Characterization of the non-functional Fas ligand of gld mice

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Serval ID
serval:BIB_0BA9B77E7F43
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Characterization of the non-functional Fas ligand of gld mice
Journal
International Immunology
Author(s)
Hahne  M., Peitsch  M. C., Irmler  M., Schroter  M., Lowin  B., Rousseau  M., Bron  C., Renno  T., French  L., Tschopp  J.
ISSN
0953-8178 (Print)
Publication state
Published
Issued date
09/1995
Volume
7
Number
9
Pages
1381-6
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Sep
Abstract
Mice homozygous for either the gld or lpr mutation develop autoimmune diseases and progressive lymphadenopathy. The lpr mutation is characterized by the absence of functional Fas, whereas gld mice exhibit an inactive FasL due to a point mutation proximal to the extracellular C-terminus. The structural repercussions of this amino acid substitution remain unknown. Here we report that FasL is expressed at similar levels on the surface of activated T lymphocytes from gld and wild-type mice. Using a polyclonal anti-FasL antibody, indistinguishable amounts of a 40 kDa protein are detected in both gld and wild-type splenocytes. The molecular model of FasL, based on the known structure of TNF-alpha, predicts that the Phe --> Leu gld mutation is located at the protomer interface which is close to the FasR interaction site. We conclude that the gld mutation allows normal FasL biosynthesis, surface expression and oligomerization, but induces structural alterations to the Fas binding region leading to the phenotypic changes observed.
Keywords
Amino Acid Sequence Animals Autoimmune Diseases/*genetics Base Sequence Fas Ligand Protein Humans Membrane Glycoproteins/analysis/*chemistry/genetics Mice Mice, Mutant Strains Molecular Sequence Data Mutation Protein Conformation Rats T-Lymphocytes/chemistry
Pubmed
Web of science
Open Access
Yes
Create date
24/01/2008 16:19
Last modification date
01/10/2019 7:16
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