Human monocyte chemoattractant protein-1 expressed in a baculovirus system

Human monocyte chemoattractant protein-1 (hMCP-1) was produced using a baculovirus system. The h MCP-1 cDNA was inserted into the genomic DNA of Autographa californica nuclear polyhedrosis virus (AcNPV) using a transfer vector, pJVP10Z. Spodoptera frugiperda insect cells, which were infected with th...

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Veröffentlicht in:	Gene 1994-03, Vol.140 (2), p.267-272
Hauptverfasser:	Ueda, Atsuhisa, Kawamoto, Susumu, Igarashi, Toshihisa, Ishigatsubo, Yoshiaki, Tani, Kenji, Okubo, Takao, Okuda, Kenji
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Autographa californica nuclear polyhedrosis virus Base Sequence Biological and medical sciences Cell Line Chemokine CCL2 Chemotactic Factors - biosynthesis Chemotactic Factors - chemistry Chemotactic Factors - genetics Chemotactic Factors - isolation & purification Cloning, Molecular DNA expression vector Fundamental and applied biological sciences. Psychology Glycosylation Humans lymphokine Molecular Sequence Data Moths Nucleopolyhedrovirus - genetics Protein hormones. Growth factors. Cytokines Proteins Recombinant DNA Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification
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Zusammenfassung:	Human monocyte chemoattractant protein-1 (hMCP-1) was produced using a baculovirus system. The h MCP-1 cDNA was inserted into the genomic DNA of Autographa californica nuclear polyhedrosis virus (AcNPV) using a transfer vector, pJVP10Z. Spodoptera frugiperda insect cells, which were infected with this recombinant virus, secreted recombinant hMCP-1 (re-hMCP-1) at the level of 10–20 μg/ml of culture medium. This product was shown to chemoattract monocytes. Three distinct bands of 11,11.5 and 12 kDa were revealed by immunoblotting analysis, and this heterogeneity was assigned to differences in carbohydrate processing. N-terminal amino-acid sequence analysis of the purified product revealed identity with hMCP-1. Thus, in this system, re-hMCP-1 was produced in large quantities and modified in a manner similar to native hMCP-1.
ISSN:	0378-1119 1879-0038
DOI:	10.1016/0378-1119(94)90556-8