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Structure and expression of the cDNA encoding human neutrophil collagenase
P Devarajan, K Mookhtiar, H Van Wart and N Berliner
Department of Internal Medicine, Yale Medical School, New Haven, CT 06510.
We have isolated and characterized a 2.4-kb cDNA clone encoding human
neutrophil collagenase (HNC), a member of the family of matrix
metalloproteinases restricted to secondary granules within neutrophils.
Partial amino acid sequence was used to deduce oligonucleotide probes.
These probes were used to screen a human granulocyte cDNA library derived
from messenger RNA (mRNA) from a patient with chronic granulocytic
leukemia. Cell-free translation of RNA produced from the cDNA produced a
52-Kd protein that was recognized by anti-HNC antibody. The cDNA clone was
sequenced and shown to encode a 467-residue protein whose sequence matched
those regions currently known for HNC. The enzyme exhibits 58% homology to
human fibroblast collagenase and has the same domain structure. It consists
of a 20-residue signal peptide, and an 80-residue propeptide that is lost
on autolytic activation by cleavage of an M-L bond. Other regions
identified include the autolytic degradation site, the "cysteine switch"
residue that is involved in latency and activation, and a putative zinc
binding sequence. HNC has six potential N-linked glycosylation sites. The
cDNA hybridized to a 3.4-kb mRNA in RNA from a patient with chronic
granulocytic leukemia, but not to RNA from uninduced HL60 cells or HL60
cells that had been induced to undergo granulocytic or monocytic maturation
with dimethyl sulfoxide or 12-O-tetradecanoylphorbol 13-acetate,
respectively. These results parallel those seen with lactoferrin and
transcobalamin I, two other secondary granule proteins.
Volume 77,
Issue 12,
pp. 2731-2738,
06/15/1991
Copyright © 1991 by The American Society of Hematology
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