Processing of Mammalian Preprogastrin‐Releasing Peptide
Processing of Mammalian Preprogastrin‐Releasing Peptide
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哺乳动物前胃泌素释放肽的加工
DOI：
10.1111/j.1749-6632.1988.tb23872.x
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发表时间：
1988
影响因子：
5.2
通讯作者：
J. Walsh
中科院分区：
文献类型：
--
作者：
J. Reeve;F. Cuttitta;S. Vigna;J. Shively;J. Walsh
在哺乳动物组织和培养细胞中，孕激素原释放肽的加工是在不连续的位置进行的(图6)。信号肽酶将信号肽从胃泌素释放肽的氨基末端分离出来。外肽酶的活性可以将二肽从氨基末端移除。酰胺化位点(图6中未示出；见图2)具有与其他酰胺化肽相同的一般序列(Gly-Lys-Lys)。在单个碱基残基之后的裂解产生来自形式I或II前原GRP的基因相关产物。一种独特的非碱性切割产生了来自第三型前原GRP的基因相关产物。形成GRP、GRP和GRP基因相关肽的过程如图7所示。ProGRP被一系列酶切割，形成带有酰胺化的羧基末端蛋氨酸的GRP(图7中用星号表示)。GRP被裂解，形成十肽GRP。所有三种mRNA翻译产物的羧基末端侧翼多肽都被切割，形成几个胃泌素释放肽基因相关产物。对胃泌素释放肽及其基因相关产品的加工过程的了解将使人们能够合成这些肽的存储形式的复制品，然后用于生物测试。
The processing of preprogastrin-releasing peptide in mammalian tissues and in cultured cells takes place at discrete sites (Figure 6). Signal peptidase cleaves away the signal peptide from the amino terminus of gastrin-releasing peptide. An exopeptidase activity may remove dipeptides from the amino terminus. The amidation site (not shown in Fig. 6; see Fig. 2) has the same general sequence (Gly-Lys-Lys) seen for other amidated peptides. Cleavage after single basic residues yields gene-related products from Form I or II preproGRP. A unique non-basic cleavage yields a gene-related product from Form III preproGRP. The processing that occurs to form GRP, GRP, and GRP gene-related peptides is shown in Figure 7. ProGRP is cleaved by a series of enzymes to form GRP with an amidated carboxyl-terminal methionine (indicated by an asterisk in Fig. 7). GRP is cleaved to form the decapeptide GRP. The carboxyl-terminal flanking peptides of all three mRNA translation products are cleaved to form several gastrin-releasing peptide gene-related products. Knowledge of the processing of gastrin-releasing peptide and its gene-related products will allow synthesis of duplicates of the stored forms of these peptides, which can then be used for biological testing.
影响因子：
2.9
作者：
Koch,TR;Otterson,MF;Roddy,DR;Go,VL
通讯作者：
Go,VL