Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
12
|
| pubmed:dateCreated |
1990-7-18
|
| pubmed:abstractText |
Two populations of Leishmania donovani chagasi promastigotes resistant to the lethal effects of tunicamycin (TM), an inhibitor of N-linked glycosylation, were raised. These parasites exhibited altered patterns of glycosylation when compared to wild-type controls. In particular the major surface glycoprotein gp63 was present in membranes of one population of TM-resistant promastigotes (population 1) primarily in a deglycosylated form, which migrated at a lower Mr than wild-type gp63. The deglycosylated protein was proteolytically inactive on substrate-containing gels, in contrast to glycosylated gp63. Assays of promastigote attachment to human macrophages revealed that, despite a proposed role for gp63 protease activity in binding to macrophage receptors, population 1 TM-resistant promastigotes appeared to attach to the CR3 but not to the mannose-fucose receptor. Control promastigotes bound to both receptors. In contrast, a second population of TM-resistant promastigotes (population 2) did not produce gp63 that could be detected on immunoblots, either in a glycosylated or deglycosylated form. The latter TM-resistant promastigotes bound to neither CR3 nor the mannose-fucose receptor, suggesting that expression of gp63 might be important for promastigotes to bind to CR3. LPG was present in immunoblots of both TM-resistant and control populations suggesting this molecule might not account for the differences in attachment. Surprisingly both TM-resistant promastigote populations contained gp63 mRNA by Northern analysis in apparently equal amounts. We conclude that N-glycosylation is probably necessary for the protease function of gp63, but that neither N-glycosylation nor protease activity of gp63 is necessary for L. donovani chagasi promastigotes to bind to CR3. Furthermore the expression of gp63 protein by TM-resistant promastigotes is dependent upon postranscriptional events.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
AIM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Concanavalin A,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins, C-Type,
http://linkedlifedata.com/resource/pubmed/chemical/Mannose-Binding Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Tunicamycin,
http://linkedlifedata.com/resource/pubmed/chemical/glycoprotein gp63, Leishmania,
http://linkedlifedata.com/resource/pubmed/chemical/mannose receptor
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0022-1767
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
144
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
4825-34
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:2191040-Animals,
pubmed-meshheading:2191040-Blotting, Northern,
pubmed-meshheading:2191040-Blotting, Western,
pubmed-meshheading:2191040-Concanavalin A,
pubmed-meshheading:2191040-Drug Resistance,
pubmed-meshheading:2191040-Glycosylation,
pubmed-meshheading:2191040-Integrins,
pubmed-meshheading:2191040-Lectins, C-Type,
pubmed-meshheading:2191040-Leishmania donovani,
pubmed-meshheading:2191040-Mannose-Binding Lectins,
pubmed-meshheading:2191040-Membrane Glycoproteins,
pubmed-meshheading:2191040-Metalloendopeptidases,
pubmed-meshheading:2191040-Molecular Weight,
pubmed-meshheading:2191040-Peptide Hydrolases,
pubmed-meshheading:2191040-Protozoan Proteins,
pubmed-meshheading:2191040-RNA, Messenger,
pubmed-meshheading:2191040-Receptors, Cell Surface,
pubmed-meshheading:2191040-Receptors, Immunologic,
pubmed-meshheading:2191040-Tunicamycin
|
| pubmed:year |
1990
|
| pubmed:articleTitle |
The major Leishmania donovani chagasi surface glycoprotein in tunicamycin-resistant promastigotes.
|
| pubmed:affiliation |
Department of Internal Medicine, VA Medical Center, Iowa City, IA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|