A Role for Sperm Surface Protein Disulfide Isomerase Activity in Gamete Fusion: Evidence for the Participation of ERp57
Autor: | Diego A. Ellerman, Paul Primakoff, Diana G. Myles |
---|---|
Rok vydání: | 2006 |
Předmět: |
Male
Time Factors Somatic cell Acrosome reaction Protein Disulfide-Isomerases Dithionitrobenzoic Acid DEVBIO Isomerase In Vitro Techniques Biology General Biochemistry Genetics and Molecular Biology Mice Bacitracin Heat shock protein medicine Animals Enzyme Inhibitors Protein disulfide-isomerase Molecular Biology Heat-Shock Proteins Membrane Fusion Proteins Sperm-Ovum Interactions Mice Inbred ICR Dose-Response Relationship Drug Acrosome Reaction Sulfhydryl Reagents Cell Biology Spermatozoa Sperm medicine.anatomical_structure Biochemistry Gamete Female Developmental Biology |
Zdroj: | Developmental Cell. 10:831-837 |
ISSN: | 1534-5807 |
Popis: | SummaryIn mammals, sperm-egg interaction is based on molecular events either unique to gametes or also present in somatic cells. In gamete fusion, it is unknown which features are gamete specific and which are shared with other systems. Conformational changes mediated by thiol-disulfide exchange are involved in the activation of some virus membrane fusion proteins. Here we asked whether that mechanism is also operative in sperm-egg fusion. Different inhibitors of protein disulfide isomerase (PDI) activity were able to inhibit sperm-egg fusion in vitro. While pretreatment of oocytes had no effect, pretreatment of sperm reduced their fusion ability. Some members of the PDI family were detected on the sperm head, and use of specific antibodies and substrates suggested that the oxidoreductase ERp57 has a role in gamete fusion. The results support the idea that thiol-disulfide exchange is a mechanism that may act in gamete fusion to produce conformational changes in fusion-active proteins. |
Databáze: | OpenAIRE |
Externí odkaz: |