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

Authors :
Balentien E
Han JH
Thomas HG
Wen DZ
Samantha AK
Zachariae CO
Griffin PR
Brachmann R
Wong WL
Matsushima K
Source :
Biochemistry [Biochemistry] 1990 Nov 06; Vol. 29 (44), pp. 10225-33.
Publication Year :
1990

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.

Details

Language :
English
ISSN :
0006-2960
Volume :
29
Issue :
44
Database :
MEDLINE
Journal :
Biochemistry
Publication Type :
Academic Journal
Accession number :
2271650
Full Text :
https://doi.org/10.1021/bi00496a011