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BIOC1011 Molecular Basis of Life > Membranes > Flashcards

Membranes Flashcards

1
Q

Metabolic Functions

A

• Major energy store
• Converted to ketone
bodies in fasting
• Energy production

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2
Q

Structural Functions

A
  • Membrane components

* Protein modification

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3
Q

4 Functions of Lipids

A

1) Structural functions
2) Metabolic functions
3) Cell signalling
4) Precursor molecules

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4
Q

Unsaturated Fats

A

Contain double bonds
‘Un’saturated because double bond kicks out 2 hydrogens
Melting point increase with # of double bonds
Solubility decreases with # of double bonds

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5
Q

Saturated Fats

A

Tail contains as many hydrogens bonded to carbon as possible

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6
Q

Glycerol formula

A 
HO - CH2 - CH - CH2 - OH
                     |
                    OH
*Fatty acid chains bind to alcohol group
- three alcohol groups
- 3 fatty acid tails can bind via ESTER bonds
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7
Q

What type of bond binds fatty acid chains to _______ in triacylglycerol

A
  • fatty acid tail bound to gylcerol OH group

- bound via ESTER bonds

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8
Q

Triacylglycerol

A

TAG = FA triester of glycerol
Most abundant type of lipid.
TAG is neutral but hydrophobic.

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9
Q

Fats Provide: (2)

A
  • 6X the energy of an equal weight of
    hydrated glycogen because of specialized cells called ADIPOCYTES are used to
    store TAG.
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10
Q

Glycerophospholipids

A
  • Also known as PHOSPHOGLYCERIDES
  • Consist of glycerol‐3‐ phosphate with FAs esterified to C1 & C2
  • 2 FA’s + 1 PO4- group
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11
Q

Gycerophospholipid structure

A 
Fatty Acid -------- G
                             L
Fatty Acid -------- Y 
(unsaturated)      C
                             E
                             R ---PO4- ---- OH
                             O              (head group)
                             L
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12
Q

Head groups of glycerophospholipids (5)

A

(GECIS)

1) Glycerol
2) Ethanolamine
3) Choline
4) Inositol
5) Serine

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13
Q

Plasmalogens

A
  • glycerophospholipids
  • C1 substituent linked via ETHER linkage instead of an ESTER linkage.
  • Ethanolamine, choline and
    serine are common head
    groups (X).
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14
Q

Why are Ether bonds found more readily in extremophile bacteria?

A

ether bonds are more resistant to
hydrolysis than the ester bonds of
glycerophospholipids

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15
Q

Sphingolipids

A
  • Major membrane components
  • Derivatives of the amino alcohol
    SPHINGOSINE (SPE)
  • N‐acyl FA derivatives of SPE are called
    CERAMIDES
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16
Q

3 major types of Sphingolipids

A

1) Sphingomyelins
2) Cerebrosides
3) Gangliosides

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17
Q

Sphingomyelins

A
  • Type of sphingolipid

- most common type, ceramides carrying phosphoCHOLINE or phosphoETHANOLAMINE head groups.

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18
Q

Cerebrosides

A 
ceramides with a single sugar as a
head group (glucose or galactose most common).
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19
Q

Gangliosides

A 
most complex, ceramides with
oligosaccharides attached (6% of brain lipid).
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20
Q

Cholesterol

A
  • 4 ringed structure
  • Contains OH group
  • contributes to membrane fluidity
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21
Q

Arachodonic Acid turns into (3)

A

Eicosanoids
Prostoglandin
Leukotreine

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22
Q

NSAID’s

A

Can block the conversion of Arachodonic Acid –> Prostoglandins and/or Eicosanoids

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23
Q

Nucleus:

A

site of DNA and RNA synthesis

a) Nucleoli: ribosome synthesis

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24
Q

Energy converting organelles

A

a) Mitochondria: site of cellular respiration

b) Chloroplasts (plant cells only): photosynthesis

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25
Q

Rough ER

A

ribosome attachment and protein synthesis

1) Attached ribosomes: synthesize secretory, ER, lysosomal, Golgi and plasma membrane proteins.
2) Free ribosomes synthesize: cytosolic, nuclear, mitochondorial and chloroplast proteins.

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26
Q 
Smooth ER:
General functions (2) + Compartment functions (3)
A

1) lipid metabolism
2) packaging of secretory proteins; & detoxification.

1) Drug detoxification by increasing solubility
2) Glycogen catabolism
3) Ca2+ storage

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27
Q

Golgi Complex:

A

processing & packaging newly synthesized proteins and lipids

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28
Q

Lysosomes (animal cells only):

A

Degradation of macromolecules

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29
Q

Peroxisomes: (2)

A

1) generating & degrading H2O2

2) FA oxidation

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30
Q

Vacuoles (2)

A

1) storage

2) plant cell turgidity

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31
Q

Functions of Membranes (5)

A

1) Delineation & compartmentalization ex) plasma & organelle membranes
2) Location of specific function e.g. proteins in specific organelle membranes (ETC in mitochondria).
3) Regulation of transport
4) Detection & transmission of signals
5) Cell‐cell communication

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32
Q

Phospholipid bilayer (4)

A
  1. Forms spontaneously
  2. Composition asymmetric across bilayer
  3. Capable of lateral diffusion but very little
    transverse diffusion (measured by membrane bleaching)
  4. Membrane fluidity is affected by
    temperature & lipid composition
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33
Q

OH of cholesterol binds to (ETHER/ESTER) bond of phospholipid

A

OH binds with ESTER bond on phospholipid

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34
Q

3 types of membrane associated proteins

A

1) Integral proteins
2) Peripheral proteins
3) Covalently associated membrane proteins

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35
Q

Types of Integral proteins (3)

A

1) monotopic (bound inside one leaflet)
2) Singlepass (single a-helix)
3) Multipass (multiple a-helix)
4) Multi-subunit (contains residues)

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36
Q

Functions of membrane proteins (4)

A 
[TREC]
Transport 
Receptors
Cell recognition and adhesion
Electron carriers
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37
Q

NH3+ and COO- placement

A

NH3+ : Outside the cell (extracellular space)

COO- : Inside the cell cytosol

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38
Q

Cell fusion experiment

A
  • showing that membrane proteins have lateral movement capability
  • Flourescently labelled proteins on mouse and human cells
  • Cells fused together
  • membrane proteins mixed together
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39
Q

Radioactive Iodine experiment

A
  • shows that membrane proteins can flip-flop (transverse movement) from inner leaflet to outer, and vis versa
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40
Q

Types of attachment to membrane proteins (2)

3 AA’s they typically attach to

A

1) N-linked attachment
2) O-linked attachment

AST -> NOO attachment

1) Asparagine; N-linked
2) Serine; O-linked
3) Threonine; O-linked

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41
Q

4 common sugars on glycoproteins

A

1) Mannose
2) Galactose
3) Glucosamine
4) Sialic Acid

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42
Q

Passive Transport

A

1) Movement of substance from region of high to low concentration down its concentration gradient
2) No input of energy

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43
Q

Rules for Simple Diffusion

A

CAN PASS

  • Small, uncharged, polar: Water
  • Lipid soluble: O2, N2, anaesthetic

CANT PASS

  • Ions
  • Large, uncharged, polar: Glucose, Sucrose
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44
Q

What can pass the lipid membrane

A

CAN PASS

  • Small, uncharged, polar: Water
  • Lipid soluble: O2, N2, anaesthetic
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45
Q

What CANT pass the lipid membrane

A

CANT PASS

  • Ions
  • Large, uncharged, polar: Glucose, Sucrose
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46
Q

Structure of many anaesthetic

A

Aromatic –Ester/amide link—NR2

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47
Q

How do local Anaesthetics work?

A

1) BH+ –> B + H+
2) uncharged B can move through lipid
3) B + H+ –> BH+
4) BH+ can block Na channels preventing depolarization

patient would be injected with a weak base

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48
Q

Energetics of Transport

Charged vs. Uncharged

A

Uncharged: depends solely on its [ ] gradient

Charged: depends on electrochemical
gradient which is generated by [ ] and
electric charge gradients

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49
Q

Energetics of Transport

A

The free energy change when diffusion of an uncharged species occurs depends on the magnitude of the [ ] difference

deltaG = RT ln[Cin]/[Cout] *x2.3 changes to log10 [Cin]/[Cout]

  • If [Cin]/[Cout] is less than unity influx of solute will be favoured and since log[Cin]/[Cout] is negative, deltaG will also be negative.
  • neg deltaG means equilibrium moves towards 0
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50
Q

Types of facilitated diffusion (2)

A

1) Carrier proteins
2) Ion Channels
a) ion gated channels
b) voltage or ligand gated ‐ neuron function

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51
Q

Types of Ion channels

A

Facilitated diffusion

1) Ion gated channels
2) voltage or ligand gated channels

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52
Q

Classes of transport channels

A

1) Uniport - glucose transporter
2) Co-transport
a) Symport
b) Anti-port

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53
Q

Active transport definition

A

Movement of substances across a membrane against its concentration gradient requires the input of energy.

54
Q

When does active transport allow intake of nutrients and when does it remove nutrients?

A
  1. Allows up‐take of nutrients even when [in]/[out]> 1
  2. Allows removal of molecules even when [in]/[out] <1
    * allows for uptake/removal of nutrients against gradient
55
Q

4 classes of ATP-ion pumps

A
  1. P‐Class
  2. V‐Class
  3. F‐Class
  4. ABC ATPases (ATP binding cassette)
56
Q

P-class Ion Pumps

A
  • On Plasma membrane
  • transporter reversibly phosphorylated to alter conformation
  • e.g. Na+/K+ ATPase
57
Q

V-class Ion Pump

A

‐ found in organelles and vesicles (V); ATP is hydrolyzed and used to generate a proton gradient; no phosphorylation occurs - e.g. lysosomal proton pump

58
Q

F-class Ion Pump

A
  • proton gradient is used to synthesize ATP - e.g. F1‐F0 ATP pump of the mitochondrial inner membrane
59
Q

ABC ATPases (ATP binding cassette)

A

a) Cystic fibrosis‐Transmembrane Conductance Regulator (CFTR)
- Transport of Cl‐
- ATP dependent‐ mechanisms unknown;
common genetic disease

b) Multidrug resistance
- ATP powered export of drugs;
- Some cancers overexpression occurs

60
Q

2 types of Active Transport

A

1) Direct Active Transport

2) Indirect Active Transport

61
Q

Direct Active Transport

A

Energy directly used to move a substance to generate an electrochemical gradient

  • Ex) Na/K pump
  • 3Na out cell ; 2K into cell
  • decreases (+) charge within cell
62
Q

Indirect Active Transport

A

Transport of one substance against its [ ] gradient is coupled to, and driven by,
movement of second substance down its gradient.
- Ex) Na/Glucose pump
- Na high outside cell due to Na/K pump, allows for Na to flow down grandient into cell, and glucose goes against gradient
- no ATP used in this mechanism

63
Q

Enterocyte uptake

A
  • cotransport of Na and glucose
  • indirect active transport from Na/K pump
  • Basal border of enterocyte has passive carrier for glucose transport into bloodstream
  • Na/K continually exports Na
  • high intracellular K has no important features in enterocyte
64
Q

Role of ER in Protein Structure

Site of: (4)

A
  1. Proper folding
    a) Chaperone proteins
    b) Unfolded protein response
  2. Disulphide bond formation
  3. Formation of multi‐subunit proteins
  4. In initial steps in the addition of carbohydrate
65
Q

Chaperones

A

Re-fold improperly folded proteins

If not possible, elicit unfolded protein response

66
Q

Unfolded Protein Response

A

When there are lots on improperly folded proteins, cells elicit unfolded protein response which is apoptosis/blebbing

67
Q

Glycosylation

A

First addition of sugars (N or O-linked) added to the Cis-Golgi Complex

N‐linked on Asn
O‐linked on Ser/Thr

Sugars are continually added throughout GC, sulphication occurs at trans-GC

68
Q

Retention and retrieval of ER proteins

A

Soluble ER proteins are retrieved from cis‐GC via retrograde transport.

  1. Protein binds specific receptor
  2. Triggers retrograde transport
  3. pH of ER lumen dissociates protein‐receptor complex
69
Q

Sorting of Golgi proteins

A
  1. Tag for retention and retrieval.

2. Size of transmembrane domain.

70
Q

Targeting of soluble lysosomal proteins

A
  1. Oligosaccharide tag targets transport.
  2. Mannose‐6‐phosphate added IN Golgi.
  3. Transported to endosome which becomes a lysosome
71
Q

2 types of targeting of secretory proteins

A
  1. Constitutive secretion e.g. ECM glycoproteins
  2. Regulated secretion e.g. insulin and
    neurotransmitters
72
Q

Constitutive Secretion

A

Type of targeting of secretory proteins

a) Secretory vesicles bud from trans‐GC
b) Vesicles fuse with plasma membrane

73
Q

Regulated Secretion

A

Type of targeting of secretory proteins

a) Secretory vesicles bud from trans‐GC
b) Mature vesicles accumulate
c) In response to a trigger (e.g. Ca2+) vesicles fuse with plasma membrane

74
Q 
Targeting of Proteins From
Free Ribosomes (2)
A

1) Nuclear proteins

2) Mitochondrial and chloroplast proteins

75
Q

Nuclear Protein targeting

A

Targeted by a nuclear localization sequence in the protein per se.

76
Q

Mitochondria and Chloroplast targeting

A

Targeted by an N‐terminal signal sequence which is cleaved after import in the organelle.

77
Q

3 Typical Signal Peptides

A

1) Retention in lumen of ER
- (short @ C‐terminal)
2) Import into nucleus
‐ (moderate @ mid)
3) Import into mitochondria
- (long @ N‐terminal)

78
Q

Exocytosis is stimulated by:

A

Ca2+

79
Q

Polarized secretions only occur on the (Basal/Ventral) surface

A

Basal Surface

80
Q

Phagocytosis vs Pinocytosis

A

Phago: ingestion of large particles
Pino: ingestion of extracellular fluid

81
Q

Receptor mediated endocytosis

A

1) Clatherin dependent
2) receptor-ligand complex endocytosed
3) receptor is recycled
4) ligand is hydrolyzed

82
Q

Transcytosis

A

Movement of material across a cell which involves both endocytosis and exocytosis

Movement THROUGH a single cell. Endocytosis on one surface and exocytosis through the other

83
Q

4 types of vesicle formation

A

1) Clathrin
2) COP-I
3) COP-II
4) SNAP/SNARE

84
Q

COP-I

A

Bidirectional between golgi and ER
Retrograde within Golgi
Coat assembly mediated by ARF

85
Q

COP-II

A

Anterograde: RER to Golgi

Sar-1 GTP-binding proteins mediates assembly

86
Q

SNARE hypothesis

A

t-SNARE and v-SNARE interaction
rab GTPase associated with hydrolysis
SNAPs and NSF bind for fusion - driven by ATP hydrolysis

87
Q

Lysosomes (3)

A

1) derived from late endosomes which have inactive enzymes
2) ATP-dependedn proton pump in membrane lowers the pH to 4-5 to activate enzymes
3) contain acid hydrolases

88
Q

Lysosome functions (4)

A

1) Phagocytosis
2) Receptor-mediated endocytosis
3) Autophagy
4) Extracellular digestion

89
Q

Autophagy

A

Degredation of damaged intracellular structures

90
Q

Mammary Secretion process (5)

A

1) Exocytosis (lactose, glucose, ions, etc)
2) Lipid pathway (TAG and P-lipids move from SER to apical membrane)
3) Apical transport (Na, K, Cl, H2O)
4) Transcytosis (move intact proteins [IgA])
5) Paracellular route (Na, Cl)

91
Q

Paracellular

A

Movement in between cells without going through them

92
Q

Endocrine

A

Long travel distance usually via blood between secretory and target cell

93
Q

Paracrine

A

Secretory and target cell are close

94
Q

Autocrine

A

same cell makes and receives signal

95
Q

What do signals do (4)

A

1) Cellular growth rate
2) Metabolism
3) Gene expression
4) Cell fate during development

96
Q

2 types of extracellular signals

A

1) Water-soluble signals

2) Lipid-soluble signals

97
Q

Water soluble signals (examples)

A

Growth factors

Some hormones

98
Q

Lipid soluble signals (examples)

A

Steroid hormones

99
Q

Properties of Membrane Receptors (5)

A

1) specificity for ligand
2) Affinity
3) Conformational change
4) Receptor/Ligand interactions
5) Can be regulated in conditions change

100
Q

G-protein-linked receptor examples (3)

A

1) Rhodopsin
2) Olfactory receptors
3) B-andregenic receptors

101
Q

G-protein linked receptor structure (3)

A

1) 7-transmembrane domains
2) intracellular loop for g-protein binding
3) ligand binding site (extracellular)

102
Q

G-proteins (GTP vs GDP)

A 
GTP = active
GDP = inactive
103
Q

G-protein pathway

A

1) Ligand binds (extracellular)
2) G-alpha releases GDP to GTP (active)
3) G-alpha attaches to protein (creates 2nd messenger)
4) G-beta-gamma binds to separate protein (inhibitory)
5) G-alpha hydrolyzes GTP to GDP (inactive)
6) G-alpha reconnects to beta-gamma

104
Q

3 types of 2nd messengers

A

1) cAMP
2) IP3
3) Ca2+

105
Q

cAMP Signalling

A

1) G-alpha binds to Adenylyl Cyclase (AC)
2) AC converts ATP to cAMP
3) cAMP activates PKA
4) PKA phosphorylates

106
Q

Phosphorylation causes changes in (3)

A

1) metabolism: glycogen synthesis
2) growth rate
3) gene expression

107
Q

Phosphodiesterase

A

Breaks phosphodiester bonds

Breaks cAMP to AMP

108
Q

DAG/IP3, Ca2+ and G-proteins

A

1) G-alpha activates Phospholipase C (PLC)
2) Activated PLC breaks down phospholipid (PIP2) into
a) DAG - Diacylglycerol
b) IP3 - Inositol-triphosphate

109
Q

IP3

A

1) Binds to Ca2+ channels in ER and releases Ca2+
2) Ca2+ bind to Calmodulin regulatory protein
3) Ca2+/calmodulin complex regulates variety of Ca2+/calmodulin dependent kinases
4) these Kinases phosphorylate proteins causing changes in cellular activity

110
Q

Nitric Oxide Mechanism

A

NO activated Guanylyl Cyclase (GC) and creates 2nd messenger cGMP

111
Q

Types of Kinase-Associated Receptors (2)

A

1) Tyrosine Kinase Receptors

2) Serine/Threonine Kinase Receptors

112
Q

Tyrosine Kinase Receptors

A

Autophosphorylation of tyrosine tails
Activates:
a) Phospholipase C pathway
b) Sos/GRB2 pathway

113
Q

Sos/GBR2 Pathway

A

Stimulates Ras pathway
Ras converts GDP to GTP (active)
Ras-GTP activated MAPK pathway (MAPK = nuclear changes)
GAP hydrolyses Ras-GTP to GDP (inactive)

114
Q

Serine/Threonine Kinase Receptors (STK-Rs)

A

Type-II receptor

SMAD and coSMAD is 2nd messenger and enters nucleus

115
Q

Adrenalin acts on (2)

A

Also known as Epinephrine
Secreted from Adrenal gland
Acts on B-andregenic receptor

1) Cardiac Cells
2) Liver cells (hepatocytes)

116
Q

4 aspects of Peptidoglycan layer

A

1) N-acetyl glucosamine (NAG)
2) N-acetyl muramic acid (NAM)
3) Tetrapeptides
4) Inter-bridge peptides

117
Q

3 types of peptidoglycan inhibitors

A

All are antibiotics (i think)

1) Cycloserine
2) Bactitracin
3) Penicillin/Cephalosporin/Vancomycin

118
Q

Cycloserine

A

Inhibits precursor formation
Site: inside cell
Inhibits: L-Alanine –> D-Alanine

119
Q

Bacitracin

A

Inhibits transport and pep. formation
Site: Cell membrane
Inhibits: Transfer of pep.

120
Q

Penicillins/Cephalosporins/Vancomycin

A

Inhibits crosslinking of peptidoglycan

Site: Outside cell

121
Q

B-lactams

A

4-membered cyclic amide ring

inhibit crosslinking

122
Q

B-lactams Antibiotics

Cephlosporins, penicillins, penems, monobactams

A

B-lactams attached to

6-membered ring: Cephlosporins
5-membered ring: Penicillins
5 membered ring: Penems
No rings: Monobactams

123
Q

Cellulose

A

Long unbranched polymer of glucose

124
Q

Pectins

A

Branched polysaccharides - gel like and trap water

125
Q

Extensins

A

Glycoproteins crosslinks to each other and cellulose to provide mechanical support

126
Q

Lignins

A

Insoluble polymer of aromatic alcohols which makes large cross-linked networks in woody tissue

127
Q

Expansins

A

Proteins that mediate cell wall loosening and expansion

128
Q

Sequential sysnthesis of plant cell wall (3)

A

1) Middle Lamella
2) Primary cell wall
3) Secondary cell wall

129
Q

Common Fungal Pathogens (5)

A

1) Dermatophytes
2) Candida
3) Aspergillus
4) Cryptococcus
5) Rhizopus

130
Q

Amphotericin B

A

Creates pores in the membrane of plant cells

131
Q

Echinocandins

A
  • Increase in chitin
  • Kills hyphae at growth tips - buds fail to separate from mother cell (apical meristem)
  • yields osmotically sensitive fungal cells

BIOC1011 Molecular Basis of Life (2 decks)

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