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Membrane sialoglycoprotein from human erythrocytes activates lysosomal proteinases.
Metadata
JournalActa Biol Med GerNot FoundDate
1979
Type
Journal Article
Volume
1979 / 38 : 1521-6
Author
Böhmer FD , Kirschke H , Bohley P , Schön R
Doi
Not Found
PMIDMESH
Animals
Cathepsins
Cell-Free System
Dose-Response Relationship, Drug
Endopeptidases
Enzyme Activation
Glycophorins
Humans
Hydrogen-Ion Concentration
Liver
Lysosomes
Rats
Sialoglycoproteins
Abstract
The capacity of membrane glycoproteins to interact with proteinases was investigated in the model system: Membrane sialoglycoprotein from human erythrocytes (glycophorin) and lysosomal proteinases from rat liver. Glycophorin was found to stimulate the activity of a lysosomal proteinase mixture up to about 150% at pH 6.9. Cathepsin L was found to be the primarily stimulated proteinase. The stoichiometry in the saturation range of the dose-response curve waas about 10 to 20 molecules glycophorin per molecule cathepsin L. The mechanism of the activation is unknown. Interactions of this type may be of importance for the regulation of cell proliferation on the level of cell membranes.
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Acta Biol Med GerActa biologica et medica Germanica
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