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Volumn 95, Issue 3, 2005, Pages 618-629

The structure and proteolytic processing of Cbln1 complexes

Author keywords

Cerebellin; Cerebellum; Complement component 1 domain; Oligomerization; Proteolysis

Indexed keywords

CEREBELLIN; CEREBELLIN 1 PRECURSOR PROTEIN; HEXADECAPEPTIDE; PEPTIDE DERIVATIVE; PROTEIN PRECURSOR; UNCLASSIFIED DRUG;

EID: 27644547692     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2005.03385.x     Document Type: Article
Times cited : (66)

References (40)
  • 1
    • 0034023659 scopus 로고    scopus 로고
    • Evidence for a paracrine role of adrenomedullin in the physiological resetting of aldosterone secretion by rat adrenal zona glomerulosa
    • Albertin G., Malendowicz L. K., Macchi C., Markowska A. and Nussdorfer G. G. (2000) Evidence for a paracrine role of adrenomedullin in the physiological resetting of aldosterone secretion by rat adrenal zona glomerulosa. Neuropeptides 34, 7-11.
    • (2000) Neuropeptides , vol.34 , pp. 7-11
    • Albertin, G.1    Malendowicz, L.K.2    Macchi, C.3    Markowska, A.4    Nussdorfer, G.G.5
  • 2
    • 0027211704 scopus 로고
    • Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: Implications for TNF receptor activation
    • Banner D. W., D'Arcy A., Janes W., Gentz R., Schoenfeld H. J., Broger C., Loetscher H. and Lesslauei W. (1993) Crystal structure of the soluble human 55 kd TNF receptor-human TNF beta complex: implications for TNF receptor activation. Cell 73, 431-445.
    • (1993) Cell , vol.73 , pp. 431-445
    • Banner, D.W.1    D'Arcy, A.2    Janes, W.3    Gentz, R.4    Schoenfeld, H.J.5    Broger, C.6    Loetscher, H.7    Lesslauei, W.8
  • 3
    • 0034881391 scopus 로고    scopus 로고
    • The adipocyte-secreted protein Acrp30 enhances hepatic insulin action
    • Berg A. H., Du Combs T. P. X., Brownlee M. and Scherer P. E. (2001) The adipocyte-secreted protein Acrp30 enhances hepatic insulin action. Nat. Med. 7, 947-953.
    • (2001) Nat. Med. , vol.7 , pp. 947-953
    • Berg, A.H.1    Du Combs, T.P.X.2    Brownlee, M.3    Scherer, P.E.4
  • 4
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumor-necrosis factor-alpha from cells
    • Black R. A., Rauch C. T., Kozlosky C. J. et al. (1997) A metalloproteinase disintegrin that releases tumor-necrosis factor-alpha from cells. Nature 385, 729-733.
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.A.1    Rauch, C.T.2    Kozlosky, C.J.3
  • 5
    • 0036175281 scopus 로고    scopus 로고
    • Insight into Schmid metaphyseal chondrodysplasia from the crystal structure of the collagen X NC1 domain trimer. Structure (Camb)
    • Bogin O., Kvansakul M., Rom E., Singer J., Yayon A. and Hohenester E. (2002) Insight into Schmid metaphyseal chondrodysplasia from the crystal structure of the collagen X NC1 domain trimer. Structure (Camb). Structure 10, 165-173.
    • (2002) Structure , vol.10 , pp. 165-173
    • Bogin, O.1    Kvansakul, M.2    Rom, E.3    Singer, J.4    Yayon, A.5    Hohenester, E.6
  • 6
    • 0023947832 scopus 로고
    • Cerebellin-like peptide: Tissue distribution in rat and guinea-pig and its release from rat cerebellum, hypothalamus and cerebellar synaptosomes in vitro
    • Bumet P. W., Bretherton-Watt D., Ghatei M. A. and Bloom S. R. (1988) Cerebellin-like peptide: tissue distribution in rat and guinea-pig and its release from rat cerebellum, hypothalamus and cerebellar synaptosomes in vitro. Neuroscience 25, 605-612.
    • (1988) Neuroscience , vol.25 , pp. 605-612
    • Bumet, P.W.1    Bretherton-Watt, D.2    Ghatei, M.A.3    Bloom, S.R.4
  • 7
    • 0026556859 scopus 로고
    • Characterization of SAP-1, a protein recruited by serum response factor to the c-fos serum response element
    • Dalton S. and Treisman R. (1992) Characterization of SAP-1, a protein recruited by serum response factor to the c-fos serum response element. Cell 68, 597-612.
    • (1992) Cell , vol.68 , pp. 597-612
    • Dalton, S.1    Treisman, R.2
  • 8
    • 0024357657 scopus 로고
    • The structure of tumor necrosis factor-alpha at 2.6 a resolution. Implications for receptor binding
    • Eck M. J. and Sprang S. R. (1989) The structure of tumor necrosis factor-alpha at 2.6 A resolution. Implications for receptor binding. J. Biol. Chem. 264, 17 595-17 605.
    • (1989) J. Biol. Chem. , vol.264
    • Eck, M.J.1    Sprang, S.R.2
  • 9
    • 0035852760 scopus 로고    scopus 로고
    • Proteolytic cleavage product of 30-kDa adipocyte complement-related protein increases fatty acid oxidation in muscle and causes weight loss in mice
    • Fruebis J., Tsao T. S., Javorschi S., Ebbets-Reed D., Erickson M. R., Yen F. T., Bihain B. E. and Lodish H. F. (2001) Proteolytic cleavage product of 30-kDa adipocyte complement-related protein increases fatty acid oxidation in muscle and causes weight loss in mice. Proc. Natl Acad. Sci. USA 98, 2005-2010.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2005-2010
    • Fruebis, J.1    Tsao, T.S.2    Javorschi, S.3    Ebbets-Reed, D.4    Erickson, M.R.5    Yen, F.T.6    Bihain, B.E.7    Lodish, H.F.8
  • 10
    • 0031791601 scopus 로고    scopus 로고
    • An improved method for culturing cerebellar Purkinje cells with differentiated dendrites under a mixed monolayer setting
    • Furuya S., Makino A. and Hirabayashi Y. (1998) An improved method for culturing cerebellar Purkinje cells with differentiated dendrites under a mixed monolayer setting. Brain Res. Brain Res. Protoc. 3, 192-198.
    • (1998) Brain Res. Brain Res. Protoc. , vol.3 , pp. 192-198
    • Furuya, S.1    Makino, A.2    Hirabayashi, Y.3
  • 12
    • 0035222012 scopus 로고    scopus 로고
    • A new algorithm for the alignment of multiple protein structures using Monte Carlo optimization
    • Guda C., Scheeff E. D., Bourne P. E. and Shindyalov I. N. (2001) A new algorithm for the alignment of multiple protein structures using Monte Carlo optimization. Pac. Symp. Biocomput. 6, 275-286.
    • (2001) Pac. Symp. Biocomput. , vol.6 , pp. 275-286
    • Guda, C.1    Scheeff, E.D.2    Bourne, P.E.3    Shindyalov, I.N.4
  • 14
    • 3142761477 scopus 로고    scopus 로고
    • T-cadherin is a receptor for hexameric and high-molecular-weight forms of Acrp30/adiponectin
    • Hug C., Wang J., Ahmad N. S., Bogan J. S., Tsao T. S. and Lodish H. F. (2004) T-cadherin is a receptor for hexameric and high-molecular-weight forms of Acrp30/adiponectin. Proc. Natl Acad. Sci. USA 101, 10 308-10 313.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101
    • Hug, C.1    Wang, J.2    Ahmad, N.S.3    Bogan, J.S.4    Tsao, T.S.5    Lodish, H.F.6
  • 15
    • 0034254453 scopus 로고    scopus 로고
    • TNF alpha and the TNF receptor superfamily: Structure-function relationship(s)
    • Idriss H. T. and Naismith J. H. (2000) TNF alpha and the TNF receptor superfamily: structure-function relationship(s). Microsc. Res. Tech. 50, 184-195.
    • (2000) Microsc. Res. Tech. , vol.50 , pp. 184-195
    • Idriss, H.T.1    Naismith, J.H.2
  • 18
    • 0022410561 scopus 로고
    • The characterization of the specific binding of [3H]-N- acetylaspartylglutamate to rat brain membranes
    • Koller K. J. and Coyle J. T. (1985) The characterization of the specific binding of [3H]-N-acetylaspartylglutamate to rat brain membranes. J. Neurosci. 5, 2882-2888.
    • (1985) J. Neurosci. , vol.5 , pp. 2882-2888
    • Koller, K.J.1    Coyle, J.T.2
  • 19
    • 0029932071 scopus 로고    scopus 로고
    • Analysis of interaction sites in homo- and heteromeric complexes containing Bcl-2 family members and the cellular prion protein
    • Kurschner C. and Morgan J. I. (1996) Analysis of interaction sites in homo- and heteromeric complexes containing Bcl-2 family members and the cellular prion protein. Brain Res. Mol. Brain Res. 37, 249-258.
    • (1996) Brain Res. Mol. Brain Res. , vol.37 , pp. 249-258
    • Kurschner, C.1    Morgan, J.I.2
  • 20
    • 0038024555 scopus 로고    scopus 로고
    • Crystal structure of the collagen alpha1 (VIII) NC1 trimer
    • Kvansakul M., Bogin O., Hohenester E. and Yayon A. (2003) Crystal structure of the collagen alpha1 (VIII) NC1 trimer. Matrix Biol. 22, 145-152.
    • (2003) Matrix Biol. , vol.22 , pp. 145-152
    • Kvansakul, M.1    Bogin, O.2    Hohenester, E.3    Yayon, A.4
  • 22
    • 0023948765 scopus 로고
    • Cerebellin and related postsynaptic peptides in the brain of normal and neurodevelopmentally mutant vertebrates
    • Morgan J. I., Slemmon J. R., Danho W., Hempsead J. L., Berrebi A. S. and Mugnaini E. (1988) Cerebellin and related postsynaptic peptides in the brain of normal and neurodevelopmentally mutant vertebrates. Synapse 2, 117-124.
    • (1988) Synapse , vol.2 , pp. 117-124
    • Morgan, J.I.1    Slemmon, J.R.2    Danho, W.3    Hempsead, J.L.4    Berrebi, A.S.5    Mugnaini, E.6
  • 23
    • 0023587857 scopus 로고
    • The neuropeptide cerebellin is a marker for two similar neuronal circuits in rat brain
    • Mugnaini E. and Morgan J. I. (1987) The neuropeptide cerebellin is a marker for two similar neuronal circuits in rat brain. Proc. Natl Acad. Sci. USA 84, 8692-8696.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8692-8696
    • Mugnaini, E.1    Morgan, J.I.2
  • 24
    • 0023920719 scopus 로고
    • Cerebellin is a postsynaptic neuropeptide
    • Mugnaini E., Dahl A. L. and Morgan J. I. (1988) Cerebellin is a postsynaptic neuropeptide. Synapse 2, 125-138.
    • (1988) Synapse , vol.2 , pp. 125-138
    • Mugnaini, E.1    Dahl, A.L.2    Morgan, J.I.3
  • 25
    • 0034280702 scopus 로고    scopus 로고
    • Cbln3, a novel member of the precerebellin family that binds specifically to Cbln1
    • Pang Z., Zuo J. and Morgan J. I. (2000) Cbln3, a novel member of the precerebellin family that binds specifically to Cbln1. J. Neurosci. 20, 6333-6339.
    • (2000) J. Neurosci. , vol.20 , pp. 6333-6339
    • Pang, Z.1    Zuo, J.2    Morgan, J.I.3
  • 26
    • 0032080801 scopus 로고    scopus 로고
    • TNF-alpha convertase enzyme from human arthritis-affected cartilage: Isolation of cDNA by differential display, expression of the active enzyme, and regulation of TNF-alpha
    • Patel I. R., Attur M. G., Patel R. N., Stuchin S. A., Abagyan R. A., Abramson S. B. and Amin A. R. (1998) TNF-alpha convertase enzyme from human arthritis-affected cartilage: isolation of cDNA by differential display, expression of the active enzyme, and regulation of TNF-alpha. J. Immunol. 160, 4570-4579.
    • (1998) J. Immunol. , vol.160 , pp. 4570-4579
    • Attur, M.G.1    Patel, R.N.2    Stuchin, S.A.3    Abagyan, R.A.4    Abramson, S.B.5    Amin, A.R.6
  • 29
    • 0032510463 scopus 로고    scopus 로고
    • The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor
    • Shapiro L. and Scherer P. E. (1998) The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor. Curr. Biol. 8, 335-338.
    • (1998) Curr. Biol. , vol.8 , pp. 335-338
    • Shapiro, L.1    Scherer, P.E.2
  • 32
    • 0024202622 scopus 로고
    • Evidence for the transneuronal regulation of cerebellin biosynthesis in developing Purkinje cells
    • Slemmon J. R., Goldowitz D., Blacher R. and Morgan J. I. (1988) Evidence for the transneuronal regulation of cerebellin biosynthesis in developing Purkinje cells. J. Neurosci. 8, 4603-4611.
    • (1988) J. Neurosci. , vol.8 , pp. 4603-4611
    • Slemmon, J.R.1    Goldowitz, D.2    Blacher, R.3    Morgan, J.I.4
  • 33
    • 0037059013 scopus 로고    scopus 로고
    • Enhanced muscle fat oxidation and glucose transport by ACRP30 globular domain: Acetyl-CoA carboxylase inhibition and AMP-activated protein kinase activation
    • Tomas E., Tsao T. S., Saha A. K., Murrey H. E., Zhang Cc. C., Itani S. I., Lodish H. F. and Ruderman N. B. (2002) Enhanced muscle fat oxidation and glucose transport by ACRP30 globular domain: acetyl-CoA carboxylase inhibition and AMP-activated protein kinase activation. Proc. Natl Acad. Sci. USA 99, 16 309-16 313.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99
    • Tomas, E.1    Tsao, T.S.2    Saha, A.K.3    Murrey, H.E.4    Zhang, Cc.C.5    Itani, S.I.6    Lodish, H.F.7    Ruderman, N.B.8
  • 34
    • 0037119375 scopus 로고    scopus 로고
    • Oligomerization state-dependent activation of NF-kappa B signaling pathway by adipocyte complement-related protein of 30 kDa (Acrp30)
    • Tsao T. S., Murrey H. E., Hug C., Lee D. H. and Lodish H. F. (2002) Oligomerization state-dependent activation of NF-kappa B signaling pathway by adipocyte complement-related protein of 30 kDa (Acrp30). J. Biol. Chem. 277, 29 359-29 362.
    • (2002) J. Biol. Chem. , vol.277
    • Tsao, T.S.1    Murrey, H.E.2    Hug, C.3    Lee, D.H.4    Lodish, H.F.5
  • 35
    • 0347379841 scopus 로고    scopus 로고
    • Role of disulfide bonds in Acrp30/adiponectin structure and signaling specificity. Different oligomers activate different signal transduction pathways
    • Tsao T. S., Tomas E., Murrey H. E., Hug C., Lee D. H., Ruderman N. B., Heuser J. E. and Lodish H. F. (2003) Role of disulfide bonds in Acrp30/adiponectin structure and signaling specificity. Different oligomers activate different signal transduction pathways. J. Biol. Chem. 278, 50 810-50 817.
    • (2003) J. Biol. Chem. , vol.278
    • Tsao, T.S.1    Tomas, E.2    Murrey, H.E.3    Hug, C.4    Lee, D.H.5    Ruderman, N.B.6    Heuser, J.E.7    Lodish, H.F.8
  • 36
    • 0026100624 scopus 로고
    • Pre-cerebellin is a cerebellum-specific protein with similarity to the globular domain of complement C1qB chain
    • Urade Y., Oberdick J., Molinar-Rode R. and Morgan J. I. (1991) Pre-cerebellin is a cerebellum-specific protein with similarity to the globular domain of complement C1qB chain. Proc. Natl Acad. Sci. USA 88, 1069-1073.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1069-1073
    • Urade, Y.1    Oberdick, J.2    Molinar-Rode, R.3    Morgan, J.I.4
  • 37
    • 0025917540 scopus 로고
    • Molecular cloning of rat cerebellin-like protein cDNA which encodes a novel membrane-associated glycoprotein
    • Wada C. and Ohtani H. (1991) Molecular cloning of rat cerebellin-like protein cDNA which encodes a novel membrane-associated glycoprotein. Brain Res. Mol. Brain Res. 9, 71-77.
    • (1991) Brain Res. Mol. Brain Res. , vol.9 , pp. 71-77
    • Wada, C.1    Ohtani, H.2
  • 38
    • 0037494960 scopus 로고    scopus 로고
    • Cloning of adiponectin receptors that mediate antidiabetic metabolic effects
    • Yamauchi T., Kamon J., Ito Y. et al. (2003) Cloning of adiponectin receptors that mediate antidiabetic metabolic effects. Nature 423, 762-769.
    • (2003) Nature , vol.423 , pp. 762-769
    • Yamauchi, T.1    Kamon, J.2    Ito, Y.3
  • 39
    • 0024321186 scopus 로고
    • Purification and characterisation of cerebellins from human and porcine cerebellum
    • Yiangou Y., Burnet P., Nikou G., Chrysanthou B. J. and Bloom S. R. (1989) Purification and characterisation of cerebellins from human and porcine cerebellum. J. Neurochem. 53, 886-889.
    • (1989) J. Neurochem. , vol.53 , pp. 886-889
    • Yiangou, Y.1    Burnet, P.2    Nikou, G.3    Chrysanthou, B.J.4    Bloom, S.R.5
  • 40
    • 0344885580 scopus 로고    scopus 로고
    • Identification, classification, and partial characterization of genes in humans and other vertebrates homologous to a fish membrane progestin receptor
    • Zhu Y., Bond J. and Thomas P. (2003) Identification, classification, and partial characterization of genes in humans and other vertebrates homologous to a fish membrane progestin receptor. Proc. Natl Acad. Sci. USA 100, 2237-2242.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2237-2242
    • Zhu, Y.1    Bond, J.2    Thomas, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.