Back to Search
Start Over
Recombinant expression, biochemical characterization, and biological activities of the human MGSA/gro protein.
- 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.
- Subjects :
- Amino Acid Sequence
Animals
Binding, Competitive
Cell Division drug effects
Cell Line
Chemokine CXCL1
Chemotaxis, Leukocyte drug effects
Cricetinae
Cricetulus
DNA genetics
Fibroblasts metabolism
Genetic Vectors
Humans
Interleukin-8 metabolism
Melanoma pathology
Molecular Sequence Data
Neoplasm Proteins genetics
Neoplasm Proteins isolation & purification
Neoplasm Proteins pharmacology
Neutrophils drug effects
Neutrophils metabolism
Recombinant Fusion Proteins isolation & purification
Recombinant Fusion Proteins pharmacology
Tumor Cells, Cultured drug effects
Chemokines, CXC
Growth Substances genetics
Growth Substances isolation & purification
Growth Substances pharmacology
Intercellular Signaling Peptides and Proteins
Subjects
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