Recombinant human MCP-1/JE induces chemotaxis, calcium flux, and the respiratory burst in human monocytes

Blood ◽  
1991 ◽  
Vol 78 (4) ◽  
pp. 1112-1116 ◽  
Author(s):  
BJ Rollins ◽  
A Walz ◽  
M Baggiolini
Keyword(s):  
Growth Factor ◽  
Respiratory Burst ◽  
Specific Activity ◽  
Calcium Flux ◽  
Human Neutrophils ◽  
Free Calcium ◽  
Secretory Proteins ◽  
Predicted Amino Acid Sequence ◽  
Human Monocytes ◽  
Inducible Gene

Abstract The JE gene was first described as a platelet-derived growth factor (PDGF)-inducible gene in mouse 3T3 cells. The human homologue of JE encodes a protein whose predicted amino acid sequence is identical to that of the monocyte chemoattractant MCP-1 (also called MCAF and SMC- CF), which belongs to a recently identified family of small secretory proteins with cytokine properties. We purified recombinant human MCP- 1/JE (hMCP-1/JE) produced in COS cells and demonstrated that it is chemotactic for human monocytes with a specific activity similar to natural MCP-1. In addition, pure recombinant hMCP-1/JE stimulates monocytes, inducing an increase in cytosolic free calcium and the respiratory burst, but is completely inactive on human neutrophils. These results help to define functionally a well-known growth factor- inducible gene and a member of a new family of cytokines.

scholarly journals Recombinant human MCP-1/JE induces chemotaxis, calcium flux, and the respiratory burst in human monocytes

Blood ◽  
1991 ◽  
Vol 78 (4) ◽  
pp. 1112-1116 ◽  
Author(s):  
BJ Rollins ◽  
A Walz ◽  
M Baggiolini
Keyword(s):  
Growth Factor ◽  
Respiratory Burst ◽  
Specific Activity ◽  
Calcium Flux ◽  
Human Neutrophils ◽  
Free Calcium ◽  
Secretory Proteins ◽  
Predicted Amino Acid Sequence ◽  
Human Monocytes ◽  
Inducible Gene

The JE gene was first described as a platelet-derived growth factor (PDGF)-inducible gene in mouse 3T3 cells. The human homologue of JE encodes a protein whose predicted amino acid sequence is identical to that of the monocyte chemoattractant MCP-1 (also called MCAF and SMC- CF), which belongs to a recently identified family of small secretory proteins with cytokine properties. We purified recombinant human MCP- 1/JE (hMCP-1/JE) produced in COS cells and demonstrated that it is chemotactic for human monocytes with a specific activity similar to natural MCP-1. In addition, pure recombinant hMCP-1/JE stimulates monocytes, inducing an increase in cytosolic free calcium and the respiratory burst, but is completely inactive on human neutrophils. These results help to define functionally a well-known growth factor- inducible gene and a member of a new family of cytokines.

Non-specific effects of 4-chloro-m-cresol may cause calcium flux and respiratory burst in human neutrophils

2005 ◽  
Vol 336 (4) ◽  
pp. 1087-1095 ◽  
Author(s):  
Carl J. Hauser ◽  
Kolenkode B. Kannan ◽  
Edwin A. Deitch ◽  
Kiyoshi Itagaki
Keyword(s):  
Respiratory Burst ◽  
Calcium Flux ◽  
Human Neutrophils ◽  
Specific Effects

scholarly journals Neutrophil-activating properties of the melanoma growth-stimulatory activity.

1990 ◽  
Vol 171 (5) ◽  
pp. 1797-1802 ◽  
Author(s):  
B Moser ◽  
I Clark-Lewis ◽  
R Zwahlen ◽  
M Baggiolini
Keyword(s):  
Respiratory Burst ◽  
Sequence Similarity ◽  
Human Melanoma ◽  
Human Neutrophils ◽  
Free Calcium ◽  
Cytosolic Free Calcium ◽  
Extensive Sequence ◽  
Stimulatory Activity ◽  
Massive Accumulation ◽  
Melanoma Growth

Melanoma growth-stimulatory activity (MGSA), a peptide reported to be mitogenic for Hs294T human melanoma cells, has extensive sequence similarity to the neutrophil-activating peptide NAP-1/IL-8, suggesting functional similarities. To test this hypothesis, MGSA was chemically synthesized and tested for its effects on human neutrophils. It was found to induce chemotaxis, exocytosis of elastase, and changes in cytosolic-free calcium to an extent and at concentrations similar to NAP-1/IL-8. However, MGSA was considerably less potent than NAP-1/IL-8 in inducing the respiratory burst. Intradermal injections in rats of MGSA resulted in a massive accumulation of neutrophils. Our data demonstrate that, apart from its growth-stimulatory activity, MGSA is a potent inflammatory agonist with neutrophil-stimulating properties.

scholarly journals Activation of human neutrophils by monoclonal antibody PMN7C3: cell movement and adhesion can be triggered independently from the respiratory burst

Blood ◽  
1986 ◽  
Vol 67 (5) ◽  
pp. 1388-1394 ◽  
Author(s):  
DA Melnick ◽  
T Meshulam ◽  
A Manto ◽  
HL Malech
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Respiratory Burst ◽  
Cellular Response ◽  
Rapid Change ◽  
Cell Movement ◽  
Human Neutrophils ◽  
Free Calcium ◽  
Transient Rise ◽  
Free Calcium Concentration

Anti-neutrophil monoclonal antibody PMN7C3 (IgG3) recognizes glycoproteins bearing the oligosaccharide lacto-N-fucopentaose III, including the C3bi receptor, LFA-1, and p150,95 on the plasma membrane and a group of granule-associated glycoproteins. We have previously shown that binding of this antibody to polymorphonuclear leukocytes (PMNs) stimulates a transient rise in cytosolic free calcium concentration but does not trigger the neutrophil respiratory burst. We now demonstrate that binding of PMN7C3 (and five other monoclonal antibodies recognizing the same antigen) to human neutrophils activates several other cellular responses. Addition of PMN7C3 to monolayers of neutrophils induces a rapid change in cell shape followed by pseudopod formation and increased migration. With incubation at 37 degrees C, the neutrophils aggregate in clusters (leukoagglutination). Quantitation of cell movement in a multiwell chemotaxis assembly or by migration of PMNs under agarose revealed that PMN7C3 is both chemotactic and chemokinetic. Pretreatment with the antibody inhibits subsequent chemotactic response to other stimuli. Monoclonal antibodies binding to other neutrophil antigens do not mimic these effects. These data suggest that cell movement and adhesion can be triggered independently from the respiratory burst. PMN7C3 may be a useful probe with which to study the events that link receptor-ligand binding to cellular response.

scholarly journals Cloning of cDNA for proteinase 3: a serine protease, antibiotic, and autoantigen from human neutrophils.

1990 ◽  
Vol 172 (6) ◽  
pp. 1709-1715 ◽  
Author(s):  
D Campanelli ◽  
M Melchior ◽  
Y Fu ◽  
M Nakata ◽  
H Shuman ◽  
...  
Keyword(s):  
Amino Acid ◽  
Serine Protease ◽  
Serine Proteases ◽  
Specific Activity ◽  
Catalytic Triad ◽  
Amino Acid Sequences ◽  
Cathepsin G ◽  
Human Neutrophils ◽  
Predicted Amino Acid Sequence ◽  
Proteinase 3

Closely similar but nonidentical NH2-terminal amino acid sequences have been reported for a protein or proteins in human neutrophils whose bioactivities is/are diverse (as a serine protease, antibiotic, and Wegener's granulomatosis autoantigen) but that share(s) several features: localization in the azurophil granules, a molecular mass of approximately 29 kD, reactivity with diisopropylfluorophosphate, and the ability to degrade elastin. We previously purified one such entity, termed p29b. Using a monospecific antibody, we have cloned from human bone marrow a cDNA encoding the complete p29b protein in its mature form, along with pre- and pro-sequences. The predicted amino acid sequence agrees closely with the NH2-terminal sequence obtained previously from purified p29b, as well as with sequences newly obtained from CNBr fragments. The primary structure is highly homologous to elastase, cathepsin G, T cell granzymes, and other serine proteases, and shares both the catalytic triad and substrate binding pocket of elastase. Hybridization of the full-length cDNA with restriction enzyme digests of human genomic DNA revealed only one fragment. This suggests that the closely related species described previously are the same, and can be subsumed by the term used for the first-described activity, proteinase 3. Proteinase 3 is more abundant in neutrophils than elastase and has a similar proteolytic profile and specific activity. Thus, proteinase 3 may share the role previously attributed to neutrophil elastase in tissue damage, and has the potential to function as an antimicrobial agent.

scholarly journals Activation of human neutrophils by monoclonal antibody PMN7C3: cell movement and adhesion can be triggered independently from the respiratory burst

Blood ◽  
1986 ◽  
Vol 67 (5) ◽  
pp. 1388-1394 ◽  
Author(s):  
DA Melnick ◽  
T Meshulam ◽  
A Manto ◽  
HL Malech
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Respiratory Burst ◽  
Cellular Response ◽  
Rapid Change ◽  
Cell Movement ◽  
Human Neutrophils ◽  
Free Calcium ◽  
Transient Rise ◽  
Free Calcium Concentration

Abstract Anti-neutrophil monoclonal antibody PMN7C3 (IgG3) recognizes glycoproteins bearing the oligosaccharide lacto-N-fucopentaose III, including the C3bi receptor, LFA-1, and p150,95 on the plasma membrane and a group of granule-associated glycoproteins. We have previously shown that binding of this antibody to polymorphonuclear leukocytes (PMNs) stimulates a transient rise in cytosolic free calcium concentration but does not trigger the neutrophil respiratory burst. We now demonstrate that binding of PMN7C3 (and five other monoclonal antibodies recognizing the same antigen) to human neutrophils activates several other cellular responses. Addition of PMN7C3 to monolayers of neutrophils induces a rapid change in cell shape followed by pseudopod formation and increased migration. With incubation at 37 degrees C, the neutrophils aggregate in clusters (leukoagglutination). Quantitation of cell movement in a multiwell chemotaxis assembly or by migration of PMNs under agarose revealed that PMN7C3 is both chemotactic and chemokinetic. Pretreatment with the antibody inhibits subsequent chemotactic response to other stimuli. Monoclonal antibodies binding to other neutrophil antigens do not mimic these effects. These data suggest that cell movement and adhesion can be triggered independently from the respiratory burst. PMN7C3 may be a useful probe with which to study the events that link receptor-ligand binding to cellular response.

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