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Publication : Characterization of Dictyostelium discoideum cathepsin D.

First Author  Journet A Year  1999
Journal  J Cell Sci Volume  112 ( Pt 21)
Pages  3833-43 PubMed ID  10523518
Mgi Jnum  J:58534 Mgi Id  MGI:1347764
Doi  10.1242/jcs.112.21.3833 Citation  Journet A, et al. (1999) Characterization of Dictyostelium discoideum cathepsin D. J Cell Sci 112(Pt 21):3833-43
abstractText  Previous studies using magnetic purification of Dictyostelium discoideum endocytic vesicles led us to the identification of some major vesicle proteins. Using the same purification procedure, we have now focused our interest on a 44 kDa soluble vesicle protein. Microsequencing of internal peptides and subsequent cloning of the corresponding cDNA identified this protein as the Dictyostelium homolog of mammalian cathepsins D. The only glycosylation detected on Dictyostelium cathepsin D (CatD) is common antigen 1, a cluster of mannose 6-sulfate residues on N-linked oligosaccharide chains. CatD intracellular trafficking has been studied, showing the presence of the protein throughout the entire endocytic pathway. During the differentiation process, the catD gene presents a developmental regulation, which is also observed at the protein level. catD gene disruption does not alter significantly the cell behaviour, either in the vegetative form or the differentiation stage. However, modifications in the SDS-PAGE profiles of proteins bearing common antigen 1 were detected, when comparing parental and catD(-) cells. These modifications point to a possible role of CatD in the maturation of a few Dictyostelium lysosomal proteins.
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