Literature DB >> 2532148

Characterization of a glycosyl-phosphatidylinositol degrading activity in Dictyostelium discoideum membranes.

A M da Silva1, C Klein.   

Abstract

Antigen 117 is a glycolipid-anchored cell surface protein implicated in cell-cell cohesion of Dictyostelium discoideum amoebae. Previous studies have demonstrated that during cell aggregation some of the protein is released from the cell surface. Here we report the characterization of the enzymatic activity involved in the 117 antigen release. The data indicate that the releasing enzyme is a phosphatidylinositol phospholipase C. The data also indicate that structural features of glycolipid anchors are conserved in a variety of organisms.

Entities:  

Mesh:

Substances:

Year:  1989        PMID: 2532148     DOI: 10.1016/0014-4827(89)90315-7

Source DB:  PubMed          Journal:  Exp Cell Res        ISSN: 0014-4827            Impact factor:   3.905


  3 in total

1.  An uncleaved glycosylphosphatidylinositol signal mediates Ca(2+)-sensitive protein degradation.

Authors:  P C Pauly; C Klein
Journal:  Biochem J       Date:  1996-07-15       Impact factor: 3.857

2.  Lack of glycosyl-phosphatidylinositol anchoring leads to precursor retention by a unique mechanism in Dictyostelium discoideum.

Authors:  P C Pauly; C Klein
Journal:  Biochem J       Date:  1995-03-15       Impact factor: 3.857

3.  Constitutive overexpression of the contact site A glycoprotein enables growth-phase cells of Dictyostelium discoideum to aggregate.

Authors:  J Faix; G Gerisch; A A Noegel
Journal:  EMBO J       Date:  1990-09       Impact factor: 11.598

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.