4 SECRETORY PROTEINS SYNTHESIZED BY HEPATOCYTES ARE TRANSPORTED FROM ENDOPLASMIC-RETICULUM TO GOLGI-COMPLEX AT DIFFERENT RATES
4 SECRETORY PROTEINS SYNTHESIZED BY HEPATOCYTES ARE TRANSPORTED FROM ENDOPLASMIC-RETICULUM TO GOLGI-COMPLEX AT DIFFERENT RATES
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DOI:
10.1002/j.1460-2075.1984.tb01775.x
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发表时间:
1984-01-01
期刊:
影响因子:
11.4
通讯作者:
PETERSON, PA
中科院分区:
文献类型:
--
作者:
FRIES, E;GUSTAFSSON, L;PETERSON, PA
Pulse-chase experiments in conjunction with subcellular fractionation and quantitative immunoprecipitation were used to study the intracellular transport of 4 secretory proteins, albumin, transferrin, prealbumin and retinol-binding protein, in isolated rat hepatocytes. The proteins were transported from the endoplasmic reticulum (ER) to the Golgi complex (GC) at greatly different rates (t1/2 [half-time] = 14-137 min), indicating that transport of secretory proteins between these organelles is effected by a selective, possibly receptor-mediated process and not through bulk phase transfers. The transport from the Golgi complex to the medium was rapid for all proteins (t1/2 .apprx. 15 min) and possibly occurred at the same rate. Consistent with these kinetic data, the amount of a rapidly transported protein (albumin) in the GC fraction was high (relative to its amount in the ER fraction) whereas the amount of a slowly transported protein (transferrin) in the GC fraction was low, as determined by radioimmunoassays.