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(Received for publication, April 5, 1996, and in revised form, August 5, 1996)
From The tissue inhibitors of metalloproteinases
(TIMPs) constitute a family of proteins, of which three members have so
far been described. Using the expressed sequence tag sequencing
approach, we have identified a novel TIMP-related cDNA fragment and
subsequently cloned a fourth human TIMP (TIMP-4) from a human heart
cDNA library. The open reading frame encodes a 224-amino acid
precursor including a 29-residue secretion signal. The predicted
structure of the new protein shares 37% sequence identity with TIMP-1
and 51% identity with TIMP-2 and -3. The protein has a predicted
isoelectric point of 7.34. The open reading frame-directed expression
of TIMP-4 protein in MDA-MB-435 human breast cancer cells showed
metalloproteinase inhibitory activity on reverse zymography. By
Northern analysis, only the adult heart showed abundant TIMP-4
transcripts with a 1.4-kilobase predominant transcript band; very low
levels of the transcripts were detected in the kidney, placenta, colon,
and testes, and no transcripts were detected in the liver, brain, lung,
thymus, and spleen. This unique expression pattern suggests that TIMP-4
may function in a tissue-specific fashion in extracellular matrix
homeostasis.
Volume 271, Number 48,
Issue of November 29, 1996
pp. 30375-30380
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
and
Human Genome Sciences, Inc.,
Rockville, Maryland 20850-3338 and § Department of
Pediatrics, Long Island Jewish Medical Center, The Long Island
Campus for the Albert Einstein College of Medicine,
New Hyde Park, New York 11042
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