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

This Article Full Text (PDF) Alert me when this article is cited 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 Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Ishidoh, K. Articles by Kominami, E. Search for Related Content PubMed PubMed Citation Articles by Ishidoh, K. Articles by Kominami, E. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 266, Issue 25, 16312-16317, Sep, 1991

Molecular cloning of cDNA for rat cathepsin C. Cathepsin C, a cysteine proteinase with an extremely long propeptide

K Ishidoh, D Muno, N Sato and E Kominami
Department of Biochemistry, Juntendo University School of Medicine, Tokyo, Japan.

A cDNA for rat cathepsin C (dipeptidylaminopeptidase I) was isolated. The deduced amino acid sequence of cathepsin C comprises 462 amino acid residues: 28 NH2-terminal residues corresponding to the signal peptide, 201 residues corresponding to the propeptide, and 233 COOH-terminal residues corresponding to the mature enzyme region. Four potential glycosylation sites were found, three located in the propeptide region, and one in the mature enzyme region. The amino acid sequence of mature cathepsin C has 39.5% identity to that of cathepsin H, 35.1% to that of cathepsin L, 30.1% to that of cathepsin B, and 33.3% to that of papain. Cathepsin C, therefore, is a member of the papain family, although its propeptide region is much longer than those of other cysteine proteinases and shows no significant amino acid sequence similarity to any other cysteine proteinase.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				N. Methot, J. Rubin, D. Guay, C. Beaulieu, D. Ethier, T. J. Reddy, D. Riendeau, and M. D. Percival Inhibition of the Activation of Multiple Serine Proteases with a Cathepsin C Inhibitor Requires Sustained Exposure to Prevent Pro-enzyme Processing J. Biol. Chem., July 20, 2007; 282(29): 20836 - 20846. [Abstract] [Full Text] [PDF]

				M. Horn, M. Baudys, Z. Voburka, I. Kluh, J. Vondrasek, and M. Mares Free-thiol Cys331 exposed during activation process is critical for native tetramer structure of cathepsin C (dipeptidyl peptidase I) Protein Sci., April 1, 2002; 11(4): 933 - 943. [Abstract] [Full Text] [PDF]

				P. J. Wolters, M. Laig-Webster, and G. H. Caughey Dipeptidyl Peptidase I Cleaves Matrix-Associated Proteins and Is Expressed Mainly by Mast Cells in Normal Dog Airways Am. J. Respir. Cell Mol. Biol., February 1, 2000; 22(2): 183 - 190. [Abstract] [Full Text]

				P. J. Wolters, W. W. Raymond, J. L. Blount, and G. H. Caughey Regulated Expression, Processing, and Secretion of Dog Mast Cell Dipeptidyl Peptidase I J. Biol. Chem., June 19, 1998; 273(25): 15514 - 15520. [Abstract] [Full Text] [PDF]

				N. V. Rao, G. V. Rao, and J. R. Hoidal Human Dipeptidyl-peptidase I. GENE CHARACTERIZATION, LOCALIZATION, AND EXPRESSION J. Biol. Chem., April 11, 1997; 272(15): 10260 - 10265. [Abstract] [Full Text] [PDF]

				I. Dolenc, B. Turk, G. Pungercic, A. Ritonja, and V. Turk Oligomeric Structure and Substrate Induced Inhibition of Human Cathepsin C J. Biol. Chem., September 15, 1995; 270(37): 21626 - 21631. [Abstract] [Full Text] [PDF]

				K. Ariizumi, G.-L. Shen, S. Shikano, S. Xu, R. Ritter III, T. Kumamoto, D. Edelbaum, A. Morita, P. R. Bergstresser, and A. Takashima Identification of a Novel, Dendritic Cell-associated Molecule, Dectin-1, by Subtractive cDNA Cloning J. Biol. Chem., June 23, 2000; 275(26): 20157 - 20167. [Abstract] [Full Text] [PDF]