Structure of the human MMP-19 gene

Mueller, Markus; Mauch, Simon; Sedláček, Radislav

doi:10.1016/s0378-1119(00)00236-5

Cited by 31 publications

(30 citation statements)

References 27 publications

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“…According to a previous study, CpG sites 28 and 29 are located at the putative transcription factor binding sites on the promoter region of MMP19 and CpG site 31 is located in MMP19 promoter region that is responsible for the majority of transcriptional activity. 24 CpG sites 30 and 31 show specific hypermethylation in six out of seven NPC cell lines as compared to NP460. This is not obvious in the SUNE1 cell line.…”

Section: Discussionmentioning

confidence: 94%

“…These four CpG sites (28À31) include predicted putative transcription factor binding sites and map within the MMP19 promoter region À129 to þ1, which is responsible for the majority of transcriptional activity. 24 Methylation index of averaged percentage of CpG sites 30 and 31 showed only 5% methylation in NP460, while the methylation index for all NPC cell lines is 45% to 95%, with the exception of SUNE1 (Fig. 2c).…”

Section: Loss Of Heterozygosity (Loh) Analysis Of Npc Biopsies and Cementioning

confidence: 96%

“…23 Bisulfite genomic sequencing (BGS) analysis and 5-aza-2 0 -deoxycytidine treatment A 1.9 kb fragment of 5 0 flanking DNA was identified as the promoter region of MMP19. 24 Although it contains no CpG islands, 31 CpG sites are scattered around the promoter region. BGS primers (5 0 -TTTATTTTAGGGAGATTTAA AGGTAGG-3 0 and 5 0 -CAACCAAAAAATATATTACAATTC ACC-3 0 ) were designed by MethPrimer (www.urogene.org/ methprimer).…”

Section: Microsatellite Typing Assaymentioning

confidence: 99%

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Catalytic activity of matrix metalloproteinase‐19 is essential for tumor suppressor and anti‐angiogenic activities in nasopharyngeal carcinoma

Chan

Lung

et al. 2011

Intl Journal of Cancer

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The association of Matrix metalloproteinase-19 (MMP19) in the development of nasopharyngeal carcinoma (NPC) was identified from differential gene profiling, which showed MMP19 was one of the candidate genes down-regulated in the NPC cell lines. In this study, quantitative RT-PCR and Western blot analysis showed MMP19 was down-regulated in all seven NPC cell lines. By tissue microarray immunohistochemical staining, MMP19 appears down-regulated in 69.7% of primary NPC specimens. Allelic deletion and promoter hypermethylation contribute to MMP19 down-regulation. We also clearly demonstrate that the catalytic activity of MMP19 plays an important role in antitumor and antiangiogenesis activities in comparative studies of the wild-type and the catalytically inactive mutant MMP19. In the in vivo tumorigenicity assay, only the wild-type (WT), but not mutant, MMP19 transfectants suppress tumor formation in nude mice. In the in vitro colony formation assay, WT MMP19 dramatically reduces colony-forming ability of NPC cell lines, when compared to the inactive mutant. In the tube formation assay of human umbilical vein endothelial cells and human microvascular endothelial cells (HMEC-1), secreted WT MMP19, but not mutant MMP19, induces reduction of tube-forming ability in endothelial cells with decreased vascular endothelial growth factor (VEGF) in conditioned media detected by enzyme-linked immunosorbent assay (ELISA). The anti-angiogenic activity of WT MMP19 is correlated with suppression of tumor formation. These results now clearly show that catalytic activity of MMP19 is essential for its tumor suppressive and anti-angiogenic functions in NPC.Nasopharyngeal carcinoma (NPC) is a malignancy arising from the epithelial cells of the nasopharynx. This cancer has a unique racial and geographic distribution with a high incidence in Southern China and Southeast Asia among the Southern Chinese population. 1 The etiology of NPC is believed to be multifactorial including dietary and

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Section: Discussionmentioning

confidence: 94%

Section: Loss Of Heterozygosity (Loh) Analysis Of Npc Biopsies and Cementioning

confidence: 96%

Section: Microsatellite Typing Assaymentioning

confidence: 99%

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Catalytic activity of matrix metalloproteinase‐19 is essential for tumor suppressor and anti‐angiogenic activities in nasopharyngeal carcinoma

Chan

Lung

et al. 2011

Intl Journal of Cancer

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“…Basal levels of MMP-19 mRNA in unstimulated keratinocytes were quite low, as detected around cycle [31][32][33]. Of the various agents tested, only PMA and TNF-␣ significantly stimulated expression of MMP-19 mRNA (Fig.…”

Section: Regulation Of Mmp-19 In Primary Keratinocytesmentioning

confidence: 84%

Matrix metalloproteinase‐19 is expressed by proliferating epithelium but disappears with neoplastic dedifferentiation

Impola

Toriseva

Suomela

et al. 2002

Intl Journal of Cancer

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“…This, together with the observed shift in balance of TIMP mRNA levels toward TIMP-1 in ruptured samples, might therefore result in a greater activity of this metalloproteinase in these samples. MMP-19, originally isolated as an autoantigen from the synovium of a rheumatoid arthritis patient (63), is widely expressed in human tissues under quiescent conditions and is proteolytically active against many components of basement membranes, but is unable to cleave triple helix collagen (64,65). Its substrates include nidogen 1, and this cleavage is thought to be inhibitory to angiogenesis (66).…”

Section: Discussionmentioning

confidence: 99%

Expression profiling of metalloproteinases and tissue inhibitors of metalloproteinases in normal and degenerate human achilles tendon

Jones¹,

Corps²,

Pennington³

et al. 2006

Arthritis & Rheumatism

261

284

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Objective. To profile the messenger RNA (mRNA) expression for the 23 known genes of matrix metalloproteinases (MMPs), 19 genes of ADAMTS, 4 genes of tissue inhibitors of metalloproteinases (TIMPs), and ADAM genes 8, 10, 12, and 17 in normal, painful, and ruptured Achilles tendons.Methods. Tendon samples were obtained from cadavers or from patients undergoing surgical procedures to treat chronic painful tendinopathy or ruptured tendon. Total RNA was extracted and mRNA expression was analyzed by quantitative real-time reverse transcription-polymerase chain reaction, normalized to 18S ribosomal RNA.Results. In comparing expression of all genes, the normal, painful, and ruptured Achilles tendon groups each had a distinct mRNA expression signature. Three mRNA were not detected and 14 showed no significant difference in expression levels between the groups. Statistically significant (P < 0.05) differences in mRNA expression, when adjusted for age, included lower levels of MMPs 3 and 10 and TIMP-3 and higher levels of ADAM-12 and MMP-23 in painful compared with normal tendons, and lower levels of MMPs 3 and 7 and TIMPs 2, 3, and 4 and higher levels of ADAMs 8 and 12, MMPs 1, 9, 19, and 25, and TIMP-1 in ruptured compared with normal tendons.Conclusion. The distinct mRNA profile of each tendon group suggests differences in extracellular proteolytic activity, which would affect the production and remodeling of the tendon extracellular matrix. Some proteolytic activities are implicated in the maintenance of normal tendon, while chronically painful tendons and ruptured tendons are shown to be distinct groups. These data will provide a foundation for further study of the role and activity of many of these enzymes that underlie the pathologic processes in the tendon.

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Structure of the human MMP-19 gene

Cited by 31 publications

References 27 publications

Catalytic activity of matrix metalloproteinase‐19 is essential for tumor suppressor and anti‐angiogenic activities in nasopharyngeal carcinoma

Catalytic activity of matrix metalloproteinase‐19 is essential for tumor suppressor and anti‐angiogenic activities in nasopharyngeal carcinoma

Matrix metalloproteinase‐19 is expressed by proliferating epithelium but disappears with neoplastic dedifferentiation

Expression profiling of metalloproteinases and tissue inhibitors of metalloproteinases in normal and degenerate human achilles tendon

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