The effects of heparin cofactor II-derived chemotaxins on neutrophil actin conformation and cyclic AMP levels.
The serine proteinase inhibitor heparin cofactor II (HC) can be cleaved by polymorphonuclear leukocyte (PMN) elastase (LE) to yield potent chemotactic activity for PMN and monocytes. In contrast to the bacterially-derived chemotaxin formyl-Met-Leu-Phe (fMLP), the HC-derived chemotaxin does not stimulate PMN degranulation or oxidative burst activity. We compared the effects of HC-derived chemotaxins to the effects of fMLP on PMN actin conformation and on the cAMP levels. Both the HC chemotaxins and fMLP rapidly induced an increase in F-actin which was similar in magnitude and time-course. However, in contrast to fMLP, HC-derived chemotaxins did not elevate cAMP levels. HC-derived chemotaxins may be useful probes of chemotactic responses, since they do not have the mixed biological activities of fMLP.
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Related Subject Headings
- Scattering, Radiation
- Protein Conformation
- Pancreatic Elastase
- Neutrophils
- N-Formylmethionine Leucyl-Phenylalanine
- Light
- Leukocyte Elastase
- Humans
- Heparin Cofactor II
- Chemotaxis, Leukocyte
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Scattering, Radiation
- Protein Conformation
- Pancreatic Elastase
- Neutrophils
- N-Formylmethionine Leucyl-Phenylalanine
- Light
- Leukocyte Elastase
- Humans
- Heparin Cofactor II
- Chemotaxis, Leukocyte