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Characterization of defensin precursors in mature human neutrophils
SS Harwig, AS Park and RI Lehrer
Department of Medicine, UCLA-Center for the Health Sciences 90024-1876.
Human defensins HNP-1 and -3 are broad spectrum antimicrobial peptides that
are synthesized by human neutrophils as 94 amino acid (aa) precursors that
require proteolytic removal of 64 amino-terminal residues to produce the
mature defensins. Recent studies have shown that the early proteolytic
processing events include two sequential cleavages, each removing 19
amino-terminal aa residues, that yield 75 aa and 56 aa prodefensins,
respectively. The subsequent processing steps that convert these 56 aa
prodefensins to mature (30 aa) HNP-1 and HNP-3 are not yet known. We
identified four new defensin precursors in mature normal neutrophils. The
most abundant of these were two 39 aa forms that resulted from the
monobasic endoproteolytic cleavage of proHNP-1 and proHNP-3. The presence
of two proline residues in the vicinity of this newly defined scission site
suggested that this cleavage might be "proline-directed." Smaller amounts
of the 34 aa and 32 aa prodefensin forms were also found. It remains to be
established if these 39, 34, and 32 aa prodefensins are obligate
intermediates in the prodefensin processing pathway, or arise from side
reactions. In either event, because these prodefensin intermediates
accounted for only 0.25% of the total defensin content, proteolytic
conversion of 56 aa prodefensins to mature defensins appears to be a highly
efficient process.
Volume 79,
Issue 6,
pp. 1532-1537,
03/15/1992
Copyright © 1992 by The American Society of Hematology
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