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.

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

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 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

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 Molecular components of the signal sequence that function in the initiation of protein export.

1982 ◽  
Vol 95 (3) ◽  
pp. 689-696 ◽  
Author(s):  
S D Emr ◽  
T J Silhavy
Keyword(s):  
Amino Acids ◽  
Signal Sequence ◽  
Protein Localization ◽  
Helical Conformation ◽  
Hydrophobic Core ◽  
Selection Procedures ◽  
Sequence Characterization ◽  
Mutant Strains ◽  
Molecular Components

We are studying the mechanism by which the LamB protein is exported to the outer membrane of Escherichia coli. Using two selection procedures based on gene fusions, we have identified a number of mutations that cause alterations in the LamB signal sequence. Characterization of the mutant strains revealed that although many such mutations block LamB export to greater than 95%, others have essentially no effect. These results allow an analysis of the functions performed by the various molecular components of the signal sequence. Our results suggest that a critical subset of four amino acids is contained within the central hydrophobic core of the LamB signal sequence. If this core can assume an alpha-helical conformation, these four amino acids comprise a recognition site that interacts with a component of the cellular export machinery. Since mechanisms of protein localization appear to have been conserved during evolution, the principles established by these results should be applicable to similar studies in eukaryotic cells.

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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