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PMID: 8425901 Published · ppublish English Journal Article

Adhesion-dependent protein tyrosine phosphorylation in neutrophils treated with tumor necrosis factor.

The Journal of cell biology ·Vol. 120 ·No. 3 ·1993-02-00 ·Pages 777-84

Fuortes M, Jin WW, Nathan C

Abstract

Human neutrophils (PMN) respond to tumor necrosis factor (TNF) by releasing their granules, reorganizing their cytoskeleton, and massively secreting hydrogen peroxide. This response is dependent on adhesion to extracellular matrix proteins and expression of CD11b/CD18 integrins (Nathan, C., S. Srimal, C. Farber, E. Sanchez, L. Kabbash, A. Asch, J. Gailit, and S. D. Wright. 1989. J. Cell Biol. 109:1341-1349). We investigated the role of tyrosine phosphorylation in the response of PMN to TNF. PMN adherent to protein-coated surfaces but not suspended PMN showed tyrosine phosphorylation of several proteins (approximately 150, approximately 115, approximately 75, and approximately 65 kD) in response to TNF. Tyrosine phosphorylation was evident 5 min after addition of TNF and lasted at least 2 h. The tyrosine kinase inhibitors K252a, genistein and ST638 suppressed tyrosine phosphorylation and blocked hydrogen peroxide production in a reversible manner at low concentrations. Tyrosine kinase inhibitors also blocked the spreading of PMN in response to TNF. Dihydrocytochalasin B did not inhibit tyrosine phosphorylation, but in its presence phosphorylation was rapidly reversed. By immunocytochemistry, the majority of tyrosine phosphoproteins were localized to focal adhesions. Thus TNF-induced tyrosine phosphorylation depends on adhesion of PMN to extracellular matrix proteins, and participates in the transduction of the signals that direct the cells to spread on a biological surface and undergo a respiratory burst.

MeSH Terms
Carbazoles/pharmacology Cell Adhesion/drug effects Cinnamates/pharmacology Extracellular Matrix Proteins/metabolism Genistein Humans Hydrogen Peroxide/blood In Vitro Techniques Indole Alkaloids Isoflavones/pharmacology Kinetics Molecular Weight Neutrophils/cytology,drug effects,physiology Phosphoproteins/isolation & purification,metabolism Protein-Tyrosine Kinases/antagonists & inhibitors,blood Recombinant Proteins/pharmacology Sulfides/pharmacology Time Factors Tumor Necrosis Factor-alpha/pharmacology
Chemicals
Carbazoles Cinnamates Extracellular Matrix Proteins Indole Alkaloids Isoflavones Phosphoproteins Recombinant Proteins Sulfides Tumor Necrosis Factor-alpha ST 638 staurosporine aglycone Hydrogen Peroxide Genistein Protein-Tyrosine Kinases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Fuortes M
Beatrice and Samuel A. Seaver Laboratory, Department of Cell Biology/Anatomy, Cornell University Medical College, New York 10021.
Jin W W
Nathan C
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.120.3.777
Published
1993-02-00
Pages
777-84
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2119542
Subset
IM
External Links
PubMed source DOI: 10.1083/jcb.120.3.777 PMC Full Text View journal details
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