Aron D C, Andrews P C, Dixon J E, Roos B A
Biochem Biophys Res Commun. 1984 Oct 30;124(2):450-6. doi: 10.1016/0006-291x(84)91574-2.
Rat prosomatostatin was isolated from a somatostatin-producing cell line and was partially microsequenced. This indicated the amino terminal structure of cellular prosomatostatin and implied a 92-amino acid sequence for the somatostatin precursor. Based on the structure for cellular prosomatostatin, a peptide was synthesized and used to develop a radioimmunoassay directed toward the amino terminal portion of prosomatostatin. This assay has revealed two peptides containing the amino-terminal portion of prosomatostatin in a somatostatin-secreting CA-77 rat medullary thyroid carcinoma cell line. These two peptides - MW 4000 and 8000 daltons - lack somatostatin immunoreactivity. Thus, processing of prosomatostatin occurs both at the amino and carboxyl regions. These results open the way for elucidation of the structure, function and metabolism of non-somatostatin peptides derived from the amino terminus of prosomatostatin.
大鼠前生长抑素是从一个产生生长抑素的细胞系中分离出来的，并进行了部分微测序。这表明了细胞前生长抑素的氨基末端结构，并暗示生长抑素前体有一个92个氨基酸的序列。基于细胞前生长抑素的结构，合成了一种肽，并用于开发针对前生长抑素氨基末端部分的放射免疫测定法。该测定法在分泌生长抑素的CA - 77大鼠甲状腺髓样癌细胞系中发现了两种含有前生长抑素氨基末端部分的肽。这两种肽——分子量分别为4000和8000道尔顿——缺乏生长抑素免疫反应性。因此，可以看出前生长抑素在氨基和羧基区域均会发生加工处理。这些结果为阐明源自前生长抑素氨基末端的非生长抑素肽的结构、功能和代谢开辟了道路。
