protein function 2 Flashcards

1
Q

what are the glycoproteins covalenty linked to?

A

oligosaccharides or polysaccharide

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2
Q

what is the weight of the glycoproteins?

A

10-15

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3
Q

what is the function of the glycoproteins?

A

protects the cell awl

cell adhesion

cell specialisation

prevent aggregation-protein folding

recognises chaperone

acts as a protease resistance

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4
Q

where is the N-linked glycosylation glycosylated in?

A

ER lumen

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5
Q

where is the O-linked glycosylation glycosylated in?

A

Golgi lumen

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6
Q

what does dolichol phosphate enable?

A

flipping

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7
Q

what does the dolicho phosphate function and bind to?

A

spans the bilayer and binds the activated sugars

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8
Q

what does the oligosaccharyltransferase glycosylates?

A

protein- happens in the secretory pathway

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9
Q

what are the stages of glycoprotein degradation?

A
  1. endocytosis to lysosome
  2. protein degrades- proteases
  3. remove sugars- lysosome glycosides
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10
Q

what is lysosomal storage diseases?

A

undigested substrates in the lysosomes.

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11
Q

what is inclusion cell diseases I- cell disease caused by?

A

defective phosphotransferase- enzyme in Golgi apparatus

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12
Q

what isInclusion-cell disease (I-cell disease) mutation?

A

recessive mutation in GNPTAB

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13
Q

what does glycosaminoglycans contain?

A

unbranched polysaccharides with amino sugars and acidic disaccharide repeats

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14
Q

what is an example of glycosaminoglycans ?

A

hyaluronan

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15
Q

what are proteoglycans?

A

glycoproteins with GAGS

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16
Q

what happens in the GAG assembly on proteins?

A
  1. tetrasaccharide is added to the serine in the golgi lumen
  2. repeats are then added one sugar at a time
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17
Q

what is the function of GAGS?

A

lubricates in the CT

cell adhesion to extracellular matrix

binds to cell proliferation factors

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18
Q

what are the stages of glycosaminoglycans degradation?

A
  1. endocytosis
  2. removes sugars
19
Q

what is the hurler disease?

A

deficiency of the lysosome enzyme

20
Q

what is the mutation of the hurler disease?

A

IDUA defect

21
Q

what does IDUA defect in hurler disease encode?

A

alpha-L- iduronidase

22
Q

what happens in a hurler disease?

A

GAGS are not degraded

enlarged lysosomes

excessive lysosomes stored in the facial soft tissue

23
Q

what are the symptoms of hurler disease?

A

build up of fluid in the brain

enlarged liver, spleen

decline in intellecular function

abnormalities in the heart valve

large head

24
Q

what are biogenic amines?

A

small organic nitrogen containing molecules that are synthesised by amino acids

25
what are the classes of biogenic amines?
1. aromatic and heterocyclic 2. aliphatic mono-, di-, tri and poly amines 3. aliphatic volatile amines
26
what are the functions of biogenic amines?
stabilises the cell membrane synthesis of protein and nucleic acids hormones neural transmission
27
what are the steps of biogenic amines synthesis?
1. decarboxylation of the amino acids 2. amination and transamination of aldehydes and ketones
28
what is serotonin used for
is a biogenic amine as it is present via tryptophan decarboxylase hormones - causes relaxation, memory and pleasure
29
what is nictinoamide unit of NAD+?
it is a vitamin B3 - coenzyme it is used for the production of energy.
30
what is epinephrine and what is it used for?
adrenalin used for hormone, flight or fight response and neurotransmitters
31
what Is thyroxine and what is it used for?
thyroid gland hormone it is used for brain development, muscle control and metabolic rate and maintenance of bones.
32
what is biogenic monoamine neurotransmitters synthesised from?
amino acids
33
what are the steps involved in the catecholamine synthesis?
1) 5-hydroxytryptamine (5-HT) - hydroxylation and then decarboxylation of tryptophan 2) Histamine - decarboxylation of histidine 3x Catecholamines: - Tyrosine hydroxylated to Dihydroxyphenylalanine (DOPA) 3) Dopamine - decarboxylated DOPA 4) Norepinephrine (noradrenaline) - β-hydroxylated dopamine 5) Epinephrine (adrenaline) - methylated noradrenaline
34
what are the key elements involved in the amine oxidases?
Enzymes Monoamine oxidases (MAO) Catechol-O-methyltransferase (COMT)
35
what are the cosubstrates involved in the amine oxidases?
S-adenosyl-L-methionine (SAM) Prosthetic group Flavin adenine dinucleotide (FAD)
36
what is an example of amine oxidases?
Monoamine oxidases (MAO)
37
what does Monoamine oxidases (MAO) require?
Prosthetic group Flavin adenine dinucleotide (FAD)
38
what are examples of deficiency caused by build-up of biogenic amines- degradation?
Vitamin B12 monoamine oxidases A inflammatory bowel disease
39
what is vitamin B12 deficiency?
it is a deficiency that required FAD as if they is a lack of it in the body that it leads to a dysfunction of the monoamine oxidases.
40
what are the symptoms of vitamin B12 deficiency?
tiredness disturbed vision psychological problems
41
what is a monoamine oxidases A deficiency?
occurs when they is a build up of serotine in the body
42
what is the symptoms of monoamine oxidases A deficiency?
loss of impulse control
43
what is a inflammatory bowel deficiency?
it is when they is a increased activity of the monoamine oxidases
44
what are the symptoms of the IBD?
causes oxidative stress which leads to vascular damage.