BIOSYNTHESIS AND AXONAL-TRANSPORT OF RAT NEUROHYPOPHYSEAL PROTEINS AND PEPTIDES
BIOSYNTHESIS AND AXONAL-TRANSPORT OF RAT NEUROHYPOPHYSEAL PROTEINS AND PEPTIDES
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DOI:
10.1083/jcb.73.2.366
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发表时间:
1977-01-01
影响因子:
7.8
通讯作者:
BROWNSTEIN, MJ
中科院分区:
文献类型:
--
作者:
GAINER, H;SARNE, Y;BROWNSTEIN, MJ
35S-cysteine injected adjacent to the supraoptic nucleus (SON) of the rat is rapidly incorporated into proteins. These 35S-cysteine-labeled proteins in the SON (1-24 h after injection) were separated by polyacrylamide gel electrophoresis, and the distribution of radioactive proteins on the gels was analyzed. One hour after injection, about 73% of the radioactivity appeared in 2 peaks (both about 20,000 MW). With time, these peaks (putative precursors of neurophysin) decreased, as a 12,000 MW peak (containing 2 distinct neurophysins) increased in radioactivity. Both the 20,000 and 12,000 MW proteins are transported into the axonal (median eminence) and nerve terminal (posterior pituitary) regions of the rat hypothalamo-neurohypophysial system. Conversion of the larger precursor protein to the smaller neurophysin appears to occur, in large part, intra-axonally during axonal transport. Six distinct 35S-cysteine-labeled peptides (< 2500 MW), in addition to arginine vasopressin and oxytocin, are also synthesized in the SON and transported to the posterior pituitary where they are released together with labeled neurophysin by K depolarization in the presence of extracellular Ca. These data provide support for the hypothesis that the neurohypophysial peptides (vasopressin and oxytocin) and neurophysins are derived from the post-translational cleavage of protein precursors synthesized in the SON, and that the conversion process can occur in the neurosecretory granule during axonal transport.