TY - JOUR
T1 - Apolipoprotein-E degradation in human very low density lipoproteins by plasma protease(s)
T2 - Chemical and biological consequences
AU - Bradley, William A.
AU - Gilliam, Ellen B.
AU - Gotto, Antonio
AU - Gianturco, Sandra H.
N1 - Funding Information:
This work was supported in part by grants from the National Heart, Lung and Blood Institute, HL-17269, a Specialized Center of Research (SCOR), HL 27341 and the American Heart Association, 80875.
PY - 1982/12/31
Y1 - 1982/12/31
N2 - Serine proteases coisolate with human very low density lipoproteins (VLDL) which degrade apolipoprotein E and cause hypertriglyceridemic VLDL to lose the ability to interact with the LDL receptor of human skin fibroblasts. We identified proteolytic fragments of apolipoprotein-E in isolated VLDL which can be produced by the action of thrombin on purified apoE. There are two major thrombin cleavage products: Mr ∼ 22,000 (E-22) and Mr ∼ 12,000 (E-12), the N- and C-terminal fragments, respectively, of apoE. We conclude that the structural integrity and the ability of VLDL to interact with cell receptors are a function of not only VLDL constituents but also of the extent to which VLDL apoprotein E has been degraded.
AB - Serine proteases coisolate with human very low density lipoproteins (VLDL) which degrade apolipoprotein E and cause hypertriglyceridemic VLDL to lose the ability to interact with the LDL receptor of human skin fibroblasts. We identified proteolytic fragments of apolipoprotein-E in isolated VLDL which can be produced by the action of thrombin on purified apoE. There are two major thrombin cleavage products: Mr ∼ 22,000 (E-22) and Mr ∼ 12,000 (E-12), the N- and C-terminal fragments, respectively, of apoE. We conclude that the structural integrity and the ability of VLDL to interact with cell receptors are a function of not only VLDL constituents but also of the extent to which VLDL apoprotein E has been degraded.
UR - http://www.scopus.com/inward/record.url?scp=0020314852&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0020314852&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(82)91927-1
DO - 10.1016/0006-291X(82)91927-1
M3 - Article
C2 - 6301435
AN - SCOPUS:0020314852
SN - 0006-291X
VL - 109
SP - 1360
EP - 1367
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -