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. |