THE DEGRADATION OF ENDOGENOUS AND EXOGENOUS PROTEINS IN CULTURED SMOOTH-MUSCLE CELLS

THE DEGRADATION OF ENDOGENOUS AND EXOGENOUS PROTEINS IN CULTURED SMOOTH-MUSCLE CELLS
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DOI:
10.1016/0304-4165(82)90113-1
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发表时间:
1982-01-01
期刊:
BIOCHIMICA ET BIOPHYSICA ACTA
影响因子:
--
通讯作者:
VANDERWESTHUYZEN, DR
VANDERWESTHUYZEN, DR
中科院分区:
其他
文献类型:
--
作者:
BATES, PJ;COETZEE, GA;VANDERWESTHUYZEN, DR

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The pathways of degradation followed by endogenous proteins in cultured [bovine] smooth muscle cells were comapred with the well-characterized lysosomal pathway involved in the degradation of apolipoprotein B of endocytosed LDL [low density lipoprotein]. Under conditions in which lysosomal activity towards 125I-labeled LDL was almost completely inhibited by chloroquine and/or ammonium chloride, the degradation of short-lived and abnormal proteins, assessed by the release of [3H]Phe, was reduced by only 10-17%. The basal rate of degradation of long-lived proteins was reduced by .apprx. 30% by the same inhibitors while the accelerated proteolysis found under nutrient-poor conditions could be completely accounted for by the lysosomal system as defined by these lysosomotrophic agents. Temperature studies indicated differences between the mechanisms involved in the degradation of long-lived proteins (Ea [activation energy] = 18 kcal/mol) and short-lived proteins (Ea = 10 kcal/mol). Arrhenius plots for the degradation of endogenous proteins showed no transitions between 15.degree. and 37.degree. C in contrast to the breakdown of LDL which ceased below 20.degree. C. The degradation of rapid-turnover proteins is apparently largely extralysosomal and a significant breakdown of long-lived proteins also occurs outside lysosomes.