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Volumn 343, Issue 1, 2006, Pages 34-42

Calumenin, a multiple EF-hands Ca2+-binding protein, interacts with ryanodine receptor-1 in rabbit skeletal sarcoplasmic reticulum

Author keywords

Cab45; Calcium binding protein; CREC family; Crocalbin; Excitation contraction coupling; Reticulocalbin

Indexed keywords

CAFFEINE; CALCIUM BINDING PROTEIN; CALCIUM ION; CALUMENIN; CALUMENIN 2; RYANODINE RECEPTOR; RYANODINE RECEPTOR 1; UNCLASSIFIED DRUG;

EID: 33645108259     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.02.115     Document Type: Article
Times cited : (43)

References (35)
  • 2
    • 0027439695 scopus 로고
    • Reticulocalbin, a novel endoplasmic reticulum resident Ca-binding protein with multiple EF-hand motifs and a carboxyl-terminal HDEL
    • M. Ozawa, and T. Muramatsu Reticulocalbin, a novel endoplasmic reticulum resident Ca-binding protein with multiple EF-hand motifs and a carboxyl-terminal HDEL J. Biol. Chem. 268 1993 699 705
    • (1993) J. Biol. Chem. , vol.268 , pp. 699-705
    • Ozawa, M.1    Muramatsu, T.2
  • 3
    • 0028339802 scopus 로고
    • The endoplasmic reticulum calcium-binding protein of 55 kDa is a novel EF-hand protein retained in the endoplasmic reticulum by a carboxyl-terminal His-Asp-Glu-Leu motif
    • K. Weis, G. Griffiths, and A. Lamond The endoplasmic reticulum calcium-binding protein of 55 kDa is a novel EF-hand protein retained in the endoplasmic reticulum by a carboxyl-terminal His-Asp-Glu-Leu motif J. Biol. Chem. 269 1994 19142 19150
    • (1994) J. Biol. Chem. , vol.269 , pp. 19142-19150
    • Weis, K.1    Griffiths, G.2    Lamond, A.3
  • 4
    • 0030610583 scopus 로고    scopus 로고
    • 2+-binding protein retained in the endoplasmic reticulum with a novel carboxyl-terminal sequence, HDEF
    • 2+-binding protein retained in the endoplasmic reticulum with a novel carboxyl-terminal sequence, HDEF J. Biol. Chem. 272 1997 18232 18239
    • (1997) J. Biol. Chem. , vol.272 , pp. 18232-18239
    • Yabe, D.1    Nakamura, T.2    Kanazawa, N.3    Tashiro, K.4    Honjo, T.5
  • 6
    • 19244369899 scopus 로고    scopus 로고
    • Human calumenin gene (CALU): CDNA isolation and chromosomal mapping to 7q32
    • D. Yabe, M. Taniwaki, T. Nakamura, N. Kanazawa, K. Tashiro, and T. Honjo Human calumenin gene (CALU): cDNA isolation and chromosomal mapping to 7q32 Genomics 49 1998 331 333
    • (1998) Genomics , vol.49 , pp. 331-333
    • Yabe, D.1    Taniwaki, M.2    Nakamura, T.3    Kanazawa, N.4    Tashiro, K.5    Honjo, T.6
  • 7
    • 1242338800 scopus 로고    scopus 로고
    • Characterization of isoforms and genomic organization of mouse calumenin
    • D.H. Jung, and D.H. Kim Characterization of isoforms and genomic organization of mouse calumenin Gene 327 2004 185 194
    • (2004) Gene , vol.327 , pp. 185-194
    • Jung, D.H.1    Kim, D.H.2
  • 8
    • 0032979150 scopus 로고    scopus 로고
    • Crocalbin: A new calcium-binding protein that is also a binding protein for clotoxin, a neurotoxic phospholipase A2
    • M.J. Hseu, C.H. Yen, and M.C. Tzeng Crocalbin: a new calcium-binding protein that is also a binding protein for clotoxin, a neurotoxic phospholipase A2 FEBS Lett. 445 1999 440 444
    • (1999) FEBS Lett. , vol.445 , pp. 440-444
    • Hseu, M.J.1    Yen, C.H.2    Tzeng, M.C.3
  • 9
    • 0033134009 scopus 로고    scopus 로고
    • Human calumenin localizes the secretory pathway and is secreted to the medium
    • H. Vorum, H. Hager, B.M. Christensen, S. Nielsen, and B. Honore Human calumenin localizes the secretory pathway and is secreted to the medium Exp. Cell Res. 248 1999 473 481
    • (1999) Exp. Cell Res. , vol.248 , pp. 473-481
    • Vorum, H.1    Hager, H.2    Christensen, B.M.3    Nielsen, S.4    Honore, B.5
  • 10
    • 0033985775 scopus 로고    scopus 로고
    • Calumenin interacts with serum amyloid P component
    • H. Vorum, C. Jacobsen, and B. Honore Calumenin interacts with serum amyloid P component FEBS Lett. 465 2000 129 134
    • (2000) FEBS Lett. , vol.465 , pp. 129-134
    • Vorum, H.1    Jacobsen, C.2    Honore, B.3
  • 11
    • 0035515246 scopus 로고    scopus 로고
    • A molecular mechanism for genetic warfarin resistance in the rat
    • R. Wallin, S.M. Hutson, D. Cain, A. Sweatt, and D.C. Sane A molecular mechanism for genetic warfarin resistance in the rat FASEB J. 15 2001 2542 2544
    • (2001) FASEB J. , vol.15 , pp. 2542-2544
    • Wallin, R.1    Hutson, S.M.2    Cain, D.3    Sweatt, A.4    Sane, D.C.5
  • 12
    • 0035940408 scopus 로고    scopus 로고
    • Dose-dependent and independent temporal patterms of gene responses to ionizing radiation in normal and tumor cells and tumor xenografts
    • N.N. Khodarev, J.O. Park, J. Yu, N. Gupta, E. Nodzenski, B. Roizman, and R.R. Weichselbaum Dose-dependent and independent temporal patterms of gene responses to ionizing radiation in normal and tumor cells and tumor xenografts Proc. Natl. Acad. Sci. USA 98 2001 12665 12670
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12665-12670
    • Khodarev, N.N.1    Park, J.O.2    Yu, J.3    Gupta, N.4    Nodzenski, E.5    Roizman, B.6    Weichselbaum, R.R.7
  • 13
    • 0036280779 scopus 로고    scopus 로고
    • Identification and validation of metastasis-associated proteins in head and neck cancer cell lines by two-dimensional electrophoresis and mass spectrometry
    • W. Wu, X. Tang, W. Hu, R. Lotan, W.K. Hong, and L. Mao Identification and validation of metastasis-associated proteins in head and neck cancer cell lines by two-dimensional electrophoresis and mass spectrometry Clin. Exp. Metastasis 19 2002 319 326
    • (2002) Clin. Exp. Metastasis , vol.19 , pp. 319-326
    • Wu, W.1    Tang, X.2    Hu, W.3    Lotan, R.4    Hong, W.K.5    Mao, L.6
  • 15
    • 12144291702 scopus 로고    scopus 로고
    • Characterization of the proteins released from activated platelets leads to localization of novel platelet proteins in human atherosclerotic lesions
    • J.A. Coppinger, G. Cagney, S. Toomey, T. Kislinger, O. Belton, J.P. McRedmond, D.J. Cahill, A. Emili, D.J. Fitzgerald, and P.B. Maguire Characterization of the proteins released from activated platelets leads to localization of novel platelet proteins in human atherosclerotic lesions Blood 103 2003 2096 2104
    • (2003) Blood , vol.103 , pp. 2096-2104
    • Coppinger, J.A.1    Cagney, G.2    Toomey, S.3    Kislinger, T.4    Belton, O.5    McRedmond, J.P.6    Cahill, D.J.7    Emili, A.8    Fitzgerald, D.J.9    Maguire, P.B.10
  • 16
    • 2942627237 scopus 로고    scopus 로고
    • The inhibitory effect of calumenin on the vitamin K-dependent gamma-carboxylation system. Characterization of the system in normal and warfarin-resistant rats
    • N. Wajih, D.C. Sane, S.M. Hutson, and R. Wallin The inhibitory effect of calumenin on the vitamin K-dependent gamma-carboxylation system. Characterization of the system in normal and warfarin-resistant rats J. Biol. Chem. 279 2004 25276 25283
    • (2004) J. Biol. Chem. , vol.279 , pp. 25276-25283
    • Wajih, N.1    Sane, D.C.2    Hutson, S.M.3    Wallin, R.4
  • 17
    • 1842528203 scopus 로고    scopus 로고
    • Proteome analysis of hepatocellular carcinoma cell strains, MHCC97-H and MHCC 97-L, with different metastasis potentials
    • S.J. Ding, Y. Li, X.X. Shao, H. Zhou, R. Zeng, Z.Y. Tang, and Q.C. Xia Proteome analysis of hepatocellular carcinoma cell strains, MHCC97-H and MHCC 97-L, with different metastasis potentials Proteomics 4 2004 982 994
    • (2004) Proteomics , vol.4 , pp. 982-994
    • Ding, S.J.1    Li, Y.2    Shao, X.X.3    Zhou, H.4    Zeng, R.5    Tang, Z.Y.6    Xia, Q.C.7
  • 18
    • 1442306221 scopus 로고    scopus 로고
    • Identification of biochemical adaptations in hyper- or hypocontractile hearts from phospholamban mutant mice by expression proteomics
    • Y. Pan, T. Kislinger, A.O. Gramolini, E. Zvaritch, E.G. Kranias, D.H. MacLennan, and A. Emili Identification of biochemical adaptations in hyper- or hypocontractile hearts from phospholamban mutant mice by expression proteomics Proc. Natl. Acad. Sci. USA 101 2004 2241 2246
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2241-2246
    • Pan, Y.1    Kislinger, T.2    Gramolini, A.O.3    Zvaritch, E.4    Kranias, E.G.5    MacLennan, D.H.6    Emili, A.7
  • 19
    • 0028349030 scopus 로고
    • Structure and development of E-C coupling units in skeletal muscle
    • C. Franzini-Armstrong, and A.O. Jorgensen Structure and development of E-C coupling units in skeletal muscle Annu. Rev. Physiol. 56 1994 509 534
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 509-534
    • Franzini-Armstrong, C.1    Jorgensen, A.O.2
  • 20
    • 0030789142 scopus 로고    scopus 로고
    • Ryanodine receptors of striated muscles: A complex channel capable of multiple interactions
    • C. Franzini-Armstrong, and F. Protasi Ryanodine receptors of striated muscles: a complex channel capable of multiple interactions Physiol. Rev. 77 1997 699 729
    • (1997) Physiol. Rev. , vol.77 , pp. 699-729
    • Franzini-Armstrong, C.1    Protasi, F.2
  • 21
    • 0030770826 scopus 로고    scopus 로고
    • Complex formation between junction, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane
    • L. Zhang, J. Kelly, G. Schmeisser, Y.M. Kobayashi, and L.R. Jones Complex formation between junction, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane J. Biol. Chem. 272 1997 23389 23397
    • (1997) J. Biol. Chem. , vol.272 , pp. 23389-23397
    • Zhang, L.1    Kelly, J.2    Schmeisser, G.3    Kobayashi, Y.M.4    Jones, L.R.5
  • 22
    • 0033083405 scopus 로고    scopus 로고
    • 2+ release channel function
    • 2+ release channel function Biochem. J. 337 1999 345 361
    • (1999) Biochem. J. , vol.337 , pp. 345-361
    • MacKrill, J.J.1
  • 23
    • 1342282949 scopus 로고    scopus 로고
    • Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin
    • J.M. Lee, S.H. Rho, D.W. Shin, C. Cho, W.J. Park, S.H. Eom, J. Ma, and D.H. Kim Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin J. Biol. Chem. 279 2004 6994 7000
    • (2004) J. Biol. Chem. , vol.279 , pp. 6994-7000
    • Lee, J.M.1    Rho, S.H.2    Shin, D.W.3    Cho, C.4    Park, W.J.5    Eom, S.H.6    Ma, J.7    Kim, D.H.8
  • 24
    • 0035955601 scopus 로고    scopus 로고
    • 2+ binding protein) and triadin in the lumen of sarcoplasmic reticulum
    • 2+ binding protein) and triadin in the lumen of sarcoplasmic reticulum J. Biol. Chem. 276 2001 39533 39538
    • (2001) J. Biol. Chem. , vol.276 , pp. 39533-39538
    • Lee, H.G.1    Kang, H.2    Kim, D.H.3    Park, W.J.4
  • 26
    • 0034671917 scopus 로고    scopus 로고
    • Molecular cloning, expression, functional characterization, chromosomal localization, and gene structure of junctate, a novel integral calcium binding protein of sarco(endo)plasmic reticulum membrane
    • S. Treves, G. Feriotto, L. Moccagatta, R. Gambari, and F. Zorzato Molecular cloning, expression, functional characterization, chromosomal localization, and gene structure of junctate, a novel integral calcium binding protein of sarco(endo)plasmic reticulum membrane J. Biol. Chem. 275 2005 39555 39568
    • (2005) J. Biol. Chem. , vol.275 , pp. 39555-39568
    • Treves, S.1    Feriotto, G.2    Moccagatta, L.3    Gambari, R.4    Zorzato, F.5
  • 28
    • 0020638835 scopus 로고
    • Purification of morphologically intact triad structures from skeletal muscle
    • R.D. Mitchell, P. Palade, and S. Fleischer Purification of morphologically intact triad structures from skeletal muscle J. Cell Biol. 96 1983 1008 1016
    • (1983) J. Cell Biol. , vol.96 , pp. 1008-1016
    • Mitchell, R.D.1    Palade, P.2    Fleischer, S.3
  • 30
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of protens silver-stained polyacrylamide gels
    • A. Shevchenko, M. Wilm, O. Vorm, and M. Mann Mass spectrometric sequencing of protens silver-stained polyacrylamide gels Anal. Chem. 68 1996 850 858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 31
    • 0033023115 scopus 로고    scopus 로고
    • A tentative mechanism of the ternary complex formation between phosphorylase kinase, glycogen phospholylase b and glycogen
    • I.E. Andreeva, V.F. Makeeva, B.I. Kurganov, N.A. Chebotareva, and N.B. Livanova A tentative mechanism of the ternary complex formation between phosphorylase kinase, glycogen phospholylase b and glycogen FEBS Lett. 445 1999 173 176
    • (1999) FEBS Lett. , vol.445 , pp. 173-176
    • Andreeva, I.E.1    Makeeva, V.F.2    Kurganov, B.I.3    Chebotareva, N.A.4    Livanova, N.B.5
  • 33
    • 0032561337 scopus 로고    scopus 로고
    • Cardiac-specific overexpression of mouse cardiac calsequestrin is associated with depressed cardiovascular function and hypertrophy in transgenic mice
    • Y. Sato, D.G. Ferguson, H. Sako, G.W. Dorn 2nd, V.J. Kadambi, A. Yatani, B.D. Hoit, R.A. Walsh, and E.G. Kranias Cardiac-specific overexpression of mouse cardiac calsequestrin is associated with depressed cardiovascular function and hypertrophy in transgenic mice J. Biol. Chem. 273 1998 28470 28477
    • (1998) J. Biol. Chem. , vol.273 , pp. 28470-28477
    • Sato, Y.1    Ferguson, D.G.2    Sako, H.3    Dorn II, G.W.4    Kadambi, V.J.5    Yatani, A.6    Hoit, B.D.7    Walsh, R.A.8    Kranias, E.G.9
  • 35
    • 4744350102 scopus 로고    scopus 로고
    • Regulation of myocardial function by histidine-rich, calcium-binding protein
    • G.C. Fan, K.N. Gregory, W. Zhao, W.J. Park, and E.G. Kranias Regulation of myocardial function by histidine-rich, calcium-binding protein Am. J. Physiol. 287 2004 H1705 H1711
    • (2004) Am. J. Physiol. , vol.287
    • Fan, G.C.1    Gregory, K.N.2    Zhao, W.3    Park, W.J.4    Kranias, E.G.5


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