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