(Q28184996)

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Down-regulation of tissue inhibitor of matrix metalloprotease-1 (TIMP-1) in aged human skin contributes to matrix degradation and impaired cell growth and survival

scientific article (publication date: December 2003)

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Down-regulation of tissue inhibitor of matrix metalloprotease-1 (TIMP-1) in aged human skin contributes to matrix degradation and impaired cell growth and survival (English)

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William Hornebeck

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December 2003

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https://api.elsevier.com/content/article/PII:S0369811403001986?httpAccept=text/xml

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https://api.elsevier.com/content/article/PII:S0369811403001986?httpAccept=text/plain

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Pathology and Biology

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51

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10

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569-73

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UV-light-induced signal cascades and skin aging.

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Molecular mechanisms of skin ageing

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Elastin and Elastic Fibers in Normal and Pathologic Skin

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Matrix metalloproteinases in skin

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Matrix metalloproteinase-1 and skin ageing in smokers

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Matrix metalloproteinases: they're not just for matrix anymore!

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How matrix metalloproteinases regulate cell behavior

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Replicative senescence of human skin fibroblasts correlates with a loss of regulation and overexpression of collagenase activity

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Differential expression of metalloproteinase and tissue inhibitor of metalloproteinase genes in aged human fibroblasts

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Altered transcriptional regulation of human interstitial collagenase in cultured skin fibroblasts from older donors

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Uncoordinate expressions of type I and III collagens, collagenase and tissue inhibitor of matrix metalloproteinase 1 along in vitro proliferative life span of human skin fibroblasts. Regulation by all-trans retinoic acid.

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Primary structure and cDNA cloning of human fibroblast collagenase inhibitor

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Chromosomal assignment of the gene encoding the human tissue inhibitor of metalloproteinases to Xp11.1-p11.4.

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Synergistic transcriptional activation of the tissue inhibitor of metalloproteinases-1 promoter via functional interaction of AP-1 and Ets-1 transcription factors

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Upstream tissue inhibitor of metalloproteinases-1 (TIMP-1) element-1, a novel and essential regulatory DNA motif in the human TIMP-1 gene promoter, directly interacts with a 30-kDa nuclear protein.

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The human tissue inhibitor of metalloproteinases (TIMP)-1 gene contains repressive elements within the promoter and intron 1.

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Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1

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Residue 2 of TIMP-1 is a major determinant of affinity and specificity for matrix metalloproteinases but effects of substitutions do not correlate with those of the corresponding P1' residue of substrate

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Growth-promoting activity of tissue inhibitor of metalloproteinases-1 (TIMP-1) for a wide range of cells. A possible new growth factor in serum

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Tissue inhibitor of metalloproteinases-1 (TIMP-1) binds to the cell surface and translocates to the nucleus of human MCF-7 breast carcinoma cells.

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Alternative splicing and promoter usage generates an intracellular stromelysin 3 isoform directly translated as an active matrix metalloproteinase

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Tissue inhibitor of metalloproteinases (TIMP-1) stimulates the secretion of collagenase from human skin fibroblasts

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