Degradation of human apolipoprotein B-100 by apolipoprotein(a)
- 27 December 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 336 (2), 327-329
- https://doi.org/10.1016/0014-5793(93)80830-n
Abstract
Human plasma low density lipoproteine (LDL) contain a very high molecular weight protein termed apoB-100 (Mr = 550,000). In many samples of LDL, minor components designated as apoB-74 (Mr = 407,000) and apoB-26 (Mr = 145,000) are present. It has been shown that they can arise as a result of proteolytic degradation of apoB-100. Our earlier studies demonstrated that the active forms of lipoprotein(a) (LP(a)) and apolipoprotein(a) (apo(a)) possess proteolytic activity. In the present study we investigated the possibility of apoB-100 degradation in the presence of activated apo(a). LDL were incubated with the purified apo(a) and analyzed by SDS-polyacrylamide gel electrophoresis. It was found that apoB is cleaved by apo(a) with formation of proteolytic fragments including B-74 and B-26. The physiological significance of apoB degradation under the action of apo(a) is consideredKeywords
This publication has 7 references indexed in Scilit:
- Enzymatic properties of active form of human apolipoprotein (a)Biochemical and Biophysical Research Communications, 1990
- cDNA sequence of human apolipoprotein(a) is homologous to plasminogenNature, 1987
- Heterogeneity of apolipoprotein B: isolation of a new species from human chylomicrons.Proceedings of the National Academy of Sciences, 1980
- The Low-Density Lipoprotein Pathway and its Relation to AtherosclerosisAnnual Review of Biochemistry, 1977
- Prostaglandins as Potentiators of Increased Vascular Permeability in InflammationNature, 1973
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- THE DISTRIBUTION AND CHEMICAL COMPOSITION OF ULTRACENTRIFUGALLY SEPARATED LIPOPROTEINS IN HUMAN SERUMJournal of Clinical Investigation, 1955