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Calpain and calpastatin in myoblast differentiation and fusion: effects of inhibitors.
Biochim Biophys Acta
September 1997
Department of Human Genetics, Sackler School of Medicine, Tel-Aviv University, Ramat Aviv, Israel.
Myoblast differentiation and fusion to multinucleated muscle cells can be studied in myoblasts grown in culture. Calpain (Ca(2+)-activated thiol protease) induced proteolysis has been suggested to play a role in myoblast fusion. We previously showed that calpastatin (the endogenous inhibitor of calpain) plays a role in cell membrane fusion.
View Article and Find Full Text PDFTranscytotic vesicle fusion with canalicular membranes is modulated by phospholipid species: implications for biliary lipid secretion.
J Gastroenterol Hepatol
July 1997
First Department of Internal Medicine, Hiroshima University School of Medicine, Japan.
Phospholipid species modulate bile metastability and the subselection of such species for biliary secretion occurs at the canalicular membrane. In this study, the role of phospholipid head groups and hydrophobic indices in transcytotic vesicle fusion with the canalicular membrane inner leaflet was investigated using rat canalicular membrane vesicles (CMV) and liposomes. The CMV were purified from Sprague-Dawley rat liver, and small unilamellar vesicles (SUV) of phosphatidylserine (PS), phosphatidylcholine (PC) and mixtures of PS/PC (1:1, 2:1 and 4:1) were labelled with 8 mol% of octadecyl rhodamine B chloride (R18).
View Article and Find Full Text PDFMammalian sperm-egg fusion: the development of rat oolemma fusibility during oogenesis involves the appearance of binding sites for sperm protein "DE".
Biol Reprod
July 1996
Instituto de Biología y Medicina Experimental, Buenos Aires, Argentina.
Rat epididymal protein DE mediates gamete fusion through complementary sites localized on the egg surface. To investigate whether these egg components are involved in the development of rat oolemma fusibility, both the presence of DE-binding components and the ability of the oolemma to fuse with sperm during oogenesis were examined. Localization of DE-complementary sites by indirect immunofluorescence revealed the absence of fluorescent labeling on growing oocytes with a diameter < 50 microns, and the presence of a uniform staining over the entire surface of germinal vesicle oocytes with a diameter > 50 microns.
View Article and Find Full Text PDFThe role of calpastatin (the specific calpain inhibitor) in myoblast differentiation and fusion.
Biochem Biophys Res Commun
March 1996
Department of Human Genetics, Sackler School of Medicine, Tel-Aviv University, Israel.
Using red cells as an experimental model, we previously showed that a limited degradation of certain membrane proteins by calpain (Ca2+-activated thiol protease) was a necessary prerequisite for cell fusion and that fusibility depended on the ratio of calpain to its endogenous inhibitor calpastatin. Here we show that fusion of rat L8 line myoblasts is accompanied by a dramatic change in the calpain/calpastatin ratio. The protein levels of mu-calpain and m-calpain increased only slightly during myoblast differentiation.
View Article and Find Full Text PDFRat erythrocytes fuse when treated with the membrane mobility agent, 2-(2-methoxyethoxy)ethyl-cis-8-(2-octylcyclopropyl)octanoate (A2C) and Ca2+, whereas human cells do not. Membrane proteolysis promoted by calpain is required for rat cell fusion [(1986) Eur. J.
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