HYDROLYSIS OF TRANSFORMING GROWTH FACTOR-ALPHA BY CELL-SURFACE PEPTIDASES INVITRO

被引：37

作者：

CHOUDRY, Y

KENNY, AJ

机构：

[1] Membrane Peptidase Res. Group, Department of Biochemistry, University of Leeds

来源：

BIOCHEMICAL JOURNAL | 1991年 / 280卷

关键词：

D O I：

10.1042/bj2800057

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Human transforming growth factor-alpha (h-TGF-alpha), a 50-amino acid residue peptide, was incubated with some purified cell-surface peptidases and with renal microvillar membranes prepared from pig and rat. Hydrolysis was monitored by h.p.l.c. and activity by a biological assay. Prolonged incubation with relatively large amounts of endopeptidase-24.11, aminopeptidase N and peptidyl dipeptidase A (angiotensin-converting enzyme) caused no observable hydrolysis and no detectable loss of biological activity. Incubation with pig renal microvilli also failed to degrade the peptide. In contrast. rat renal microvilli readily degraded h-TGF-alpha, as did endopeptidase-2, which is located in rat renal and intestinal brush borders, but is absent from pig kidneys. This enzyme degraded about 30 nmol of h-TGF-alpha/h per mg of protein. The physiological significance of these results is discussed.

引用

页码：57 / 60

页数：4

共 41 条

[31] THE METABOLISM OF NEUROPEPTIDES - HYDROLYSIS OF PEPTIDES BY THE PHOSPHORAMIDON-INSENSITIVE RAT-KIDNEY ENZYME ENDOPEPTIDASE-2 AND BY RAT MICROVILLAR MEMBRANES [J].