Pulse-chase studies of the synthesis and intracellular transport of apolipoprotein B-100 in Hep G2 cells.
作者： K Boström , M Wettesten , J Borén , G Bondjers , O Wiklund
DOI: 10.1016/S0021-9258(18)67090-5
关键词: Intracellular 、 Hep G2 、 Golgi apparatus 、 Secretion 、 Endoplasmic reticulum 、 Biology 、 Biophysics 、 Secretory protein 、 Cell fractionation 、 Extracellular 、 Biochemistry
摘要: The synthesis and secretion of apolipoprotein B-100 (apoB-100) have been studied in a human hepatoma cell line, the Hep G2 cells. time needed for apoB-100 was estimated to be 14 min, which corresponds translation rate approximately 6 amino acids/s. ApoB-100 compared with albumin alpha 2-macroglobulin as distribution between membrane luminal content endoplasmic reticulum (ER) Golgi apparatus. results suggested that followed these secretory proteins Golgi, while ratios percent membrane-bound or were 3-4:1 ER. This may suggest occurs membrane-associated form ER prior integration lipoproteins. Pulse-chase studies combined subcellular fractionation used investigate kinetics intracellular transfer apoB-100. A 3-min pulse [35S]methionine by an increase radioactivity during first 10-15 min chase. following chase characterized linear decrease decay 6%/min. residence differed from transferrin probably also albumin. By comparing maximum denser fractions could 10 min. newly synthesized 30 indicates protein through apparatus extracellular space requires 20
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