메뉴 건너뛰기




Volumn 31, Issue 6, 2010, Pages 371-377

Effect of HSP47 expression levels on hetero trimmer formation among type iv collagen α3, α4 and α5 chains

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; COLLAGEN TYPE 4; COLLAGEN TYPE 4 ALPHA3 CHAIN; COLLAGEN TYPE 4 ALPHA4 CHAIN; COLLAGEN TYPE 4 ALPHA5 CHAIN; HEAT SHOCK PROTEIN 47; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 78650840802     PISSN: 03886107     EISSN: 1880313X     Source Type: Journal    
DOI: 10.2220/biomedres.31.371     Document Type: Article
Times cited : (3)

References (23)
  • 1
    • 0037127254 scopus 로고    scopus 로고
    • The recombinant expression of full-length type VII collagen and characterization of molecular mechanisms underlying dystrophic epidermolysis bullosa
    • Chen M, Costa FK, Lindvay CR, Han YP and Woodley DT (2002) The recombinant expression of full-length type VII collagen and characterization of molecular mechanisms underlying dystrophic epidermolysis bullosa. J Biol Chem 277, 2118-2124.
    • (2002) J Biol Chem , vol.277 , pp. 2118-2124
    • Chen, M.1    Costa, F.K.2    Lindvay, C.R.3    Han, Y.P.4    Woodley, D.T.5
  • 3
    • 0036020918 scopus 로고    scopus 로고
    • Meta-analysis of genotype-phenotype correlation in X-linked Alport syndrome: Impact on clinical counselling
    • Gross O, Netzer KO, Lambrecht R, Seibold S and Weber M (2002) Meta-analysis of genotype-phenotype correlation in X-linked Alport syndrome: impact on clinical counselling. Nephrol Dial Transplant 17, 1218-1227.
    • (2002) Nephrol Dial Transplant , vol.17 , pp. 1218-1227
    • Gross, O.1    Netzer, K.O.2    Lambrecht, R.3    Seibold, S.4    Weber, M.5
  • 4
    • 0031665081 scopus 로고    scopus 로고
    • HSP47, a collagen-specifc molecular chaperone, delays the secretion of type III procollagen transfected in human embryonic kidney cell line 293: A possible role for HSP47 in collagen modifcation
    • Hosokawa N, Hohenadl C, Satoh M, Kühn K and Nagata K (1998) HSP47, a collagen-specifc molecular chaperone, delays the secretion of type III procollagen transfected in human embryonic kidney cell line 293: a possible role for HSP47 in collagen modifcation. J Biochem 124, 654-662.
    • (1998) J Biochem , vol.124 , pp. 654-662
    • Hosokawa, N.1    Hohenadl, C.2    Satoh, M.3    Kühn, K.4    Nagata, K.5
  • 6
    • 33745747824 scopus 로고    scopus 로고
    • Type I collagen in Hsp47-null cells is aggregated in endoplasmic reticulum and deficient in N-propeptide processing and fbrillogenesis
    • Ishida Y, Kubota H, Yamamoto A, Kitamura A, Bächinger HP and Nagata K (2006) Type I collagen in Hsp47-null cells is aggregated in endoplasmic reticulum and deficient in N-propeptide processing and fbrillogenesis. Mol Biol Cell 17, 2346-2355.
    • (2006) Mol Biol Cell , vol.17 , pp. 2346-2355
    • Ishida, Y.1    Kubota, H.2    Yamamoto, A.3    Kitamura, A.4    Bächinger, H.P.5    Nagata, K.6
  • 8
    • 33846029867 scopus 로고    scopus 로고
    • Molecular recognition in the assembly of colla-gens: Terminal noncollagenous domains are key recognition modules in the formation of triple helical protomers
    • Khoshnoodi J, Cartailler JP, Alvares K, Veis A and Hudson BG (2006) Molecular recognition in the assembly of colla-gens: terminal noncollagenous domains are key recognition modules in the formation of triple helical protomers. J Biol Chem 281, 38117-38121.
    • (2006) J Biol Chem , vol.281 , pp. 38117-38121
    • Khoshnoodi, J.1    Cartailler, J.P.2    Alvares, K.3    Veis, A.4    Hudson, B.G.5
  • 9
    • 0345376870 scopus 로고    scopus 로고
    • Characterization of assembly of recombinant type IV collagen α3, α4, and α5 chains in transfected cell strains
    • Kobayashi T and Uchiyama M (2003) Characterization of assembly of recombinant type IV collagen α3, α4, and α5 chains in transfected cell strains. Kidney Int 64, 1986-1996.
    • (2003) Kidney Int , vol.64 , pp. 1986-1996
    • Kobayashi, T.1    Uchiyama, M.2
  • 10
    • 37549007858 scopus 로고    scopus 로고
    • Mutational analysis of type IV collagen α5 chain, with respect to hetero-trimer formation
    • Kobayashi T, Kakihara T and Uchiyama M (2008) Mutational analysis of type IV collagen α5 chain, with respect to hetero-trimer formation. Biochem Biophys Res Commun 366, 60-65.
    • (2008) Biochem Biophys Res Commun , vol.366 , pp. 60-65
    • Kobayashi, T.1    Kakihara, T.2    Uchiyama, M.3
  • 11
    • 77951252367 scopus 로고    scopus 로고
    • Mutant-type α5(IV) collagen in a mild form of Alport syndrome has residual ability to form a heterotrimer
    • Kobayashi T and Uchiyama M (2010) Mutant-type α5(IV) collagen in a mild form of Alport syndrome has residual ability to form a heterotrimer. Pediatr Nephrol 25, 1169- 1172.
    • (2010) Pediatr Nephrol , vol.25 , pp. 1169-1172
    • Kobayashi, T.1    Uchiyama, M.2
  • 12
    • 33645639418 scopus 로고    scopus 로고
    • Specifc recognition of the collagen triple helix by chaperone HSP47: Minimal structural requirement and spatial molecular orientation
    • Koide T, Asada S, Takahara Y, Nishikawa Y, Nagata K and Kitagawa K (2006) Specifc recognition of the collagen triple helix by chaperone HSP47: minimal structural requirement and spatial molecular orientation. J Biol Chem 281, 3432- 3438.
    • (2006) J Biol Chem , pp. 3432-3438
    • Koide, T.1    Asada, S.2    Takahara, Y.3    Nishikawa, Y.4    Nagata, K.5    Kitagawa, K.6
  • 14
    • 0347418197 scopus 로고    scopus 로고
    • Collagens, modifying enzymes and their mutations in humans, fies and worms
    • Myllyharju J and Kivirikko KI (2004) Collagens, modifying enzymes and their mutations in humans, fies and worms. Trends Genet 20, 33-43.
    • (2004) Trends Genet , vol.20 , pp. 33-43
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 15
    • 0034683570 scopus 로고    scopus 로고
    • Embryonic lethality of molecular chaperone Hsp47 knockout mice is associated with defects in collagen biosynthesis
    • Nagai N, Hosokawa M, Itohara S, Adachi E, Matsushita T, Hosokawa N and Nagata K (2000) Embryonic lethality of molecular chaperone Hsp47 knockout mice is associated with defects in collagen biosynthesis. J Cell Biol 150, 1499-1505.
    • (2000) J Cell Biol , vol.150 , pp. 1499-1505
    • Nagai, N.1    Hosokawa, M.2    Itohara, S.3    Adachi, E.4    Matsushita, T.5    Hosokawa, N.6    Nagata, K.7
  • 16
    • 0031940622 scopus 로고    scopus 로고
    • Expression and function of heat shock protein 47: A collagen-specifc molecular chaperone in the endo-plasmic reticulum
    • Nagata K (1998) Expression and function of heat shock protein 47: a collagen-specifc molecular chaperone in the endo-plasmic reticulum. Matrix Biol 16, 379-386.
    • (1998) Matrix Biol , vol.16 , pp. 379-386
    • Nagata, K.1
  • 17
    • 0742304951 scopus 로고    scopus 로고
    • HSP47 as a collagen-specific molecular chaperone: Function and expression in normal mouse development
    • Nagata K (2003) HSP47 as a collagen-specific molecular chaperone: function and expression in normal mouse development. Semin Cell Dev Biol 14, 275-282.
    • (2003) Semin Cell Dev Biol , vol.14 , pp. 275-282
    • Nagata, K.1
  • 18
    • 42949094169 scopus 로고    scopus 로고
    • Making recombinant extracellular matrix proteins
    • Ruggiero F and Koch M (2008) Making recombinant extracellular matrix proteins. Methods 45, 75-85.
    • (2008) Methods , vol.45 , pp. 75-85
    • Ruggiero, F.1    Koch, M.2
  • 19
    • 0029968576 scopus 로고    scopus 로고
    • Intracellular interaction of collagen-specifc stress protein HSP47 with newly synthesized procollagen
    • Satoh M, Hirayoshi K, Yokota SI, Hosokawa N and Nagata K (1996) Intracellular interaction of collagen-specifc stress protein HSP47 with newly synthesized procollagen. J Cell Biol 133, 469-483.
    • (1996) J Cell Biol , vol.133 , pp. 469-483
    • Satoh, M.1    Hirayoshi, K.2    Yokota, S.I.3    Hosokawa, N.4    Nagata, K.5
  • 20
    • 33846850183 scopus 로고    scopus 로고
    • The collagen-specifc molecular chaperone HSP47: Is there a role in fibrosis?
    • Taguchi T and Razzaque MS (2007) The collagen-specifc molecular chaperone HSP47: is there a role in fibrosis? Trends Mol Med 13, 45-53.
    • (2007) Trends Mol Med , vol.13 , pp. 45-53
    • Taguchi, T.1    Razzaque, M.S.2
  • 21
    • 0034657132 scopus 로고    scopus 로고
    • Hsp47: A molecular chaperone that interacts with and stabilizes correctly-folded procollagen
    • Tasab M, Batten MR and Bulleid NJ (2000) Hsp47: a molecular chaperone that interacts with and stabilizes correctly-folded procollagen. EMBO J 19, 2204-2211.
    • (2000) EMBO J , vol.19 , pp. 2204-2211
    • Tasab, M.1    Batten, M.R.2    Bulleid, N.J.3
  • 22
    • 0038768172 scopus 로고    scopus 로고
    • Alport syndrome and basement membrane collagen
    • Scriver CR, Beaudet AL, Sly WS and Valle D, McGraw-Hill, New York
    • Tryggvason K and Martin P (2001) Alport syndrome and basement membrane collagen. In: The Metabolic and Molecular Bases of Inherited Disease (vol 4) (Scriver CR, Beaudet AL, Sly WS and Valle D, eds), pp 5453-5466, McGraw-Hill, New York.
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , vol.4 , pp. 5453-5466
    • Tryggvason, K.1    Martin, P.2
  • 23
    • 34447515630 scopus 로고    scopus 로고
    • A novel Cys1638Tyr NC1 domain substitution in α5(IV) collagen causes Alport syndrome with late onset renal failure without hearing loss or eye abnormalities
    • Wilson JC, Yoon HS, Walker RJ and Eccles MR (2007) A novel Cys1638Tyr NC1 domain substitution in α5(IV) collagen causes Alport syndrome with late onset renal failure without hearing loss or eye abnormalities. Nephrol Dial Transplant 22, 1338-1346.
    • (2007) Nephrol Dial Transplant , vol.22 , pp. 1338-1346
    • Wilson, J.C.1    Yoon, H.S.2    Walker, R.J.3    Eccles, M.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.