Block 3 Flashcards
(213 cards)
1
Q
Amphiphathic
A
Hydrophobic/Nonpolar & Hydrophilic/Polar
2
Q
Outer Leaflet (Faces extracellular matrix)
A
Glycolipids, Glycoproteins, Proteoglycans
3
Q
Phosphatidylserine involved in what type of signal?
A
apoptosis
4
Q
what recognize phosphatidylserine when its flipped to the outer leaflet?
A
macrophages
5
Q
what forces hold the leaflets together
A
van der waals
6
Q
Flip-flop requires
A
Flippases and Scrambalases
7
Q
flippases characteristics?
A
phospholipid specific
8
Q
scrambalases characteriscs?
A
Non-specific scrambling
• In smooth ER membrane: mix up newly synthesised phospholipids
• Activated during apoptosis
9
Q
what Increase Fluidity in membranes?
A
Unsaturated Fatty Acids (More
cis-double bond kinks)
• Increase temperature
• Short chains
10
Q
what Decrease Fluidity in membranes?
A
Saturated Fatty Acids (NO
double bond kinks)
• Decrease temperature
• Long chains
11
Q
Lipid Rafts
A
Rich in Cholesterol & Glycosphingolipids,
Contain integral & peripheral membrane proteins, GPI: Glycosylphosphatidylinositol anchor
12
Q
GPI: Glycosylphosphatidylinositol anchor
A
Glycolipid that attaches proteins to PM
13
Q
Membrane Protein Functions
A
Transport (nutrients, metabolites, ions across bilayer)
• Anchor membrane to macromolecules on either side
• Receptors: signal transduction
• Enzymes (lactase in apical membrane of GI epithelial cells)
• Cell identity markers: MHC
• Protein movement: Rotational and lateral diffusion
14
Q
Integral transmembrane proteins (30% total proteins, amphipathic)
A
Single: (Glycophorin) /Multipass: (Band3) proteins
• Often α-helical in secondary protein structure
• Receptors (signalling & adhesion), channels, transporters/pumps
15
Q
Peripheral proteins
A
Located entirely outside but associated with inner / outer leaflet by noncovalent
(often electrostatic) interactions
• Part of cytoskeleton, cytochrome C
16
Q
Lipid-anchored (peripheral) proteins
A
Located either side of bilayer, have lipid group that inserts into bilayer
• Signaling (Glycosylphosphatidylinositol: GPI – Outer Leaflet) &
Adhesion (Fatty acylation or prenylation link proteins – Inner Leaflet)
17
Q
Red Blood Cell Membrane main characteristic
A
no nucleus
18
Q
Two types of Transmembrane proteins present in RBC?
A
glycophorin and Band 3
19
Q
glycophorin
A
single pass transmembrane protein present in rbc
20
Q
Band 3
A
Multi pass transmembrane protein in rbc
21
Q
Peripheral proteins in rbc?
A
Ankyrin and Band protein 4.1
22
Q
Ankyrin
A
Connects Band 3 with spectrin
23
Q
Band Protein 4.1:
A
Connects Glycophorin with Actin and also
connects Band 3 with Spectrin “BAG of BS”
24
Q
Cytoskeletal protein of rbc
A
spectrin
25
spectrin
(α & β chains) that reinforces bilayer, deformable
| network, and can withstand stress
26
Junctional Complex on rbc
4-5 tetramers of Spectrin held together by Actin and
| Protein 4.1 “SAP”
27
Acanthocytosis / Spur Cell Anaemia mechanism?
```
Increase Cholesterol (Transferred to outer leaflet)
defects RBC cell membrane → Acanthocytes →
Decreased deformability → Sequesration and
destruction by spleen → Haemolytic Anemia
→Increase Reticulocytes
```
28
Acanthocytosis / Spur Cell Anaemia key words to look for
Jaundice, Ascites, Caput Medusa, Chronic Liver
| Disease, Acanthocytes, Spur Cells
29
Acanthocytosis / Spur Cell Anaemia cell biology
```
Decreased Fluidity:
Increased cholesterol
Saturated fatty acid tails (No cis-double bonds)
Long fatty chains
Decreased Temp
```
30
Hereditary Spherocytosis inheritance pattern?
Autosomal dominant in 75% of cases
31
Hereditary Spherocytosis mechanism
Defect Spectrin, Ankyrin, Protein 4.1 defects RBC
cytoskeleton membrane → Decreased
deformability → Sequesration and destruction by
spleen → Haemolytic Anemia →Increase
Reticulocytes
32
Hereditary Spherocytosis key words
Splenomegaly, Jaundice, Gallstone
| Spectrin, Ankyrn, Protein 4.1
33
Hereditary Spherocytosis cell biology
Spectrin: Cytoskeletal protein that forms junctional
complex
Ankyrn: Peripheral protein that connects Band 3
(multipass transmembrane protein) with spectrin
Protein 4.1: Peripheral protein that connects
Glycophorin with Actin and also connects Band 3
with Spectrin
34
Glycocalyx
5% cell membrane = carbohydrate (prrimary marker for cell recognition)
35
Glycocalyx function in the cell
Protection (from acid, enzymes, etc.)
• Recognition (leukocyte binding to endothelial wall) & Cell adhesion
• Repulsion: negative charges from sialic acid sugars
• Embryonic development: guides embryonic cells to destination
36
how glycocalyx differ in cancer cells than on normal cells?
different sugar coat than noncancerous cells, Immune defense: recognizes difference
37
Anti-cancer therapy and glycocalyx
target enzymes that assemble tumor Glycocalyx
38
Electin
important for binding to sugar chains involved for cell to cell
recognition
39
L-selectins recognise?
addressins on lymphoid organ endothelial cells
40
G protein Cycle
The GTP “switch”
41
Small monomeric G proteins
RAS, RHO, RAB, RAN, ARF
42
Every G protein has what in coomon?
GAP and GEF
43
GAPs
GAPs: “Turns OFF” Hydrolyze GTP to GDP “GAP turns me OFF”
44
GEFs: guanidine nucleotide exchange factor
“Turns ON” Exchange GDP for GTP “GEF turns me ON”
45
Nuclear Import
process that imports cargo from the cytosol into the nucleus
46
cargo protein that is destine to go into the nucleus contains?
Nuclear Localization Signal (NLS)
47
Importin
(Import receptors in cytosol) binds NLS & nucleoporins:
| Imports
48
nuclear export
process to carry cargo from the nucleus to the cytosol. such as ribosomes or mrna
49
cargo protein that is destined to go out of the nucleus contains what?
Nuclear Export Signal (NES)
50
Exportin
(export receptors in nucleus) binds NES & nucleoporins:
| Exports
51
Import & Export require what?
Translocation of protein complexes through NPC requires energy
(RAN GTPase)
52
Nuclear Import steps
```
1. Importin binds to Cargo w/
NLS in cytoplasm
2. Cargo-Importin binds to NPC to
enter the nucleus
3. Ran-GTP binds to Importin thus
creating dissociation of Cargo
in nucleus
4. Importin-GTP enters cytoplasm
5. Ran-GAP hydrolyzes Ran-GTP
→ Ran-GDP thus creating
dissociation of Importin in
cytoplasm
```
53
nuclear export steps
```
1. Exportin bound Ran-GTP binds
to Cargo w/ NES in nucleus
2. RanGTP-Exportin-Cargo complex
binds to NPC enter cytoplasm
3. Ran-GAP hydrolyzes Ran-GTP →
Ran-GDP thus creating
dissociation of Exportin, Cargo,
and Ran-GDP
4. Exportin returns back to nucleus
(Does NOT need signal to return
back to nucleus)
```
54
Ran GEF
```
• Guanidine Nucleotide
Exchange Factor
• ON SWITCH
• Exchange GDP with GTP
• In nucleus
```
55
Ran GAP
* GTPase Activating Protein
* OFF SWITCH
* Hydrolyze GTP to GDP
* In cytosol
56
related to the nuclear envelope, what triggers the start of mitosis
Lamin phosphorylation
57
when is lamin phosphorylated and which kinase does the job?
during prophase 1 by Cdk1
58
what is the result of the phosphorylation of lamins?
nuclear lamina disassembly
| → nuclear envelope disassembly into vesicles containing Lamin B
59
how are lamins A, B and C released after phosphorylation?
Lamins A & C released as free dimers
| • Lamin B = anchored to inner membrane
60
what triggers the end of mitosis? by what process?
Lamin Dephosphorylation → Inactivation of Cdk1
61
process of nuclear reassembly after mitosis?
* Membrane vesicles bind chromosome surface → reassembly
| * Telophase: Lamin A and C start to bind again to lamin B
62
nuclear membrane outer layer is continous with what other organelle?
Rough ER
63
On the outer membrane of the nucleus are proteins that interact with what?
cytoskeletal fillamets
64
function of nuclear lamins?
Maintain structure & stability:
attaches to integral membrane
proteins & NPCs (important for
spatial separation), protects DNA
65
Nucleolus substructures
Fibrillar center, Dense fibrillar components / pars fibrosa “Fibrillar Fix”, Granular component / pars granulosa “Great Assembly”
66
Fibrillar center of nucleolus
* Transcriptionally inactive DNA
| * NORs (Nucleolar Organiser Regions: pre-rRNA genes located)
67
Dense fibrillar components / pars fibrosa
"fibrilar fix" •rRNA being transcribed then cleaved & modified by snoRNPs
68
Granular component / pars granulosa
“Great Assembly”
| •rRNAs begin assembly with ribosomal proteins
69
Hutchinson-Gilford Progeria Syndrome inherritance pattern?
(Autosomal Dominant Sporadic)
70
Hutchinson-Gilford Progeria Syndrome mechanism?
“progeriA defect lamin A”
Defect in ONLY Lamin A → Unstable Nuclear Envelope (Bleb
formation, Loss of peripheral heterochromatin, NPC clustering)
→ Progressive Nuclear Damage → Premature Cell Death
71
Hutchinson-Gilford Progeria Syndrome key words
“Premature Aging”
Lamin A, Prominent eyes, Alopecia (Loss of hair), Loss of
subfat, Arteriosclerosis, Joint stiffness, Accelerated age, Bleb
formation
72
Hutchinson-Gilford Progeria Syndrome cell biology
Arteriosclerosis: Scarring of vesicles and become hard
73
co-translation translocation meaning
transport into the ER
74
Post-translational translocation?
transport into other organelles
75
Emery-Dreifuss muscular dystrophy
| affect which part of the cell?
Nucleus
76
Emery-Dreifuss muscular dystrophy
| what type of effect on the organelle it affects?
```
Mutation Emerin or LaminA/C
Contractures, especially in the elbows, ankles, neck → Flexion deformity of elbows, limited neck flexion
Muscle weakness & atrophy
Conduction defects & arrhythmias
Sudden heart failure common
```
77
Cotranslational Translocation steps
1. Signal Recognition Particle (SRP) binds to ER signal sequence
on protein
2. SRP binds to SRP receptor in ER membrane
3. SRP brings ribosome to translocon (pore complex) and transfers the
ribosome
4. SRP displace and recycled
78
BiP (Binding Protein):
Lumenal ER chaperone (help proteins fold)
| and binds peptide in ER lumen & pulls it in
79
Signal peptidase cleaves what off
N-terminal signal peptide as protein
| enters ER lumen
80
what doenst get cleaved during cotranslational translocation?
the internal sequences of proteins
81
Single-Pass Transmembrane Proteins, N-terminal signal sequence job
(Start Transfer signal) initiates
| translocation (Gets Cleaved)
82
Single-Pass Transmembrane Proteins, Stop Transfer signal job
Anchors protein in membrane AFTER ER signal sequence is cleaved
83
Single-Pass Transmembrane Proteins, Internal signal sequence job
(start transfer signal) initiates
| translocation (NOT cleaved)
84
Multipass transmembrane proteins
• Internal signal sequence (start transfer signal)
• Stop transfer sequence
• The multiple stop signals
→ Many hydrophobic α-helices cross the membrane
85
If a protein has an N terminal ER signal sequence, and two additional
hydrophobic stretches of amino acids, what type of protein is this?
Transmembrane
86
If a protein has an N terminal ER signal sequence, and two additional
hydrophobic stretches of amino acids, where will the C terminus of the protein be located?
ER lumen
87
r ER fuction
Produces proteins destined for the ER, Golgi apparatus, endosomes, lysosomes, plasma membrane, & for secretion
88
what do Free ribosomes synthesise
all other proteins & discharge in cytosol
| (proteins targeted to nucleus, mitochondria, peroxisomes; post-translational translocation)
89
Dolichol
is a membrane bound lipid that attaches 14 sugars to asparagine nonspecifically on proteins in the rER
• “N-linked: Asparagine.
2) the 14 sugar oligosaccharide gets assembled temporarily on it. It serves as an achor so when the protein gest made the sugar string is made and transferred to the nitrogen of the asparagine AA.
90
Oligosaccharide Processing in the ER
4 sugars removed from the N-linked precursor oligosaccharide (still in the
ER) signals time to move to Golgi
91
Glycosylation: Important for?
correct folding, transport, and function
92
O-Linked: Hydroxyl?
Processing of proteins that continues in Golgi (Specificity) after N-glycosylation in the ER
93
where does O-Linked: glycosylation of collagen takes place?
in the ER
94
where does protein without ER signal sequence end up?
in the cytosol
95
where does protein with NLS signal sequence end up? and what AA sequence they are?
in the nucleus
| Asp, Leu, Ser
96
where does protein with SKL signal sequence end up? and what AA sequence they are
peroxisomes,
| Ser, Lys, Leu
97
where does protein with mitochondrial signal sequence end up? and what AA sequence they are
mitochondria
98
where does protein with KDEL signal sequence end up?
ER, soluble
| "KDEL is solubel"
99
where does protein with KKXX signal sequence end up?
ER (transmembrane) where XX is any amino acid
100
where does protein with M6P signal sequence end up?
Lysosome
101
where are the default destinations for proteins with no signal sequence?
plasma membrane and for secretion
102
If a protein has an ER signal sequence and one internal stop transfer
sequence (no other sequences or tags) where will it end up? why?
In the plasma membrane (cell surface) WHY b/c it has no KDEL or KKXX
103
exocutosis
deliver proteins to plasma membranes and extracellular space
104
two tyupes os secretion
constitutive and regulated secretion
105
constituitive secretion
proteins are secreted as soon as they are made. examples are trans-membrane proteins
106
regulated secretion
vesicles are ready and docked to the plasma membrane and waiting for a signal molecules to tell them to be secreted.
107
how regulated secretion work
vesicles are charged with proteins to be delivered, signal comes com outside the cell, opens calcium ion channels that allows calcium to rush into the cell and interact twith the vesicle allowing it to fuse to the membrane
108
how vesicles endup in the lysosomes?
M6P signal
109
transcytosis
combination of endo and exocytosis. example: maternal IgG antibodies in breast milk are transported across intestinal epithelial cells
110
processing in secretory vesicles
concentration of proteins and transport recycled from endosomes back to golgi
111
progressive acidification allows for
activation of enzymes that will modify proteins contained into the vessicles
112
pre-pro-proteins
example: proalbumin to albumim
113
whats included in the recycled vesicles going back to the golgi
cargo receptors which will go back and pick up more cargo
114
RAB-GTP
regulates initial docking and binding of SNAREs. GTP hydrolyses to GDP
115
SNARE
proteins that provide specificity v-SNARE and t-SNARE
116
v-SNARE
interact with v-snare to form complex
117
synaptoragmins
calcium ion channels that open to allow calcium to go in the cell that allow v and t snares to fuse and let the vesicle bind the membrane and move on to the exocytosis process
118
botulin toxin mechanism to paralysis
the neuro muscular junction contain Ach, the toxin cleaves the v-snares on vesicles that contain Ach. resultis in not being able to fuse their vesicles with the membrane and not release ACh into the muscle
119
botulism
flaccid paralysis. floppy baby syndrome.
120
tetanospasmin mechanism
cleaves v-snare of vesicles containing GABA and glycine, will result in spastic paralysis.
121
initial signs of tetanus
trismus (lockjaw). nech stiffness, dysphagia
122
simple test for tetanus
spatula test. induce gag reflex will result in patient locking jaw
123
Endocytosis
how things get into the cell
124
how many types of endocytosis
3: pinocytosis, phogocytosis, receptor mediated endocytosis
125
pinocytosis
cell-dringling (fluid and solutes)
126
phagocytosis
cell eating (food, development, defense) completely non-specific
127
receptor mediated endocytosis
clathrin-coated pits, caveolin-coated cavellae
128
two functions of endocytosis
bring material into the cell and reclycle plasma membrane
129
what types of cell undergo pinocytosis?
all cells
130
what causes membrane deformation for vesicles budding?
actin filaments
131
opsonins?
anything that a macrophage has a receptor to bind to
132
what happens when macrophage binds to a cells opsonis?
the actin filaments are activated and start to change the shape of the membrane to start engolphin the dying cell
133
phases of phagocytosis
attachment, engulfment, fusion, difestion
134
attachmetnt phase of phagocytosis
phagocyte binds to opsonins
135
engulfment phase during phagocytosis
binding of receptors to foreign particles initiates actin filaments assembly. phagocytic cup form around foreingner
136
residual body
anything that cant be digested in the phagolysosomes, that will be secreted from the cells
137
receptor mediated endocytosis
protein coat binging to the membrane to initiate, (a hormone for example)
138
lipid rafts
concentrate proteins inthe same place in the mmembrane
139
dynamin
large Gprotein use ennergy to squeeze vesicle trhough membrane
140
what allows the cargo to be released into the endosome from vesicles
higher pH
141
steps in endocytic vesicle formation and destination
```
1 AP (adaptins recruitments
2 clathrin assembly ???
```
142
endosomes
immature lysosome
143
what endosomes contain
endocytic material, concentrate the materials
144
example of membrane reclyng
LDL recptor to pick up more cargo
145
familial hypercholesterolemia
mutation on LDL-R that increases cholesterol, increases synthesis LDL, the receptors dont fold into lipid rafts. makes it difficult to proteins to cluster there, endocytosis will not work there
146
types of mutation on LDL-R
affects: synthesis, transport, biding, clustering, recycling
147
what any of the mutation in LDL-Receptor result in?
hypercholesterolemia
148
caveolin-coated vesicles
type of coat protein in the membrane, they cluster into lipid rafts to dissociate the vesicle. (just recognize that it is a type of coat protein
149
Lysosome?
principal sites of intracellular digestion
150
what is the pH of a lysosome?
around 4.5
151
types of lysosome?
primary: only contain lysosomal enzymes directly made from transgolgi
secondary: fusion of primary lysosome with substrate to be degraded, involved in varioys stages of degradation
152
what is contained within late endosomes?
material from endocytosis and hydrolytic enzymes
153
vesicles from early endosomes bud off from early endosomes and go to the golgi carrying what?
receptors to be recycled
154
waht any vesicles traveling in the cell have in their membrane?
hydrogen pumps, to make the inside more acidic
155
difference of endosome and lysosome,
echo
156
difference btw early and late lysosome
echo
157
when a endosome become a lysosome?
when all enzymes are fully active
158
M6P tag
echo
159
how are cathrin-coated vesicle created?
1 cargo receptors bind cargo proteins,
2 receptors concentrated in membrane
3 adaptins link receptors to clathrin coat proteins
5 coat proteins disassemble, exposing Rab and SNAREs then docking and fusion
160
transport of hydrolases to lysosomes steps
Cargo binds to M6P Receptor
M6P Receptor clusters, with adaptors, clathrin buds off vesicle
Clathrin coat removed & fusion with acidic endosome
Acid dissociates cargo from M6P receptor
Phosphate removed from cargo so can not rebind to M6P receptor
M6P Receptors recycled to TGN
161
Acidification of Endosome & Lysosome
V-type ATPase (H pumps), use energy from ATP to pump H+ into the lumen to make it more acidic
162
3 pathways to degradation in lysosomes
Endocytosis
Phagocytosis
Autophagy
cells use this to regulate the amount of organelles needed or not needed.
163
Maturation of early endosomes containing endocytic vesicles to late endosomes occurs via?
“Multivesicular bodies”
164
Late endosomes become endolysosmes & lysosomes by?
Fusing with preexisting lysosomes
| Progressive acidification
165
why does multivesicular bodies (MVB) shed vesicles?
to recycle material back to PM and Gradually convert into late endosomes by fusing with eachother / with other late endosomes
166
what do proteins destined to join MVB get?
a mono-ubiquitin tag
167
what do M6P receptor are for?
to interact with lysosomal enzymes. vesicles have them
168
how downregulate transmembrane protein
they become multivesicular bodies inside endosomal compartment
169
difference btw poly and mono ubiquitin tag
poly: brings proteins from the cytosol to the proteosome,
mono: tag transmembrane proteins to be engulfed within a lysosome
170
residual body
anything that cant be digested, can remain in the cell as lipofuscin or be exocytosed
171
autopahgy
ER envelopes old organelles (ie: mitochondria)
Fusion with a lysosome
lysosomal lipases break down all inner membranes;
lysosomal membrane protected by heavily glycosylated proteins & lipids
172
lipofuscin?
pigmented lipids (“age pigments” accumulate in multiple organs)
173
Mucopolysaccharidoses (MPS)
Defective degradation of GAGs (mucopolysaccharides)
MPS I – MPS VII
All Autosomal Recessive EXCEPT Hunter (X-linked)
174
Hurler syndrome (MPS IH) inheritance pattern
autosomal recessive
175
Hurler syndrome (MPS IH) mechanism
Defect alpha-L-iduronidase → Accumulation of GAGs:
Dermatan sulphate and Heparan sulphate
“hurLer alpha-L-iduronidase”
176
Hurler syndrome (MPS IH) key words
alpha-L-iduronidase, Corneal clouding,
| Hepatosplenomegaly, Coarse facial features, Hirsutism,
177
Hurler syndrome (MPS IH) cell biology
2 GAGs: Dermatan sulphate and Heparan Sulphate
• Dermatan sulphate: Functions in coagulation, cardiovascular
disease, carcinogenesis, wound repair, and fibrosis
• Heparan sulphate: Regulates biological activities and has cell
receptors for viruses
• Hirsutism: Abnormal growth of hair on face and body
• Coarse: Not proportional
178
Hurler syndrome (MPS IH) similar to which other disease symptoms?
I cell disease. (inclusion cell disease
179
mode of inheritance of hunter syndrome (MPS II)
X-Linked
180
hunter, hurler, I cell disease
know enzymes affected
181
Hunter syndrome (MPS II) inherritance pattern
X-linked recessive
182
Hunter syndrome (MPS II) mechanism
Defect iduronodate sulphatase → Accumulation of GAGs:
| Dermatan sulphate and Heparan sulphate
183
Hunter syndrome (MPS II) key works
“Hunters like to DATE their sulFATE”
| IduronaDATE sulFATEase
184
Hunter syndrome (MPS II) cell biology
“Hunters aim for the X so they can see later”
Similar to Hurler syndrome BUT
X-Linked NOT autosomal recessive
NO Corneal clouding
Later presentation (2-4yrs) and milder course (30’s)
185
Chédiak-Higashi syndrome inherritance pattern
autosomal recessive (rare)
186
Chédiak-Higashi syndrome mechanism
“cheDiak-Higashi: DAG HAR”
Mutated CHS1/LYST: → “DAG”
1) → Delayed fusion of phagosome with lysosome in
leukocytes
2) → Autophagocytosis of melanosomes in melanocytes
→ Albinism
3) → Granular defects in NK cells & platelets
187
Chédiak-Higashi syndrome key words
“HAR” Hypopigmentation, Autophagosome, Recurrent infections
188
Chédiak-Higashi syndrome cell biology
Hypopigmentation, Autophagosome, Recurrent infections
189
Chédiak-Higashi syndrome cell biology
NK: Natural Killers contain cytosolic granules to aid in immune system
190
what the pH in a peroxysome?
regular physiological pH
191
number of enzymes in a peroxisome?
about 50
192
what do peroxisome produce?
hydrogen peroxide.
193
perexidase function
break down Hydro peroxide
194
what signal a protein need to get into a peroxisome?
C terminal SKL (Ser-Lys-Leu) import signal (PTS1 signal)
195
peroxins
import protein that recognize the SKL import signal. to aid proteins to get from the cytoplasm into the peroxisome
196
biosynthetic function of peroxisomes
```
Plasmalogen synthesis (ether phospholipid)
Bile acid synthesis (derived from cholesterol; occurs in liver) Lipid biosynthesis: Cholesterol & dolichol (also made by sER)
```
197
degradative function of peroxisome?
VLCFA β-oxidation
Purine catabolism (xanthine oxidase)
H2O2
198
only place that beta oxidation of very long chain fatty acids (VLCFA) can be broken down?
peroxisomes only
199
xanthine oxidase finction
degrades nucleic acid purines A and G into uric acid that is secreted after
200
allopurinol
xanthine oxidase inhibitor which results in hyperuricaemia (gout arthritis)
201
plasmalogen
Membrane components of heart & brain
202
Zellweger Syndrome mode of inheritance
autosomal recessive, congenital
203
Zellweger Syndrome mechanism
Defected Peroxin does not recognize SKL ! failure to import peroxisomal enzymes ! empty peroxisomes ! peroxisome deficiency: VLCFA
accumulation glial cell membrane ! abnormal brain development ! neuronal migration defects & hypomelination (lack of plasmalogen); accumulation of VLCFA in liver !
hepatomegaly & liver failure; lack of bile acids ! decreased fat absorption ! decreased ATP! muscle weakness.
204
X-linked Adrenoleukodystrophy (XALD) mechanism?
Defect in transport of VLCFA into peroxisome ! defective breakdown of
VLCFAs ! accumulation of VLCFA: brain (glial cells) ! myelin breakdown; adrenal cortex! adrenal atrophy
205
mitochondria innermembrane strrcture
permeable and allow free diffusion of small molecules and ions
206
functions of mitochondria
atp production, and apoptosis
207
number of mitochondria in a cell is related to what
the cell's need for energy. more active cells will have more.
208
mitochondria innermembrane
impermeable to most molecules. has cristae to increase surface area
209
most important feature of inner membrane of mitochondria
the impermeability which allows for gradient
210
where in the mitochondira is atp produced?
in the matrix, even though the atp synthase is in the inner membrane
211
cardiolioin importance in the inner membrane?
lipid that makes is impermeable.
212
properties of cardiolipin present in the inner membrane of mitochondria
it makes up to 20% of the inner membrane, it has double phospholipid (4 tails) it is made in the mitochondria unlike the others that are imported
213
Barth syndrome
X-linked cardiolipin synthesis disorder
Cardiomyopathy
Generalised muscle weakness & chronic fatigue
Neutropenia
