PERANAN SITOSKELETON MENJAGA STABILITAS DAN ELASTISITAS
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2 Table of Contents No. Title Page 1 PERANAN SITOSKELETON MENJAGA STABILITAS DAN ELASTISITAS 2 PENGARUH PERUBAHAN LETAK TITIK BERAT DAN TITIK TUMPU TUBUH KERJA BUBUT POSISI BERDIRI ERGONOMIS TERHADAP KELELAHAN OTOT BIOMEKANIK 3 STUDY OF SOME BIOCHEMICAL PARAMETERS IN YOUNG MAN AS EFFECTED BY RAMADAN FASTING 4 PENGARUH CURCUMIN TERHADAP KEKUATAN KONTRAKSI JANTUNG TIKUS BETINA YANG DIPERLAKUKAN ISKEMIA â REPERFUSI DENGAN METODE LANGENDORFF 5 PLASTICITY BIOLOGIS SEL IMUNOKOMPETEN PADA PEMBERIAN DEXAMETHASON 6 PERAN LEPTIN DALAM MENINGKATKAN DENSITAS TULANG 0 0
3 Vol. 5 No. 2 / TOC :, and page : PERANAN SITOSKELETON MENJAGA STABILITAS DAN ELASTISITAS PERANAN SITOSKELETON MENJAGA STABILITAS DAN ELASTISITAS Abstract 1. Agustina Rahayu M > 2. Tjitra Wardani > Erythrocyte has bigger diameter than capillary but erythrocyte can through the capillary. Erythrocyte membrane is very elastic so the change of shape when entering capiler not influence erythrocyte membrane structure. The strength of this membrane is caused by cytoskeleton that prop up lipid bilayer membrane. When erythrocyte enter capillary, calcium level will increase that lead into many phosphorilation. Calcium elevation more than 106 M will cause calcium bind with calmodulin at the end of spectrin ï COOH. Calsiumcalmodulin binding activate PKC in adducin and protein 4.1. Activation of PKC cause spectrin binding site in Factin opened and make spectrin boound to Factin and lead to spectrin ï shortness. These interaction is called horizontal interaction. Calcium elevation more than 10 7 M, is caused vertical interaction through many phosforilation processes (spectrinankrynband 3, spectrinprotein 4.1band 3, spectrinprotein 4.1glycophorin C and spectrin protein 4.1 band 3), that pull on lipid bilayer membrane. By this horizontal and vertical interactions, erythrocyte membrane become stable and elastic when entering capillary. Keyword : cytoskeletal, erythrocyte, calcium, capillary,, Daftar Pustaka : 1. J P Anderson, (1987). The interaction of calmodulin with human erythrocyte spectrin. J Biochem 262. : 2. JS Morrow, (1987). The interaction of calmodulin with human erythrocyte spectrin. J Biochem 262. : 3. V Bennett, (0000). spectrin and ankyrin based pathways: metazoan inventions for integrating cells into tissues. Am J Physiol 81. : 4. A Baines, (0000). spectrin and ankyrin based pathways: metazoan inventions for integrating cells into tissues. Am J Physiol 81. : 5. S H Chang, (2001). Regulation of the glycophorin Cprotein 4.1 membrane to skeleton bridge and evaluation of its contribution to erythrocyte membrane stability. J Biochem 276. : 6. P S Low, (2001). Regulation of the glycophorin Cprotein 4.1 membrane to skeleton bridge and evaluation of its contribution to erythrocyte membrane stability. J Biochem 276. : 7. RH Chen, (1997). The role of the PH domain in the signaldependent membrane targeting of Sos. EMBO Journal 16. : 8. G S Corbalan, (1997). The role of the PH domain in the signaldependent membrane targeting of Sos. EMBO Journal 16. : 9. S D Bar, (1997). The role of the PH domain in the signaldependent membrane targeting of Sos. EMBO Journal 16. : 10. L Cherry, (1999). Interactions of the ï spectrin Nterminal region with ï spectrin J Biochem 274. : 11. N Menhart, (1999). Interactions of the ï spectrin Nterminal region with ï spectrin J Biochem 274. : 12. F L WoMei, (1999). Interactions of the ï spectrin Nterminal region with ï spectrin J Biochem 274. : 13. C M Cohen, (1980). Spectrindependent and â independent association of Factin with the erythrocyte membrane J Cell Biology 86. : 14. S F Foley, (1980). Spectrindependent and â independent association of Factin with the erythrocyte membrane J Cell Biology 86. : 15. V M Fowler, (1990). Tropomodulin: a cytoskeletal protein that binds to the end of erythrocyte tropomyosin and inhibits tropomyosin binding to actin J Cell Biology 111. : 16. V Fowler, (2000). Models for actin filament organization in the erythrocyte membrane skeleton. Blood 96. : 17. AC Guyton, (2000). Text book of medical physiology. Philadelphia : WB Sauders Co 18. JE Hall, (2000). Text book of medical physiology. Philadelphia : WB Sauders Co 19. R Khanna, (2002). Headpiece domain of dematin is required for the stability of the erythrocyte membrane PNAS 99. : 20. S H Chang, (2002). Headpiece domain of dematin is required for the stability of the erythrocyte membrane PNAS 99.
4 : 21. S Andrabi, (2002). Headpiece domain of dematin is required for the stability of the erythrocyte membrane PNAS 99. : 22. X Li, (1996). Identification of the spectrin subunit and domains required for formation of spectrin/adducin/actin complexes. J Biochem 271. : 23. V Bannett, (1996). Identification of the spectrin subunit and domains required for formation of spectrin/adducin/actin complexes. J Biochem 271. : 24. E Ling, (1988). Modulation of red cell band 4.1 function by campdependent kinase and protein kinase C phosphorylation. J Biochem 263. : 25. Y N Danilov, (1988). Modulation of red cell band 4.1 function by campdependent kinase and protein kinase C phosphorylation. J Biochem 263. : 26. C M Cohen, (1988). Modulation of red cell band 4.1 function by campdependent kinase and protein kinase C phosphorylation. J Biochem 263. : 27. E Ling, (1986). Protein kinase C phosphorylates a recently identified membrane skeleton associated calmodulin binding protein in human erythrocytes. J Biochem 261. : 28. K Gardner, (1986). Protein kinase C phosphorylates a recently identified membrane skeleton associated calmodulin binding protein in human erythrocytes. J Biochem 261. : 29. V Bennett, (1986). Protein kinase C phosphorylates a recently identified membrane skeleton associated calmodulin binding protein in human erythrocytes. J Biochem 261. : 30. H Lodish, (2000). Molecular cell biology. 4th Ed. New york : W.H freeman and Co 31. J W Lomasney, (1999). Activation of phospholipase C ï 1 through C2 domain by a Ca2+enzyme phosphatidylserine ternary complex. J Biochem 274. : 32. H F Cheng, (1999). Activation of phospholipase C ï 1 through C2 domain by a Ca2 enzyme phosphatidylserine ternary complex. J Biochem 274. : 33. S R Roffler., (1999). Activation of phospholipase C ï 1 through C2 domain by a Ca2 enzyme phosphatidylserine ternary complex. J Biochem 274. : 34. K King, (1999). Activation of phospholipase C ï 1 through C2 domain by a Ca2 enzyme phosphatidylserine ternary complex. J Biochem 274. : 35. R I MacDonald., (2004). Stabilities of folding of clustered, tworepeat fragments of spectrin reveal a potential hinge in the human erythroid spectrin tetramer PNAS 101. : 36. J A Cummings, (2004). Stabilities of folding of clustered, tworepeat fragments of spectrin reveal a potential hinge in the human erythroid spectrin tetramer PNAS 101. : 37. D Mandal, (2002). Mapping of a spectrin binding domain of human eruthrocyte membrane protein 4.2. J Biochem 364. : 38. P K Moitra, (2002). Mapping of a spectrin binding domain of human eruthrocyte membrane protein 4.2. J Biochem 364. : 39. J Basu, (2002). Mapping of a spectrin binding domain of human eruthrocyte membrane protein 4.2. J Biochem 364. : 40. Y Matsuoka, (1996). Adducin regulation definition of the calmodulinbinding domain and sites of phosphorylation by protein kinases A and C. J Biochem 271. : 41. C A Hughes, (1996). Adducin regulation definition of the calmodulinbinding domain and sites of phosphorylation by protein kinases A and C. J Biochem 271. : 42. V Bennett, (1996). Adducin regulation definition of the calmodulinbinding domain and sites of phosphorylation by protein kinases A and C. J Biochem 271. : 43. N Mohandas, (2001). Structural organization of the RBC membrane. : 44. W Nunomura, (1997). Regulation of CD 44protein 4.1 interaction by Ca2+ and calmodulin. J Biochem 272. : 45. Y Takakuwa, (1997). Regulation of CD 44protein 4.1 interaction by Ca2 and calmodulin. J Biochem 272. : 46. R Tokimitsu, (1997). Regulation of CD 44protein 4.1 interaction by Ca2 and calmodulin. J Biochem 272. : 47. V P Patel, (1986). Relationship of major phosphorylation reactions and MgATPase activities to ATPdependent shape change of human erythrocyte membranes. J Biochem 261. : 48. G Fairbanks, (1986). Relationship of major phosphorylation reactions and MgATPase activities to ATPdependent shape change of human erythrocyte membranes. J Biochem 261. : 49. A M Rubtson, (2000). Minireview ankyrin FEBS 482. : 50. O D Lopina, (2000). Minireview ankyrin FEBS 482. : 51. L A Sung, (2000). Tropomyosin isoform 5b is expressed in human erythrocytes: implication of tropomodulintm5 or tropomodulintm5b complexes in the protofilament and hexagonal organization of membrane skeletons. Blood 95. : 52. K M Gao, (2000). Tropomyosin isoform 5b is expressed in human erythrocytes: implication of tropomodulintm5 or tropomodulintm5b complexes in the protofilament and hexagonal organization of membrane skeletons. Blood 95. : 53. L J Yee, (2000). Tropomyosin isoform 5b is expressed in human erythrocytes: implication of tropomodulintm5 or tropomodulintm5b complexes in the protofilament and hexagonal organization of membrane skeletons. Blood 95. :
5 Powered by TCPDF ( 54. L Sung, (2000). A view on the molecular basis of erythrocyte membrane mechanics. Blood 96. : 55. T Tanaka, (1991).. Ca2+ dependent regulation of the spectrin/actin interaction by calmodulin and protein 4.1 J Biochem 266. : 56. K Kadowaki, (1991).. Ca2 dependent regulation of the spectrin/actin interaction by calmodulin and protein 4.1 J Biochem 266. : 57. E Lazarides, (1991).. Ca2 dependent regulation of the spectrin/actin interaction by calmodulin and protein 4.1 J Biochem 266. : 58. K Sobue, (1991).. Ca2 dependent regulation of the spectrin/actin interaction by calmodulin and protein 4.1 J Biochem 266. : 59. D Voet, (1995). Biochemistry. 2nd Ed. New york : John wiley & sons inc 60. J C Winkelmann, (1993). and nonerythroid spectrin. Blood 81. : 61. BG Forget, (1993). and nonerythroid spectrin. Blood 81. : 62. S Wolfe, (1993). Molecular and cellular biology. California : Wadsworth publishing Co 63. R Workman, (1998). Biochemical analysis of potential sites for protein 4.1 mediated an choring of the spectrinactin skeleton to the erythrocyte membrane. J Biochem 273. : 64. D Zhang, (2000). Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3. Blood 96. : 65. A Kiyatkin, (2000). Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3. Blood 96. : 66. J T Bolin, (2000). Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3. Blood 96. : 67. PS Low, (2000). Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3. Blood 96. :
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