TAILIEUCHUNG - Báo cáo khoa học: Molecular characterization and gene disruption of mouse lysosomal putative serine carboxypeptidase 1

The retinoid-inducible serine carboxypeptidase 1 (Scpep1; formerly RISC) is a lysosomal matrix protein that was initially identified in a screen for genes induced by retinoic acid. Recently, it has been spotlighted by several proteome analyses of the lysosomal compartment, but its cellular function and properties remain unknown to date. | ễFEBS Journal Molecular characterization and gene disruption of mouse lysosomal putative serine carboxypeptidase 1 Katrin Kollmann1 Markus Damme1 Florian Deuschl1 Jorg Kahle2 Rudi D Hooge3 Renate Lullmann-Rauch4 and Torben Lubke1 1 Abteilung Biochemie II Georg-August Universitat Gottingen Germany 2 Abteilung Molekularbiologie Georg-August Universitat Gottingen Germany 3 Laboratory of BiologicalPsychology KU Leuven Belgium 4 Anatomisches Institut Universitat Kiel Germany Keywords gene disruption lysosomes processing Scpepl serine carboxypeptidase Correspondence T. Lubke Zentrum Biochemie und Molekulare Zellbiologie Abteilung Biochemie II Georg-August Universitat Gottingen Heinrich-Duker-Weg 12 D-37073 Gottingen Germany Fax 49 551 395979 Tel 49 551 395932 E-mail tluebke@ Received 4 July 2008 revised 18 December 2008 accepted 23 December 2008 doi The retinoid-inducible serine carboxypeptidase 1 Scpepl formerly RISC is a lysosomal matrix protein that was initially identified in a screen for genes induced by retinoic acid. Recently it has been spotlighted by several proteome analyses of the lysosomal compartment but its cellular function and properties remain unknown to date. In this study Scpep1 from mice was analysed with regard to its intracellular processing into a mature dimer consisting of a 35 kDa N-terminal fragment and a so far unknown 18 kDa C-terminal fragment and the glycosylation status of the mature Scpep1 fragment. Although Scpep1 shares notable homology and a number of structural hallmarks with the well-described lysosomal carboxypeptidase protective protein cathepsin A the purified recombinant 55 kDa precursor and the homogenates of Scpepl-overexpressing cells do not show proteolytic activity or increased serine carboxypeptidase activity towards artificial serine carboxypeptidase substrates. Hence we disrupted the Scpepl gene in mice by a gene trap cassette resulting in a Scpep1 P-galactosidase neo-mycin .

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