Glycoproteins Flashcards

1
Q

What is a Glycoprotein?

A

a protein with covalently attached carbohydrate (saccharides); Tends to be used to refer to proteins with lower carbohydrate content, but there is a wide variability

Ubiquitionous extracellular proteins that carry out many body functions.

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2
Q

What is a proteoglycan?

How does their carbohydrate content compare with glycoproteins?

A

Glycoproteins with glycosaminoglycan chains (GAGs).

Proteoglycans tend to have a higher carbohydrate content than glycoproteins.

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3
Q

Where are most glycoproteins located?

Are there any exceptions?

A

Almost all glycoproteins are extracellular, and most extracellular proteins are glycosylated.

Yes, ;Albumin - abundant serum transport protein, is not glycosylated.

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4
Q

How many glycoproteins exist?

Name 5 common glycoproteins

A

A tremendous number of glycoproteins exist.

  • *1. lectins** (carbohydrate binding proteins for cell attachment, immune response, lung surfactant, sperm-egg binding).
  • *2. Ceruloplasmin** copper binding & transport.
  • *3. Immunoglobulin,**
  • *4. collagen,**
  • *5. fibronectin**
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5
Q

How are sugars linked to glycoproteins?

What are common sugars that are used as building blocks of glycoproteins?

A

These sugars can be linked by enzymes through many of their hydroxyl groups to form oligosaccharides that are transferred to the protein in the process of glycosylation.

  1. Mannose
  2. N-acetyl Glucosamine
  3. Sialic Acid
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6
Q

Where, When, and How does glycosylation occure?

A

WHERE: In the lumen of the R.E.R. (rough endoplasmic reticulum)

WHEN:; As the polypeptide is being synthesized

HOW: A preassembled oligosaccharide is transferred to a an appropriate Asparagine in the sequence …[ASN-X-Ser/Thr]

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7
Q

What is glycosylation?

A

Glycosylation - the process of biosynthetically sugar coating proteins:
N-linked oligosaccharides

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8
Q

How are oligosaccharides preassembled?

Is this process conserved throughout species?

A

A preassembled oligosaccharide on a dolichol carrier.

Yes

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9
Q

Where is the preassembles oligosaccharide transfered to?

Where and when does this happen?

A

The preassembled oligosaccharide is transferred to an acceptor ASN in the sequence
ASN-X-SER/THR

In the lumen of the rough endoplasmic reticulum as the protein is being synthesized

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10
Q

Where does the growing peptide accept the oligosaccharide?

A

In the lumen of the rough endoplasmic reticulum

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11
Q

Is the N-Linked oligosaccharide enzymatically modified before release from the rough endolasmic reticulum?

A

The final form of N-linked sugar is dependent on modifying enzymes that trim off sugars and add sugars so that there are a large variety of oligosaccharides possible.

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12
Q

Are all the N-Linked olligosaccharides initially the same?

A

even though all N-linked oligosaccharides are initially the same modifications change the final oligosaccharide.

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13
Q

Provide an example of N-Linked olligosaccharide modification

A

E.g. glucoses and some of the mannoses are removed, and galactose, sialic acid, and fucose can be added.

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14
Q

Olligosaccharides are modified by the __________ removal and addition of sugars

A

SEQUENTAL

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15
Q

Where is the N-Glycosylated protein altered to its final form?

A

The Golgi gives glycosylated proteins increasingly more complex sugar modifications. The final modification being sialic acid.

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16
Q

Where are the sugan molecules attached to the protein?

A

Sugars of glycoproteins are attached to the amino acid side chain of the asparagine side chain making them N-linked olligosaccharides.

The Hydroxyl group of the sugar is linked to the N in the asparagine residue in the protein sequence.

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17
Q

How are glycoproteins glycosylated?

A

A preassembled, dolichol phosphate-oligosaccharide is transferred to asparagin (ASN or N) in a
-ASN-X-SER/THR- sequence.

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18
Q

Name the key differences between O-Linked Glycosylation and N-Linked Glycosylation

A

O-Linked glycosylation utilizes glycosyl transferase molecules to sequentially add (ex. UDP-Gal) to the acceptor hydroxylated amino acids.

O-Linked glycosylation links sugars to serine and N-liked glycosylation covalently attaches preassembled sugars to ASN molecules.

Glycosyl transferase molecules use sugar nucleotides as a substrate

19
Q

What is O-Linked Glycosylation?

What kind of molecules have O-Linked Sugars?

A

Takes place with specific glycosyl transferases using sugar molecules ie UDP-Gal to acceptor glycosylated aminoacids.

Proteoglycans

20
Q

What is the structure and function of fibronectin?

Describe its structure?

How many forms are made? How many genes code for fibronectin?

A

Fibronectin binds cell surface molecules (such as integrin) with extracellular macromolecular structures (such as collagen)

Its structure consists of a dimer of two subunits joined by disulfide bonds at the C-terminus

3 formes are made from one gene

21
Q

What functional regions does a fibronectin molecule have? (name 4)

A
  1. Collagen binding
  2. Fibrin Binding
  3. Heprin BInding
  4. Cell Binding
22
Q

Are N-Linked and O-Linked Olligosaccharides both glycoproteins?

A

YES

23
Q

Are most extracellular matrix proteins Glycoproteins?

Name 6 major types

A

Yes most extracellular matrix proteins are glycoproteins

coagulation proteins, collagen, fibronectin, laminin, aggrecan

24
Q

What are the three main functions of glycoproteins?

A

Solubility, protection, and recognition

25
Q

How do glycoproteins work in recognition?

(Name 5)

A

Glycoproteins comprose recognition proteins for many areas of the body.

  1. receptor ligand binding,
  2. host defense,
  3. intracellular protein trafficing,
  4. binding protein protein interactions
  5. connective tissue scaffolding
26
Q

How do glycoproteins function in protection and solubility?

A

Protection- Glycoproteins can bing integrins on the cell surface and prevent proteases from gaining access to the cell and degrading it.

Solubility- Glycoproteins can add structural integrity to the surface of the molecule thus holding it together and precenting it from being falling apart rendering it insoluble

27
Q

What is the major recognition function for glycoproteins?

A

Beta Glycan, a hormone receptor, is a transmembrane protein that regulates growth factor beta

Integrins are cell surface receptors for the extracellular matrix. Integrins are transmembrane Glycoproteins can mediate cell matrix binding

28
Q

What are Cadherins

A

Cadherins are calcium dependent signaling molecules that mediate cell-cell interactions such as interations of like populations of cells.

29
Q

What is the role of glycoproteins in fertilization?

A

The Zona Pellucida is made of glycoproteins and can act as a barrier OR a sperm receptor

Functions in sperm capication which alters the membrane glycoprotein and gal transferase recognizes the egg.

30
Q

Name the recognition functions of Glycoproteins.

A

**Selectins **

The extraversion of white blood cells allow them to pass through the epithelium. Selectins are glycoproteins that recognize sugars and allow WBC’s to adhere to the epithelieum.

31
Q

What happens if you inhibit selectin?

Provide a clinical example in relation to heart attacks

A

Inhibiting selectin will inhibit extravasation.

Anti-P-Selectin can be administered after MI to prevent extravasation and thus prevent damage to the ischemic region of the heart.

Protects the heart from leukocyte induced damage.

32
Q

How can glycoproteins be targeted to the lysosome?

A

Mannose-6-Phosphate tag

33
Q

How do glycoproteins get out of the cell? What makes up the majority of proteins secreted by the cell?

A

Glycoproteins pass through the Golgi and are exported via constituted and regulated secretion. The majority of exported proteins are glycoproteins.

34
Q

The sugar saccharides on glycoproteins have many Biological functions including: recognition, controlling protein lifespan, and as a recognition signal for intracellular sorting.

T/F

A

True

35
Q

Most serum proteins are glycosylated (T/F)?

A

True

36
Q

Proteins with covalently attached carbohydrates are called peptidoglycans?

A

False

37
Q

I-Cell Disease is due to a problem in proper glycosylation of certain proteins (T/F)?

A

TRUE mothafucka

38
Q

Examples of sugars in N-Linked Oligosaccharides are ribose, araribose, infraayanose (T/F)?

A

False

39
Q

The initial transfer of preassembled oligosaccharide units to an acceptor ANS-X-SER asparagine occurs in the lumen of the endoplasmic reticulum (T/F)?

A

True

40
Q

Dolichol Phosphate is a versitile carbohydrate carrier molecule in that it must be able to carry all of the wide variety of oligosaccharide in pre-assembled form. (T/F)

A

False

41
Q

Fibronectin is a proteoglycan?

A

False

42
Q

More than one fibronectin can be derived from one gene?

A

True

43
Q
A