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Medical Cell Biology

Polarized Cells 2 different cell membrane. Apical BM and Basal Lateral BM
Unpolarized Cells One plasma membrane
Double membrane organelles Mitochondria and Nucleus
Secretory pathway Made in ER - Golgi - Secretory Vesicle - Plasma Membrane
Non-secretory Pathway Made in ER - Golgi - Secretory Vesicle - Endosome - Lysosome (need M6P)
Double Membrane - Inner Contain nuclear lamina (fibrous network of IFs for shaping nuclear envelope)
Double Membrane - Outer Continuous with rough ER
Nucleolus where rRNA synthesized
Nuclear Matrix Inside nucleus, provide scaffold for chromatin binding
Nuclear Pores Complex Transport materials in and out of nucleus. Contain 8 protein subunit. These proteins are joined by spokes. Allow free movement of anything smaller than 9 nm or 60kDa
NLS Protein that helps transport materials IN the nucleus if it is large
NES Protein that helps transport material OUT of the nucleus if is is to large for diffusion
Nucleoskeleton The ring attached inside of the nuclear pore complex
Cytoskeleton The ring attached on the the outside of the nuclear pore complex
Nuclear Lamina Fibrous network of intermediate filaments that underly the inner surface of nuclear membrane. Composed of Lamin A, B,C
Prophase Condense of chromosome by depolymerization and break down of nuclear membrane - through phosphorylation of lamins by lamina kinase
Telophase Decondense of chromosome, reassembly of nuclear envelope by dephosphorylation of lamins by lamin phosphatases
Emery-Dreifuss muscular dystrophy Mutation in Emerin. Elbow and neck become stiff. Cardiac conduction block and weakness
Familial partial lipodystrophy Skin condition. Loss of subcutaneous fat
Charcot marie tooth disorder type 2 Non-demyellinating peripheral neuropathy, Distal muscle weakness and atrophy
Hutchison Gilford Progeria Premature aging
Functions of SER Glucose mobilization from glycogen, Storage of calcium, Drug detoxification, lipid synthesis
Glucose-6-Phosphatase An enzyme that breaks glycogen into glucose. Remove Pi group in order to export
Von Gierke's Disease Increase glycogen storage cause hypoglycemia, enlarged liver and kidney, abnormal growth
Cytochrome p450s Use oxygen and NADPH to hydroxylate steroids and drugs
Hydroxylation Means increase water solubility to hydrophobic drugs
Chronic barbiturate use Increase in p450 and SER and SER expansion
Lipid Synthesis: Phospholipids Assembly in SER and flippase will distribute
rER function Glycosylation, folding, quality control, and degredation of proteins not passing quality control
Signal Recognition Particle (SRP) Direct ribosome and mRNA to rER membrane. Nascent polypetide translocated across ER membrane.
Signal Peptidase Cleaves signal sequence
P54 Binds signal peptide
P9/P14 Binds ribosome carrying mRNA
P68/P72 Needed for translocation
P19 Attaches p54 to the rest of the SRP
What is needed for integral membrane proteins translation and translocation Signal Sequence and Stop Transfer sequence
Type I Integral Membrane Protein Has an N-term cleavalbe signal peptide and stop transfer anchor
Type II Integral Membrane Protein No cleavable peptide site, positive N-terminal side
Type III Integral Membrane Protein No cleavable peptide side, positive C-terminal side
Type IV Protein Multi stop transfer sequence and signal anchor
Mannose-6-phophate (M6P) During protein glycosylation, Mannose-6-phosphate is added to target lysosomal enzymes to lysosome
N-Linked glycosylation Occurs in the rER. A tree of sugars (oligosaccharide) is added to Asn residues
Chaperones Needed for proper folding
ERAD Misfolded proteins will be sent to ERAD (ER associated degradation pathway)
BiP Shield hydrophobic residues inside
Protein Disulfide isomerases Form disulfide bond b/w cysteine and sulfhydryl group
Calreticulin & Calnexin Bind glucose on N-Linked oligosaccharides to promote folding
Calnexin Single pass TM protein, need to bind to ERp57 for proper folding
Calreticulin Soluble protein
Cystic Fibrosis Mutation in CFTR, deletion of phenylalanine at Position 508, Protein misfolded-- send to degradation, Defective Cl channel, Cl cannot taken inside the cell
Scaffold proteins of coat Determined what cargo is selected
Formation of Vesicle Coat First recruitment of small GTP-binding protein that is initiated by GEF
Vesicle Tethering Regulated by Rab
Choroideremia Defective Rab, vision disorder
Vesicle Fusion Need SNARES, V-snares and T-snares
NSF (N-ethylmaleimide sensitive factor) ATPase that disassemble SNARE complexes
COP II Anterograde transport. ER to Golgi
Sar1 Recruits COPII
Sec 23 and Sec 24 Adaptor protein, inner layer for COP II coat
Sec 13 and Sec 31 Adaptor protein, outer layer for COP II coat.
ERGIC53 Escort protein for COPII anterograde transport
Mutation in ERGIC53 Cause bleeding disorder FACTOR V and VIII
O-linked glycosylation Takes place by glycosyl transferases. Occurs in the golgi
COP I Retrograde transport. Golgi to ER. Return SNARE proteins to rER
KDEL C-terminal retrograde transport signals. Soluble protein. Needed in COP I.
KKXX C-terminal retrograde transport signal. Nonsoluble, hydrophobic membrane proteins, Needed in COP I.
Regulated Secretion Store proteins and peptides-release when needed. N-glycosylation
Constitutive Secretion Replinish (fill or restore) lipids and proteins, no coat protein idenitified.
I-Cell Disease Defect in the GlcNac phophotransferase. Lysosomal enyzme is not phosphorylated and secreted so will get accumulation of undigested glycolipids
Clathrin Coat TGN to Lysosome
ARF-1 Recruit clathrin to bind to vesicles form a coating
AP-1 adaptor proteins is in inner layer of the coat that bind to cargo protein
Cholesterol and LDL Receptor Inner coat layer is AP-2, LDL bind Apo-B 100 then bind to LDL receptor then bind to AP-2 formed a coat vesicle
Transferrin Iron binding blood plasma glycoprotein. Low pH induce conformational change that stimulates the release of iron
Proteasome Needs ubiquitin to attach to target
Ubiquination Needed for translation, activation of transcription DNA repair, apoptosis
Ring E3 Direct transfer
HECT E3 Indirect Ub transfer to target
E4 Conjugating factor for polyubiquitination
Ubiquination complex Consist of 2alpha (outer) and 2beta (inner). Consists of two 19S core and one 20S core unite
19S Recognition of target
20S Degradation of target
Functions of Mitochondria ATP production, Kreb Cycle, Heme synthesis, gluconeogenesis, Regulators of programmed cell death
MLS (Mitochondrial localization signals) Needed for protein transport
Cardiolipin Phospholipid that is located in the inner membrane of a mitochondria
Mitochondrial Genome 2rRNA genes, 22tRNA genes, 13 genes for electron transport chain and oxidative phosphorylation
Mitochondrial Diseases Maternally inherited
LHON (Leber's Hereditary Optic Neuropathy) Bilateral, point mutations in mitochondrial DNA (ND1, ND4, ND6) subunit of NADH-ubiquinone Oxidoreductase
Protein Import: Matrix Protein Binds to TOM 20/22-- Goes through TOM 40 -- Transferred to TIM 23/17 complex and passes through TIM 50 -- PAM
Protein Import: Outer Membrane Binds to TOM 20 -- Passes through TOM 40 -- Then through TIMS-- TIMS bring it to SAM 50 -- Becomes beta barrel protein
Protein Import: Inner Membrane Carrier Portein precursor binds to TOM 70 -- Translocate through TOM 40 General -- Present it to small TIMS in the inter membrane space -- Small TIMs present it to TIM 22 complex -- Now get folded and become carrier proteins
Oxidase Peroxisome protein that is involve in hydrogen peroxide catabolism
Catalases Peroxisome protein that is involved in hydrogen peroxide breakdown
Functions of Peroxisome VLC fatty acid oxidation, Cholesterol and bile synthesis, Synthesis of Plasmologens which is synthesis of Ether Lipids by ester linkage (R'-O-R), Detoxification of H2O2.
Import of peroxisomal proteins Must be FOLDED, Need Peroxisomal localization Signal
PTS1 C terminal target sequence (Peroxisome)
PTS2 N terminal target sequence
PEX5P Cytosolic receptor of PTS1
PEX7P Cytosolic receptor of PTS2
Are PTS removed inside the peroxisome NOOOO!
X-linked adreno leukodystrophy (X-ALD) Peroxisomal Disease, Accumulation of VLC acid in brain and adrenal cortex, due to defective membrane transport protein so cannot transport inside the peroxisome, Destroy myelin sheath around the nerves cell
Zellweger Syndrome Defect in PEX receptor, inability to import of peroxisomal proteins and enzymes
Created by: jsabangan