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Department of Pathology, University of Connecticut Health Center, Farmington, Connecticut 06032 and the Department of Experimental Pathology, Scripps Clinic and Research Foundation, La Jolla, California 92307
Abstract
The complement-derived chemotactics factors, C3a, C5a, and C567, as well as the chemotactic factor obtained from culture filtrates of Escherichia coli, induce release of the lysosomal enzymes,
-glucuronidase and lysozyme, from rabbit peritoneal neutrophils. Under the same circumstances, there is little or no release of the cytoplasmic marker, lactic dehydrogenase, indicating that the release is a form of induced secretion.
The release occurs to an appreciable extent only when the neutrophils settle on filters of average pore size of 0.60 µm or greater; however, increasing the pore size of the filters from 0.60 to 5 µm does not increase the amount of lysosomal enzyme secretion. The requirement for an appropriate surface suggests that enzyme release by chemotactic factors is a form of induced secretion on non-phagocytosable surfaces studied previously.
No statistically significant correlation was found between the chemotactic responsiveness of neutrophils from different rabbits and their ability to give lysosomal enzyme release when stimulated by the same chemotactic factor. This suggests, at least, that a critical step or steps in the biochemical sequence or sequences governing chemotaxis and induced secretion of lysosomal enzymes in neutrophils is different or has a different quantitative importance.
Footnotes
1 This is Publication No. 54 from the Department of Pathology, University of Connecticut Health Center, Farmington, Connecticut 06032, and Publication No. 782 from the Department of Experimental Pathology, Scripps Clinic and Research Foundation, La Jolla, California 92307.
2 This work was supported by United States Public Health Service Grant AI-09648 to E. L. B. and United States Public Health Service Grant AI-07007 and 3-K04 Gm-42, 567-0151 to P. M. H.
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