Loss of covalently labeled glycoproteins and glycolipids from the surface of newly transformed schistosomula of Schistosoma mansoni.
Open Access
- 1 August 1982
- journal article
- research article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 94 (2) , 363-369
- https://doi.org/10.1083/jcb.94.2.363
Abstract
Schistosomula of Schistosoma mansoni were labeled by oxidation with galactose oxidase or with periodate followed by reduction with NaB3H4 to study the loss of the surface membrane of these parasites in vitro. Grain counts of light microscope autoradiographs (LMARG) of radiolabeled schistosomula show that both galactose oxidase and periodate specifically label the surface of the organisms. Galactose oxidase labels 11 glycoproteins on the surface of skin and mechanical schistosomula, ranging in apparent molecular weight from 17,000 to greater than 105,000. These glycoproteins are lost from the surface of schistosomula with a halftime of 10-15 h in culture in defined medium. Most of these glycoproteins appear to be shed intact from the surface of the schistosomula rather than endocytosed and degraded, because greater than 50% of each of the lost proteins can be recovered by trichloroacetic acid precipitation of the culture medium and because there is no internalization of the radiolabels into cultured schistosomula examined by LMARG. In addition to glycoproteins, periodate labels at least seven glycolipids on the surface of mechanical schistosomula. After culture for 15 h, more than half of each of these periodate-labeled proteins and lipids are lost from the schistosomula, and their abundance relative to each other remains similar to that of freshly labeled organisms. Since both proteins and lipids are lost from the surface of the schistosomula at the same rate, we believe that we are observing a general loss of the parasite surface membrane.This publication has 21 references indexed in Scilit:
- Schistosoma mansoni: Analysis of surface membrane carbohydrates using lectinsExperimental Parasitology, 1978
- Selective radioactive labeling of cell surface sialoglycoproteins by periodate-tritiated borohydride.Journal of Biological Chemistry, 1977
- Quantitative Film Detection of 3H and 14C in Polyacrylamide Gels by FluorographyEuropean Journal of Biochemistry, 1975
- A Film Detection Method for Tritium‐Labelled Proteins and Nucleic Acids in Polyacrylamide GelsEuropean Journal of Biochemistry, 1974
- GOLGI FRACTIONS PREPARED FROM RAT LIVER HOMOGENATESThe Journal of cell biology, 1973
- Schistosoma mansoni: Topochemical features of cercariae, schistosomula, and adultsExperimental Parasitology, 1973
- External Labeling of Cell Surface Galactose and Galactosamine in Glycolipid and Glycoprotein of Human ErythrocytesJournal of Biological Chemistry, 1973
- A reagent for the non-destructive location of steroids and some other lipophilic materials on silica gel thin-layer chromatogramsJournal of Chromatography A, 1971
- Effect of Modification of N-Acetylneuraminic Acid on the Binding of Glycoproteins to Influenza Virus and on Susceptibility to Cleavage by NeuraminidaseJournal of Biological Chemistry, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970