Cloning of cDNAs encoding human TIMP-3, a novel member of the tissue inhibitor of metalloproteinase family

Silbiger, Scott M.; Jacobsen, V L; Cupples, Rod; Koski, Raymond A.

doi:10.1016/0378-1119(94)90588-6

Cited by 65 publications

(51 citation statements)

References 17 publications

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“…Three members of the family of TIMP have been identified to date: TIMP-1, TIMP-2 and TIMP-3 [3,[7][8][9][10][11]. The level of *Corresponding author.…”

Section: Introductionmentioning

confidence: 99%

Folding and characterization of the amino‐terminal domain of human tissue inhibitor of metalloproteinases‐1 (TIMP‐1) expressed at high yield in E. coli

et al. 1996

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Methods are described for producing an active aminoterminal domain of tissue inhibitor of metalioproteinases-1 (N-TIMP-1) from inactive protein expressed as inclusion bodies in E. coli. Yields exceed 20 mg per litre of bacterial culture. Activity measurements, CD spectroscopy and NMR spectroscopy of the lSN-labeled protein show that it is fully active, homogeneous in conformation and suitable for high-resolution structural analysis. The affinity of N-TIMP-1 for matrix metalloproteinases 1, 2 and 3 is 6-8-fold less than that of the recombinant full-length protein, indicating that deletion of the Cterminal domain reduces the free energy of interaction by < 10%.

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“…Three members of the family of TIMP have been identified to date: TIMP-1, TIMP-2 and TIMP-3 [3,[7][8][9][10][11]. The level of *Corresponding author.…”

Section: Introductionmentioning

confidence: 99%

Folding and characterization of the amino‐terminal domain of human tissue inhibitor of metalloproteinases‐1 (TIMP‐1) expressed at high yield in E. coli

et al. 1996

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“…Exon 1 contains the translation initiation start codon ATG as well as 280 bp of upstream sequence corresponding to the most S'-extending cDNA isolated (Silbiger et al 1994). This suggests that the S'-flanking region of the TIMP3 gene is not interrupted further by intervening sequences.…”

Section: Genomic Organization Of the Human Timp3 Genementioning

confidence: 99%

“…Assuming very similar functions of the highly homologous TIMP3 genes in human and mouse (Silbiger et al 1994;Leco et al 1994), the regulation of TIMP3 expression should be subjected to strong evolutionary constraints for preservation of putative regulatory elements. Therefore, we compared -1200 bp of the S'-flanking region of representation of the G + C content and frequency of CpG dinucleotides across the coding region of exon 1 and 1184 bp of the 5'-flanking region of the human and murine TIMP3 genes.…”

Section: Comparison Of the S'-flanking Regions Of The Human And Mousementioning

confidence: 99%

“…For library screening TIMP3 cDNA probes were obtained by RT-PCR amplification of total human retinal RNA with three primer pairs designed according to published TIMP3 cDNA sequences (Silbiger et al 1994). Primers used were S'TIMP (S'-TTCTCCTCCTCCTCTTGC-3')/1FF (S'-ACGATGTCGGAGTTGCA-3'), 1F (S'-TGGAGCCTGGGG-GACTGG-3')/1R (S'-CTGGGAGAGGGTGAGCTGG-3'), and 2F (S'-CAACTTCGTGGAGAGGTGGG-3')/2R (S'-AGGGTCTGGCGCTCAGGG-3').…”

Section: Nethodsmentioning

confidence: 99%

“…The regulation of the MMPs occurs at many levels and includes the tissue inhibitors of metalloproteinases (TIMPs). To date, three members of the TIMP gene family have been identified: TIMP1 (Docherty et al 1985), TIMP2 (Boone et al 1990), and TIMP3 (Apte et al 1994a;Silbiger et al 1994).…”

mentioning

confidence: 99%

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Genomic organization of the human tissue inhibitor of metalloproteinases-3 (TIMP3)

Stöhr¹,

Roomp

Felbor³

et al. 1995

Genome Res.

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The tissue inhibitors of metalloproteinases (TIMPs) play a crucial role in the physiological turnover of the extracellular matrix {ECM) by tightly regulating matrix metailoproteinase flvIMP) activities. Disturbances in the TIMP/MMP system have been implicated in many disease processes where loss of ECM integrity is a principal feature. More recently, we have shown that mutations in TIMP3 cause the autosomal dominant disorder Sorsby's fundus dystrophy (SFD}. This is a macular degeneration disorder with characteristic ECM irregularities in Bruch's membrane. To further facilitate mutational analysis and to provide a basis for functional studies, we now report the genomic organization of the human TIMP3 gene.

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Temporal and spatial regulation of gene expression mediated by the promoter for the human tissue inhibitor of metalloproteinases-3 (TIMP-3)-encoding gene

Zeng

Rosborough

et al. 1998

Dev. Dyn.

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A complex interplay between enzymes involved in extracellular matrix formation and their inhibitors is thought to control organogenesis during mammalian development. Disturbance of this balance may result in a wide range of diseases, including macular degeneration, arthritis, and tumor metastases. In order to define elements which may be involved in regulating human tissue inhibitor of metalloproteinase 3 (TIMP3) expression, we isolated and sequenced a clone containing 1315 bp of the 5′‐upstream region of the human TIMP‐3‐encoding gene. A 1.2 kb fragment of this clone, which contains multiple motifs which are binding sites for known transcription factors, was used to drive expression of the lacZ reporter gene in multiple lines of transgenic mice. TIMP3 promoter activity, detected through β‐galactosidase histochemical assay, was observed at high levels in selected tissues, the identity of which varied according to developmental stage. TIMP3 promoter activity was detected at embryonic and early postnatal stages in tissues undergoing extensive remodeling, such as developing somites, bones and joints, choroid plexus, webs between the digits, and the spongiotrophoblastic portion of the placenta. In adulthood, TIMP3 promoter activity was restricted to a few tissues which exhibit high metabolic activity or rapid turnover. These include the retinal pigment epithelium (RPE), cells of the kidney cortex, hair follicles, gingiva, ovarian follicles, and testis. The results suggest that TIMP3 expression plays an active role in developmental patterning and in the maintenance of specific differentiated tissues. Dev. Dyn. 1998;211:228‐237. © 1998 Wiley‐Liss, Inc.

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Cloning of cDNAs encoding human TIMP-3, a novel member of the tissue inhibitor of metalloproteinase family

Cited by 65 publications

References 17 publications

Folding and characterization of the amino‐terminal domain of human tissue inhibitor of metalloproteinases‐1 (TIMP‐1) expressed at high yield in E. coli

Folding and characterization of the amino‐terminal domain of human tissue inhibitor of metalloproteinases‐1 (TIMP‐1) expressed at high yield in E. coli

Genomic organization of the human tissue inhibitor of metalloproteinases-3 (TIMP3)

Temporal and spatial regulation of gene expression mediated by the promoter for the human tissue inhibitor of metalloproteinases-3 (TIMP-3)-encoding gene

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