scholarly journals Functional and receptor binding characterization of recombinant murine macrophage inflammatory protein 2: Sequence analysis and mutagenesis identify receptor binding epitopes

1997 ◽  
Vol 6 (8) ◽  
pp. 1643-1652 ◽  
Author(s):  
L. Fred Jerva ◽  
Elias Lolis ◽  
Gail Sullivan
Keyword(s):  
Sequence Analysis ◽  
Receptor Binding ◽  
Murine Macrophage ◽  
Inflammatory Protein ◽  
Macrophage Inflammatory Protein

scholarly journals Cloning and Characterization of a Novel Murine Macrophage Inflammatory Protein-1α Receptor

1996 ◽  
Vol 271 (24) ◽  
pp. 14445-14451 ◽  
Author(s):  
Alexandra Meyer ◽  
Anthony J. Coyle ◽  
Amanda E. I. Proudfoot ◽  
Timothy N. C. Wells ◽  
Christine A. Power
Keyword(s):  
Murine Macrophage ◽  
Inflammatory Protein ◽  
Macrophage Inflammatory Protein

scholarly journals Cloning and characterization of cDNAs for murine macrophage inflammatory protein 2 and its human homologues.

1990 ◽  
Vol 172 (3) ◽  
pp. 911-919 ◽  
Author(s):  
P Tekamp-Olson ◽  
C Gallegos ◽  
D Bauer ◽  
J McClain ◽  
B Sherry ◽  
...  
Keyword(s):  
Raw 264.7 Cells ◽  
Raw 264.7 ◽  
U937 Cells ◽  
Murine Macrophage ◽  
Myristate Acetate ◽  
Platelet Factor ◽  
Inflammatory Protein ◽  
Human Genes ◽  
Macrophage Inflammatory Protein

A cDNA clone of murine macrophage inflammatory protein 2 (MIP-2) has been isolated from a library prepared from lipopolysaccharide (LPS)-stimulated RAW 264.7 cells and the nucleotide sequence determined. This cDNA was used to clone cDNAs for human homologues of MIP-2 from a library prepared from phorbol myristate acetate-treated and LPS-stimulated U937 cells. Two homologues were isolated and sequenced. Human MIP-2 alpha and MIP-2 beta are highly homologous to each other and to a previously isolated gene, human gro/melanoma growth-stimulating activity (MGSA). These three human genes, MIP-2 alpha, MIP-2 beta, and gro/MGSA, constitute a sub-family within the cytokine family represented by platelet factor 4 and interleukin 8.

scholarly journals Cloning and characterization of a novel murine macrophage inflammatory protein-1α receptor

1996 ◽  
Vol 271 (38) ◽  
pp. 23601
Author(s):  
Alexandra Meyer ◽  
Anthony J. Coyle ◽  
Amanda E.I. Proudfoot ◽  
Timothy N.C. Wells ◽  
Christine A. Power
Keyword(s):  
Murine Macrophage ◽  
Inflammatory Protein ◽  
Macrophage Inflammatory Protein

Functional characterization of rat chemokine macrophage inflammatory protein-2

Inflammation ◽  
1995 ◽  
Vol 19 (1) ◽  
pp. 133-142 ◽  
Author(s):  
Charles W. Frevert ◽  
Anthony Farone ◽  
Hadi Danaee ◽  
Joseph D. Paulauskis ◽  
Lester Kobzik
Keyword(s):  
Functional Characterization ◽  
Inflammatory Protein ◽  
Macrophage Inflammatory Protein

scholarly journals Cloning and characterization of a cDNA for murine macrophage inflammatory protein (MIP), a novel monokine with inflammatory and chemokinetic properties.

1988 ◽  
Vol 167 (6) ◽  
pp. 1939-1944 ◽  
Author(s):  
G Davatelis ◽  
P Tekamp-Olson ◽  
S D Wolpe ◽  
K Hermsen ◽  
C Luedke ◽  
...  
Keyword(s):  
Sequence Data ◽  
Signal Sequence ◽  
Sequence Similarity ◽  
Alpha Helix ◽  
Phage Library ◽  
Hydrophobic Core ◽  
Inflammatory Protein ◽  
Characteristic Signal ◽  
Macrophage Inflammatory Protein

In the course of studies on cachectin/TNF being conducted in our laboratory, a novel macrophage product has been detected and characterized. Termed macrophage inflammatory protein or MIP, this protein appears to be an endogenous mediator of the inflammatory events induced by endotoxin. A cDNA cloned probe for this protein has been isolated from a lambda gt10 phage library prepared from poly(A)+ RNA obtained of endotoxin-induced RAW264.7 cells. The sequence codes for a 92 amino acid-long polypeptide, of which 69 amino acids correspond to the mature product. The sequence predicts a molecular weight of 7,889 and structural analysis of the protein indicates a characteristic signal sequence alpha-helix and a hydrophobic core. Sequence data also confirm no sequence similarity to any other protein listed in the Dayhoff data base.

Pharmacological characterization of fever evoked by intrahypothalamic macrophage inflammatory protein-1

1990 ◽  
Vol 183 (3) ◽  
pp. 883 ◽  
Author(s):  
F.J. Miñano ◽  
M. Sancibrian ◽  
M. Vizcaino ◽  
X. Paez ◽  
G. Davatelis ◽  
...  
Keyword(s):  
Pharmacological Characterization ◽  
Inflammatory Protein ◽  
Macrophage Inflammatory Protein

scholarly journals Resolution of the two components of macrophage inflammatory protein 1, and cloning and characterization of one of those components, macrophage inflammatory protein 1 beta.

1988 ◽  
Vol 168 (6) ◽  
pp. 2251-2259 ◽  
Author(s):  
B Sherry ◽  
P Tekamp-Olson ◽  
C Gallegos ◽  
D Bauer ◽  
G Davatelis ◽  
...  
Keyword(s):  
Amino Acid ◽  
Inflammatory Responses ◽  
Inflammatory Protein ◽  
Product Comparison ◽  
Synthetic Oligonucleotide Probe ◽  
Terminal Amino ◽  
Macrophage Inflammatory Protein

A number of macrophage-derived mediators have been implicated in the vascular changes of inflammation. We recently reported the isolation of a novel monokine, macrophage inflammatory protein 1 (MIP-1), which causes local inflammatory responses in vivo, and induces superoxide production by neutrophils in vitro. Purified native MIP-1 comprises two peptides with very similar physical characteristics. We report here the resolution of MIP-1 into component peptides by SDS-hydroxylapatite chromatography, and compare the NH2-terminal sequences of the two peptides, now referred to as MIP-1 alpha and MIP-1 beta. A synthetic oligonucleotide probe pool corresponding to the NH2-terminal amino acid sequence of MIP-1 beta was used to isolate a cDNA clone containing its coding sequence. The sequence codes for a 109 amino acid-long polypeptide, of which 69 amino acids correspond to the mature product. Comparison of this MIP-1 beta cDNA with our previously cloned MIP-1 alpha sequence reveals that the MIP-1 peptides, members of a growing family of potential inflammatory mediators, are distinct but highly homologous (58.9% sequence identity) products of different genes.

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