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METALLOPROTEASE AND SERINE-PROTEASE ARE INVOLVED IN CLEAVAGE OF CD43, CD44, AND CD16 FROM STIMULATED HUMAN GRANULOCYTES - INDUCTION OF CLEAVAGE OF L-SELECTIN VIA CD16
Author(s): BAZIL V, STROMINGER JL
Source: JOURNAL OF IMMUNOLOGY    Volume: 152    Issue: 3    Pages: 1314-1322    Published: FEB 1 1994  
Times Cited: 108     References: 47     
Abstract: CD43, CD44, CD16, and L-selectin have been previously shown to be enzymatically cleaved from stimulated leukocytes. However, little is known about the enzymes involved in these processes. Here, metalloprotease(s) inhibitable by 1,10-phenanthroline together with serine protease(s) inhibitable by Nalpha-p-tosyl-L-lysine chloromethyl ketone and 3,4-dichloroisocoumarin are shown to be involved in the cleavage of CD43, CD44, and CD16 but not in the cleavage of L-selectin on granulocytes. in addition, mAbs that recognize these individual receptors and induce their specific cleavage did not initiate cleavage of the others. In one case only, L-selectin, cleavage was also triggered by mAbs interacting with CD16 (the low affinity FcgammaR). Thus, this mechanism represents a novel pathway of L-selectin cleavage induction.
Document Type: Article
Language: English
Addresses:
1. HARVARD UNIV, SCH MED, DANA FARBER CANC INST, DEPT BIOCHEM & MOLEC BIOL, BOSTON, MA 02115 USA
2. CZECHOSLOVAK ACAD SCI, INST MOLEC GENET, PRAGUE 4, CZECH REPUBLIC
Publisher: AMER ASSOC IMMUNOLOGISTS, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814
Subject Category: Immunology
IDS Number: MV630
ISSN: 0022-1767
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