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Publication : Identification of a novel family of non-lysosomal aspartic proteases in nematodes.

First Author  Jolodar A Year  1998
Journal  Biochim Biophys Acta Volume  1382
Issue  1 Pages  13-6
PubMed ID  9507052 Mgi Jnum  J:46119
Mgi Id  MGI:1197154 Doi  10.1016/s0167-4838(97)00141-6
Citation  Jolodar A, et al. (1998) Identification of a novel family of non-lysosomal aspartic proteases in nematodes. Biochim Biophys Acta 1382(1):13-6
abstractText  A protein encoded by cDNAs from the human parasite Onchocerca volvulus and its homologs from Caenorhabditis elegans and Ancyclostoma caninum define a family of aspartic proteases that are most closely related to cathepsins D, but differ from them in lacking the N-glycosylation site known to be required for lysosomal targeting. The nematode proteins have a potential N-glycosylation site at the same position as mammalian cathepsins E and in common with these have atypically long N-terminal extensions. The literature implies that cathepsins E may be secreted, and adult female O. volvulus are known to secrete a specific inhibitor of aspartic proteases; we therefore predict that the protease is secreted as an enzyme-inhibitor complex.
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