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Test

BMS2002 L.9

Daniel Kim 9 preguntas

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Preguntas del test (9)

  1. 1Only connective tissue interacts with ECM, which is basal lamina.
    1. AVerdadero
    2. BFalso
  2. 2Functions of ECM
    1. ASupport
    2. BStrength
    3. CCellular communication
    4. DNeuropathic communication
    5. ECell migration
    6. FCell polarity
    7. GCell shape
    8. HCell apoptosis
    9. ISelf-aggregation
    10. JCalcification
  3. 3• Connective tissue - Types of cells:
    1. [blank_start]Indigenous[blank_end]
    (1) [blank_start]primitive mesenchymal[blank_end] cells – help generation of other connective tissue cells & fat cells & mast cells
    (e.g) [blank_start]fibroblasts[blank_end] – in many connective tissues & synthesise most components of ECM)
    (2) [blank_start]specialised[blank_end] cells – in specialised connective tissues ([blank_start]cartilage[blank_end] & bone)
    (e.g) adipocytes, mast cells, [blank_start]chondrocytes[blank_end], osteoblasts)
    2. immigrants
    (1) [blank_start]immune[blank_end] cells
    1. AIndigenous
    2. Bprimitive mesenchymal
    3. Cmesenchymal stem
    4. Dfibroblasts
    5. Efibrosteoid
    6. Ffibrogens
    7. Gspecialised
    8. Hcartilage
    9. Icollagen
    10. Jchondrocytes
    11. Kcollagenase
    12. Laggrecanase
    13. Mimmune
  4. 43 major composition of connective ECM is [blank_start]Proteoglycan[blank_end]s, structural [blank_start]fibrous[blank_end] proteins, and specialised adhesive [blank_start]glycoprotein[blank_end]s.
    1. AProteoglycan
    2. Bfibrous
    3. Cglycoprotein
  5. 51. Proteoglycan
    • GAGs (Glycos[blank_start]amino[blank_end]glycans - highly negative [blank_start]polysaccharides[blank_end]) → covalently bind to core proteins → attract with [blank_start]sodium[blank_end] → attract with [blank_start]water[blank_end] via [blank_start]osmosis[blank_end] → keep ECM [blank_start]hydrated[blank_end]
    • Most anionic (-ve) molecules from animals, made of [blank_start]sulphate[blank_end] disaccharide repeats
    • Usually linked to core protein (simple → complex → compacted/aggregated)
    1. Aamino
    2. Bamine
    3. Campicillin
    4. Damino acidic
    5. Epolysaccharides
    6. Fmonosaccharides
    7. Gdisaccharides
    8. Htrisaccharides
    9. Isodium
    10. Jcalcium
    11. Kpottasium
    12. Liron
    13. Mwater
    14. Nwater
    15. Osodium
    16. Ppottasium
    17. Qiron
    18. Rosmosis
    19. Scarrier proteins
    20. Tion channels
    21. Uhydrated
    22. Vdehydrated
    23. Wstrong
    24. Xsulphate
    25. Ycalcium
    26. Zpottasium
    27. AAiron
    28. ABzinc
  6. 62. Fibrous proteins ([blank_start]collagen[blank_end] family – 40 types, [blank_start]3[blank_end] polypeptides = different [blank_start]α[blank_end] chain combination → different types of [blank_start]collagen[blank_end] (e.g) type XVIII basal lamina))
    • Most abundant proteins in mammals
    • Long & strong & [blank_start]tri[blank_end]-stranded helix → pulling strength of tissues
    • [blank_start]3[blank_end] polypeptides form a coil ([blank_start]α[blank_end] chains – rich in proline & glycine) → self-[blank_start]aggregation[blank_end] (→ fibrils → fibres)
    1. Acollagen
    2. Baggrecan
    3. Cintegrin
    4. Dcadherin
    5. Ehedgehog
    6. Fcollagen
    7. Gintegrin
    8. Hglycoprotein
    9. Ipeptide
    10. Jtri
    11. Kdi
    12. Lmono
    13. Mpoly
    14. N3
    15. O2
    16. P1
    17. Qα
    18. Rb
    19. Salpha&beta
    20. T3
    21. U2
    22. V1
    23. Wα
    24. Xb
    25. Yalpha&beta
    26. Zaggregation
    27. AAproferilation
    28. ABhelicase
    29. ACdegradation
    30. ADcomplication
  7. 73. Glycoproteins (NOT [blank_start]collagen[blank_end] family → elastin, fibronectin)
    • [blank_start]Elastin[blank_end] = provide elasticity & [blank_start]similar[blank_end] structure to collagen
    • [blank_start]Fibronectin[blank_end] = bind other matrix → cell-matrix link
    • Similar contents for all, but, different ratio & organisation
    • But, special connective tissue ECM exist → can be [blank_start]calcified[blank_end] (bone, teeth) or [blank_start]transparent[blank_end] (cornea)
    1. Acollagen
    2. Bdifferent
    3. CFibronectin
    4. DElastin
    5. Esimilar
    6. Fcalcified
    7. Gsolidified
    8. Hmagnified
    9. Itransparent
    10. Jtranslucent
  8. 8All character of integrin
    1. AReceptor
    2. BIon channel
    3. CCarrier proteins
    4. DBind ECM components
    5. EBind cholinergic receptors
    6. F24 different types
    7. G15 different types
    8. H40 different types
    9. IShort intracellular domain binding adaptors
    10. JLong intracellular domain binding adaptors
  9. 9• Different integrin α & β chain combination → bind to different [blank_start]ECM ligands[blank_end]
    • Interaction between ECM and [blank_start]cytoskeleton[blank_end] via integrin → strength ([blank_start]Talin[blank_end] =adaptor molecule)
    • Integrin can be active/inactive (when it is active, strong [blank_start]ligand[blank_end] binding & adaptor-protein binding)
    • Inactivation of integrin is due to continuous [blank_start]migration[blank_end] of connective tissue via ECM
    • Activation of integrin require [blank_start]intracellular[blank_end] signalling
    • Integrin mediate signalling too → recruit [blank_start]FAK[blank_end] → altered gene expression
    1. AECM ligands
    2. BECM G-protein
    3. Ccytoskeleton
    4. Dglycoprotein
    5. Epeptides
    6. Fintegrins
    7. GTalin
    8. HBalin
    9. IMetelloproteinase
    10. Jligand
    11. KG-protein
    12. Lpeptide
    13. Mhydrogen
    14. Nmigration
    15. Odegeneration
    16. Psynthesis&breakdown
    17. Qconcentration changes
    18. Rintracellular
    19. Sextracellular
    20. Tnucleic
    21. Uhormonal
    22. Vneuropathic
    23. WFAK
    24. XFUK
    25. YFEK
    26. ZFWK
    27. AAproteoglycan

Información

Descripción
Test sobre BMS2002 L.9, creado por Daniel Kim el 26/11/2017.
Idioma
English
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