Functions Of Secreted Glycoproteins Flashcards

1
Q

T or F: most extracellular Proteins are Glycoproteins

A

True

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2
Q

What are N-linked sugars attached to?

A

Asparagine (N)

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3
Q

What are O-linked sugars attached to?

A

Serine, Threonine, Hydroxylysine

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4
Q

T or F: Cells that are present in the wrong places in the body will likely die

A

True, e.g. liver cells can’t live in the skin

  • This is due to lack of the appropriate receptors on the liver cell to get the stuff it needs from the environment
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5
Q

How does ebola initiate interactions with endothelial cells?

  • Why not other cells?
  • How does proliferation continue?
A
  1. Finds a coat glycoprotein on endothelial Cells
  2. Cell becomes infected and dies (Hemorrage)
  3. Soluble Glycoprotein blocks early general assault and inflammation (blocks neutrophils)
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6
Q

What is the difference between a glycoprotein and a proteoglycan?

**Note: that proteoglycans are just a subset of glycoprotein

A

Glycoprotein:
low amount of Carbs attached

Proteoglycan:
More sugar and GLYCOSAMINOGLYCAN chains (GAGs) are attached

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7
Q

What is a glycosaminoglycan (GAG)?

A
  • Repeated polysaccharide with alternating amino sugars and acidic sugars
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8
Q

What is one important exception to the fact that all glycoproteins are extracellular and most extracellular proteins are glycosylated?

A

Albumin - abundant Serum Transport Protein

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9
Q

What are lectins?

A

Carbodydrate binding proteins for:

  • cell attachment
  • immune response
  • lung surfactant
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10
Q

What glycoprotein is involved in copper binding and transport?

A

Ceruloplasmin

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11
Q

What is N-acetyl-glucosamine?

A

Glucose Ring Derivatized at the 2-position

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12
Q

T or F: Sialic acid is aka as N-Acetylneuraminate (NANA)

A

True

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13
Q

What is glycosylation?

A
  • The process of transferring an oligosaccharide to a protein
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14
Q
******************************
N-linked Glycosylation:
- Where does it occur?
- When does it happen
- How does it happen?
A

Where:
- Starts in Rough ER and is finished in the Golgi

When:
- AS the Polypeptide is being synthesized

How:
- Preassembled oligosaccharide is transferred to the appropriate Asparagine

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15
Q

What sequence gives consensus for N-linked glycosylation?

A

Asn-X-Ser/Thr

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16
Q

T or F: from yeast to man, the preassembled oligosaccharide is always the same

A

True

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17
Q

Dolichol:

  • What is it?
  • Bond Type?
  • Predominant Sugar?
A
  • Dolichol is a carrier of the universal pre-assembled oligosaccharide
  • Linked to the Oligosaccharide via a diphosphate bond
  • Mannose and Glucose are Predominant in this molecule
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18
Q

When can a preassembled oligosaccharide be transferred from Dolichol to another protein?
- Bonds Broken and Formed?

A
  • Transferred to Asn-X-Ser/Thr

- Disulfate bond to Dolichol is broken, and N-glycosyl bond is formed

19
Q

Where does Dolichol transfer the oligosaccharide to proteins, where is Dolichol located?

A
  • Dolichol present in RER membrane transfers Oligosaccharide to and Asn In the RER LUMEN
20
Q

If all N-glycolsylated proteins start off with the same oligosaccharide attached how do they differentiate?
- where does this occur

A

Remove:

  • Glucoses
  • Mannoses

Add:

  • Galactose
  • Sialic Acid
  • Fructose

**Occurs as the protein passes from the ER to the Golgi

21
Q

T or F: O-linked glycosylation occurs one sugar at a time

22
Q

What adds glycosyl groups in O-linked glycosylation?

- substrate for these enzymes?

A
  • Glycosyl Transferases Used

- Sugar Nucleotide (e.g. UDP-Gal) are used

23
Q

What is the job of fibronectin?

A
  • Binds Both Cells and Extracellular Matrix Molecules (e.g. Collagen)
24
Q

What does the structure of fibronectin consist of?

A
  • Dimer (2 similar subunits)

- Joined by Disulfide Bond at C-terminal

25
How many many Fibronectin Genes are there? | - How many isoforms
1 Gene 3 Isoforms **Alternate splicing allows for this
26
What modules are in Fibronectin? | - Function
- Globular Polypeptides that are like beads on a string - Each "Bead" has a different function Module Functions: 1. Cell (Integrin) Binding 2. Collagen Binding 3. Heparan Sulfate Binding 4. Fibrin Binding
27
What is Laminin?
- Similar to Fibronectin (binds different things together) - formed in basal lamina (glycoprotein)
28
What is aggrecan?
- Glycoprotein that forms a shock absorbing aggregate
29
What are 3 main functions of glycoproteins?
1. Comprise Recognition Signals 2. Intracellular Trafficking 3. Building Protein-Protein Interactions for CT scaffolding
30
What happens if glycoproteins loose too many of their glycosylations?
- They loose their water solubility and fallout of solution | - PROTEASES then degrade these
31
T or F: glycosylation protects glycoproteins from degradation
True
32
What happens if 2 of the 10 sialic acids are removed from the glycosylated portion of ceruloplasmin?
Half Life Deceases by 700x
33
What is Beta-glycan?
Transmembrane glycoprotein: | - Hormone Receptor for transforming growth factor-beta
34
Integrins: - What do they do? - How do they do it?
What they do: Transmembrane Glycoproteins that mediate Cell-matrix binding How: - Binding ECM protein to allow cells to grip a given surface
35
T or F: most cells must be anchored to ECM by integrin to be viable
True, keeping the cell bound to ECM keeps it in contact with cell survival signals
36
What is a cadherin?
Ca2+ dependent Adhesion Molecule
37
If you chop up liver and retina cells and mix them what will happen an why?
- Retina Cells will aggregate with each other and Liver cells will aggregate with other liver cells - This happens because of specific Cell-Cell interactions that only occur between cells of the same type
38
What role do glycoproteins play in fertilization of an egg by sperm?
1. Capacitation - sperm alters is membrane glycoprotein and gal-transferase recognizes egg 2. Zona Pellucida (glycoproteins) act as a sperm receptor
39
What role do glycoproteins play in the extravasation of white cells?
1. Selectins present on endothelial cells and bring white cells to a rolling stop 2. Integrins then grab onto the cell tighter and it is pulled through the endothelium (extravasation) **Leads to an inflammatory Response
40
Why would you want to inhibit selectin that is used in extravasation?
- Extravasation leads to inflammation - After a heart attack inflammation is bad and can cause additional damage **No selectin, then no extravasation
41
What is needed to target a protein to a Lysosome?
- Glycoprotein with a PHOSPHOMANNOSE
42
What happens if PHOSPHOMANNOSE can't be added to a protein?
- It will not get targeted to lysosome - This can cause accumulation of macromolecules in Lysosome (e. g I-Cell disease and ß-glucuronidase)
43
T or F: sugars in glycoproteins are covalently attached
True