Co-localization of receptor and transducer proteins in the glycosphingolipid-enriched, low density, detergent-insoluble membrane fraction of sea urchin sperm

The low density, detergent-insoluble membrane fraction (LD-DIM), where gangliosides are likely to be highly enriched, was prepared from sperm of two sea urchin species, Hemicentrotus pulcherrimus and Strongylocentrotus purpuratus. Immunoblotting showed the presence in the LD-DIM of two receptors for...

Full description

Saved in:
Bibliographic Details
Published in:Glycoconjugate journal 2000-03, Vol.17 (3 -4), p.205-214
Main Authors: Ohta, K, Sato, C, Matsuda, T, Toriyama, M, Vacquier, V D, Lennarz, W J, Kitajima, K
Format: Article
Language:English
Subjects:
Animals
Blotting, Western
Carbohydrate Sequence
Cell Membrane - chemistry
Cell Membrane - metabolism
Detergents - chemistry
Echinoidea
Fluorescent Antibody Technique
Gangliosides - immunology
Gangliosides - metabolism
Glycosphingolipids - chemistry
Glycosphingolipids - metabolism
GTP-Binding Protein alpha Subunits, Gs - metabolism
Hemicentrotus pulcherrimus
Male
Molecular Sequence Data
Precipitin Tests
Proteins
Receptors, Cell Surface - metabolism
Sea Urchins
Signal transduction
Solubility
Spermatozoa - chemistry
Spermatozoa - metabolism
Strongylocentrotus purpuratus
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The low density, detergent-insoluble membrane fraction (LD-DIM), where gangliosides are likely to be highly enriched, was prepared from sperm of two sea urchin species, Hemicentrotus pulcherrimus and Strongylocentrotus purpuratus. Immunoblotting showed the presence in the LD-DIM of two receptors for egg ligands, a glycosylphosphatidylinositol (GPI)-anchored protein, and four proteins which may be involved in signal transduction. Co-immunoprecipitation revealed that at least three proteins, the speract receptor, the 63kDa GPI-anchored protein and the alpha subunit of a heterotrimeric Gs protein, are localized in the LD-DIM. This suggests that the LD-DIM fraction may be a membrane microdomain for speract-speract receptor interaction, as well as the subsequent signal transduction pathway involved in induction of sperm respiration, motility and possibly the acrosome reaction.
ISSN:0282-0080
1573-4986
DOI:10.1023/a:1026589223811