in type 2 collagen (cartilage) - defect in development of cartilage of long bones giving arrested growth and dwarfism

26
Q

What can help decrease swelling in Rheumatoid arthritis patients?

A

Organ administration of type II collagen

27
Q

What is the structure of collagen?

A

A triple alpha helix forms a tropocollogen molecule and these line up to give fibrils

28
Q

What are some medical applications of collagen?

A

Bone grafting as triple helix makes it strong and does not compromise skeletal structural integrity and is prevented from enzyme breakdown - scaffolds for tissue regeneration and deposition of cells - skin grafts - wound healing processes and cosmetic fillers

29
Q

What do elastins do?

A

Give elasticity to tissues allowing them to stretch and return to their original pposition

30
Q

Where are elastins found?

A

Blood vessels, lungs, skin, bladder, ligaments, elastic cartilage

31
Q

What are elastins synthesized by? What degrades them?

A

Fibroblasts and smooth muscle cells, elastase enzymes degrades activated by fibroblasts and inflammatory cells and MMPs also degrade

32
Q

What are the elastin receptors?

A

Fibulin-5, Elastonectin, Ficolin, Hucolin

33
Q

What are some diseases associated with elastin?

A

Some congenital heart defects and hypertension, elastolysis (cutis laxa is the absence of elastin fibers - rare and inherited gives loose folds), williams syndrome, menkes, Marfan’s syndrome, and hurler disease

34
Q

How much can elastin stretch and why?

A

1.5 times their length and snap back to original length because of heavy crosslinking

35
Q

What are examples of adhesive glycoproteins?

A

Fibronectin, laminin

36
Q

What is the structure of fibronectin? and what is it’s cell binding sequence?

A

Rod like structure with three modules, tripeptide arg-gly-asp are the rgd cell binding sequence - binds to integrin receptors - exists as a dimer in its active form consisting of two nearly identical monomers linked by disulfide bonds

37
Q

How are fibronectins secreted and where do they bind?

A

Secreted in unfolded, inactive form and then bind to integrins which unfold the fibronectin molecules - where they can form dimers

38
Q

Do fibronectins bind substances besides integrins?

A

Yes, they are multiadhesive

39
Q

What are two types of fibronectins present in vertebrates?

A

Insoluble cellular FN - secreted by fibroblasts, major ECM component
Soluble plasma FN is a component of blood plasma produced in liver by hepatocytes

40
Q

What is the function of fibronectin?

A

Cell adhesion, growth, migration and diifferentiation in cell signaling, form blood clots in plasma, structural support and compartmentalization in cellular FN, embryonic development, carcinoma development - alters cell motility so cells get where they don’t belong, wound healing

41
Q

What is required for collagen to deposited at wound sites?

A

FN

42
Q

What are laminins? What is their structure?

A

A family of glycoproteins that are import to the structural scaffold - major proteins of basal lamina - a heterotrimeric multi-adhesive matrix protein - from networks of web-like structures that resist tensile forces - vital for maintenance and survival of tissues, cell differentiation, migration and adhesion - t structure is advantageous to cross linking

43
Q

What do laminins bind?

A

Other ECM components like collagens

44
Q

What diseases result from laminin issues?

A

Congenital muscular dystrophy gives weak muscle, joints and retardation and junctional epidermolysis bullosa (JEB) a skin blistering disease, breast cancer development, neural development - substrate for nerve axon growth

Cell Bio (9 decks)

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