HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) An addition or correction has been published Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hung, C.-H. Articles by Chang, G.-D. Search for Related Content PubMed PubMed Citation Articles by Hung, C.-H. Articles by Chang, G.-D. Social Bookmarking                      What's this?

Volume 272, Number 21, Issue of May 23, 1997 pp. 13772-13778
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Purification and Cloning of Carp Nephrosin, a Secreted Zinc Endopeptidase of the Astacin Family

(Received for publication, October 25, 1996, and in revised form, January 24, 1997)

Ching-Hsiang Hung , Hon-Ren Huang ^¶ , Chang-Jen Huang , Fore-Lien Huang ^¶ and Geen-Dong Chang

From the  Graduate Institute of Biochemical Sciences and ^¶ Department of Zoology, National Taiwan University, Taipei 10098 and the  Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan

We have purified a secreted proteinase of 23 kDa from carp head kidney by sequential column chromatography on a Reactive Blue 72-agarose dye affinity column and an FPLC Mono-P column. The secretion of this proteinase from carp head kidney can be stimulated by high concentrations of potassium. Since the carp proteinase is present mainly in the head kidney, kidney, and spleen (all of which are lymphohematopoietic organs), it is named nephrosin. The carp nephrosin is most sensitive to metal chelators, but not to inhibitors specific for other classes of proteinases. A cDNA clone has been isolated from a carp head kidney cDNA library by immunoscreening with a polyclonal antiserum raised against purified nephrosin. The cloned cDNA is 1086 base pairs in length and has an open reading frame encoding a protein of 273 amino acids, including a 19-amino acid signal peptide and 56-amino acid propeptide. The deduced amino acid sequence shows moderate levels of identity to medaka HCE1 (52.5%), medaka LCE (50.7%), crayfish astacin (33.2%), murine meprin- (34%), and murine meprin- (33.5%), all members of the astacin family of zinc endopeptidases. Nephrosin is the first member of the astacin family found in lymphohematopoietic tissues.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				A. Harlin-Cognato, E. A. Hoffman, and A. G. Jones Gene cooption without duplication during the evolution of a male-pregnancy gene in pipefish PNAS, December 19, 2006; 103(51): 19407 - 19412. [Abstract] [Full Text] [PDF]

				T. Kijimoto, M. Watanabe, K. Fujimura, M. Nakazawa, Y. Murakami, S. Kuratani, Y. Kohara, T. Gojobori, and N. Okada cimp1, A Novel Astacin Family Metalloproteinase Gene from East African Cichlids, Is Differentially Expressed Between Species During Growth Mol. Biol. Evol., August 1, 2005; 22(8): 1649 - 1660. [Abstract] [Full Text] [PDF]

				H.-D. Song, X.-J. Sun, M. Deng, G.-W. Zhang, Y. Zhou, X.-Y. Wu, Y. Sheng, Y. Chen, Z. Ruan, C.-L. Jiang, et al. Hematopoietic gene expression profile in zebrafish kidney marrow PNAS, November 16, 2004; 101(46): 16240 - 16245. [Abstract] [Full Text] [PDF]

				P.-L. Tsai, C.-H. Chen, C.-J. Huang, C.-M. Chou, and G.-D. Chang Purification and Cloning of an Endogenous Protein Inhibitor of Carp Nephrosin, an Astacin Metalloproteinase J. Biol. Chem., March 19, 2004; 279(12): 11146 - 11155. [Abstract] [Full Text] [PDF]

				Y. Shibata, T. Iwamatsu, Y. Oba, D. Kobayashi, M. Tanaka, Y. Nagahama, N. Suzuki, and M. Yoshikuni Identification and cDNA Cloning of Alveolin, an Extracellular Metalloproteinase, Which Induces Chorion Hardening of Medaka (Oryzias latipes) Eggs upon Fertilization J. Biol. Chem., March 17, 2000; 275(12): 8349 - 8354. [Abstract] [Full Text] [PDF]

				S. L. Schissel, G. A. Keesler, E. H. Schuchman, K. J. Williams, and I. Tabas The Cellular Trafficking and Zinc Dependence of Secretory and Lysosomal Sphingomyelinase, Two Products of the Acid Sphingomyelinase Gene J. Biol. Chem., July 17, 1998; 273(29): 18250 - 18259. [Abstract] [Full Text] [PDF]