人MGSA/gro蛋白的重组表达、生化特性及生物学活性

Recombinant expression, biochemical characterization, and biological activities of the human MGSA/gro protein.

作者信息

Balentien E, Han J H, Thomas H G, Wen D Z, Samantha A K, Zachariae C O, Griffin P R, Brachmann R, Wong W L, Matsushima K

机构信息

Department of Developmental Biology, Genentech Inc., South San Francisco, California 94080.

出版信息

Biochemistry. 1990 Nov 6;29(44):10225-33. doi: 10.1021/bi00496a011.

DOI:10.1021/bi00496a011

PMID:2271650

Abstract

Melanoma growth stimulatory activity (MGSA) is a mitogenic protein secreted by Hs294T melanoma cells that corresponds to the polypeptide encoded by the human gro gene. The MGSA/gro cDNA has been expressed in mammalian cells and the secreted recombinant factor has been purified. Biochemical and biological characterization shows that the recombinant protein is identical with the natural protein and is devoid of posttranslational glycosylation, sulfation, and phosphorylation. The two C-terminal amino acids are proteolytically removed from the mature recombinant MGSA, indicating a length of 71 instead of the predicted 73 amino acids. The recombinant MGSA is mitogenically active on the Hs294T melanoma cells. The purified MGSA competes with interleukin 8 for binding to neutrophil receptors and exhibits neutrophil chemotactic activity equivalent to that of interleukin 8.

摘要

黑色素瘤生长刺激活性（MGSA）是一种由Hs294T黑色素瘤细胞分泌的促有丝分裂蛋白，它与人gro基因编码的多肽相对应。MGSA/gro cDNA已在哺乳动物细胞中表达，分泌的重组因子已被纯化。生化和生物学特性表明，重组蛋白与天然蛋白相同，且没有翻译后糖基化、硫酸化和磷酸化。成熟的重组MGSA经蛋白水解作用去除了两个C末端氨基酸，表明其长度为71个氨基酸，而非预测的73个氨基酸。重组MGSA对Hs294T黑色素瘤细胞具有促有丝分裂活性。纯化的MGSA与白细胞介素8竞争结合中性粒细胞受体，并表现出与白细胞介素8相当的中性粒细胞趋化活性。