Title: The propeptide of preprosomatostatin mediates intracellular transport and secretion of alpha-globin from mammalian cells Document date: 1989_5_1
ID: kjid2e3q_41
Snippet: Our data are similar to those reported by Lippincott-Schwartz et al. (18) and Chen et al. (6) who demonstrated degradation of incompletely assembled T cell receptor (TCR) o~-or A-subunits in the ER. The kinetics of globin degradation were significantly faster than for the TCR or-and A-subunits; we did not observe a lag period of 20 min before degradation and the half-life of globin was 4-5 min compared to •50 min for TCR or-chains. These result.....
Document: Our data are similar to those reported by Lippincott-Schwartz et al. (18) and Chen et al. (6) who demonstrated degradation of incompletely assembled T cell receptor (TCR) o~-or A-subunits in the ER. The kinetics of globin degradation were significantly faster than for the TCR or-and A-subunits; we did not observe a lag period of 20 min before degradation and the half-life of globin was 4-5 min compared to •50 min for TCR or-chains. These results suggest the presence of enzymes which recognize and rapidly degrade "aberrant" proteins. This function may be distinct from any role BiP, the heavy chain binding protein (3), may have in controlling export of proteins from the ER. Our data and those on TCR assembly (6, 18) suggest that the ER or an "early" Golgi compartment has multiple proofreading mechanisms which regulate the flow of proteins through the secretory apparatus.
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