Connect

Question 1

-Provide structural & mechanical support
-elasticity & high tensile strength
- absorbing shock and weight
-cell signaling & adhesion
Network of collagen, glycoproteins, & proteoglycans

Answer 1

ECM

Question 2

-Structural support
-25% of skin weight (type I)
-secreted by fibroblasts
-type III in papillary dermis
Defect cause keloids

Answer 2

Collagen

Question 3

-Absorb shock & resist compression
Has more/ long/ unbranched carbs
-lubricants and support

Answer 3

Proteoglycan

Question 4

Cells producing components of ECM

Answer 4

Chondrocyte

Question 5

-Cell-cell communication
-Immune response 💉
-cell adhesion
-cell surface recognition (signaling)
Has less/ short/ branched carbs🪸

Answer 5

Glycoproteins

Question 6

-Covalently linked to the proteins by N- or O glycosidic bonds
-both containing the same pentasaccharide core but a diverse range of additional sugars🍬
-mannose is the most abundant

Answer 6

Oligosaccharides

Question 7

-formed between sugar & N of Asparagine

Answer 7

N glycosidic bonds

Question 8

Formed between sugar & Serine or Theonine

Answer 8

O glycosidic bonds

Question 9

Glycosylation begins in ER, completed in Golgi

Answer 9

N-link Glycoprotein

Question 10

Glycosylation happens in golgi

Answer 10

O-link Glycoprotein

Question 11

-Absorb shock & Has more/ long/ unbranched carbs
-large complex of negative (carboxyl & sulfate) heteropolysaccharide chains
-repeating disaccharide units (N-acetylated amino sugar)

Answer 11

GAG

Question 12

Providing viscous, lubricating properties of mucous secretions

Answer 12

Mucopolysaccharides

Question 13

-Acetylated Amino group eliminates positive charge
-N-acetylglucosamine (GlcNAc)
-N-acetylgalactosamine (GalNAc)

Answer 13

Amino sugar

Question 14

-Consist of a core protein attached to linear chains of GAGs
-chondroitin sulfate
-keratan sulfate

Answer 14

Monomer structure

Question 15

-Covalent linkages of GAG on protein through a trihexoside & serine residue
-o-glycosidic bond is formed between xylose & the OH group of the Serine

Answer 15

GAGs-protein linkage

Question 16

-Proteoglycan monomers can associate with one molecule of hyaluronic acid to form Proteoglycan aggregates (cartilage)
-stabilized by link proteins

Answer 16

Aggregate formation

Question 17

20% of glucose flows through this pathway

Answer 17

Synthesis of the amino sugar

Question 18

Components of GAGs:
-Glucuronic acid (detox of lipophilic compounds “bilirubin &steroids”)
-iduronic acid

Answer 18

Synthesis of the acid sugars

Question 19

Glycosylate core proteins

Answer 19

Glycosyltransferase

Question 20

GAG
In: Synovial fluid 💦
-vitreous humor 👁️
-ECM, Cartilage
The Only non-sulfated GAG
-Not covalently linking to protein
-Form no Proteoglycan but teams up with it to form aggregates

Answer 20

Hyaluronic Acid

Question 21

GAG💪
In: cartilage, tendon
-ligament, bone 🩻🦴
-skin
-vessels, heart valves🫀
Most abundant GAG
-Not covalently linking to protein
-Forms proteoglycan aggregates🍗

Answer 21

Chrondroitin sulfate

Question 22

GAG
-Extracellular GAG found in basement membranes & cell surfaces
-cell adhesion
-growth factor binding

Answer 22

Heparan sulfate

Question 23

GAG
Component of intracellular granules of mast cells lining the arteries of:
-lungs 🫁
-liver
-skin
An anticoagulant 🩸

Answer 23

Heparin

Question 24

GAG
In: skin
-blood vessels
-heart valves 🫀

Answer 24

Dermatan sulfate

Question 25

GAG In: cartilage -bone🦴 -cornea of the eye 👁️ -loose connective tissue Proteoglycan aggregates with chrondroitin sulfate

Answer 25

Keratan sulfate

Question 26

-cartilage GAG -synovial fluid GAG 💦 surrounded in water molecules -slippery consistency reduces friction -water can be compressed out (bounce back due to negative charges)

Answer 26

Biochemical shock absorbers

Question 27

-Most abundant protein in body -3 long & rigid polypeptides in a rope-like triple helix -rich in glycine & proline Arranged at an angle in bone 🦴 -gel like in vitreous humor 👁️ ECM support

Answer 27

Collagen

Question 28

-Amino acid unique to collagen -used to measure collagen content -y not x -maximize interchain H bonds to stabilize triple helical structure -vitamin C required

Answer 28

Hydroxyproline

Question 29

In RER: Prepro-alpha chain synthesis

Answer 29

Collagen synthesis step 1

Question 30

In RER: Create Pro-alpha chain by removing signal sequence from Prepro-alpha chain

Answer 30

Collagen synthesis step 2

Question 31

In RER: Hydroxylation of proline/ Lysine -requires vitamin C

Answer 31

Collagen synthesis step 3

Question 32

In RER: Glycosylate Hydroxylysine

Answer 32

Collagen synthesis step 4

Question 33

In RER: Form Procollagen triple helix

Answer 33

Collagen synthesis step 5

Question 34

Secrete procollagen into ECM

Answer 34

Collagen synthesis step 6

Question 35

In ECM: Producing Tropocollagen by cleaving procollagen

Answer 35

Collagen synthesis step 7

Question 36

In ECM: Collagen fibrils are formed by Tropocollagen spontaneously associating

Answer 36

Collagen synthesis step 8

Question 37

In ECM: Collagen fiber formed by Lysyl oxidase forming cross-links among fibrils -requires Cu+

Answer 37

Collagen synthesis step 9

Question 38

-subcutaneous leakage of blood 🩸 -capillary fragility -Ecchymoses (bruises) -fail to stabilize triple helix

Answer 38

Scurvy

Question 39

Occurs when: mutations of genes encode alpha chains - abnormal posttranslational modification - deficiency of cofactors present

Answer 39

Collagen degradation

Question 40

Classic EDS & fibrillar

Answer 40

EDS type V collagen

Question 41

Lethal EDS

Answer 41

EDS type III collagen

Question 42

-common connective tissue disorder -alpha 1&2 chain of type I collagen mutation at glycine -blue sclerae due to lack of collagen

Answer 42

OI