Matrilysin 1 Influences Colon Carcinoma Cell Migration by Cleavage of the Laminin-5 β3 Chain

Rémy, Lionel; Trespeuch, Cécile; Bachy, Sophie; Scoazec, Jean‐Yves; Rousselle, Patricia

doi:10.1158/0008-5472.can-06-1187

Cited by 64 publications

(63 citation statements)

References 33 publications

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“…Migration of resident HSCs is believed to be critical for the progression of liver fibrosis because it accounts for the increased numbers of activated HSCs in areas of injury. 29 Moreover, MMP-7 is able to cleave ECM and basement membrane, 30 and mediate E-cadherin ectodomain shedding in injured lung epithelium, 24 leading to accelerated cell migration. In this study, the wound healing and Boyden chamber assays demonstrated that HSC-T6 cells expressing MMP-7(Asp-137) variant acquired an enhanced migratory capacity as compared with cells expressing MMP-7(Gly-137) (Fig.…”

Section: Discussionmentioning

confidence: 99%

A Novel Nonsynonymous Variant of Matrix Metalloproteinase-7 Confers Risk of Liver Cirrhosis†

Hung

Chang

et al. 2009

Hepatology

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Liver cirrhosis is characterized by progressive accumulation of extracellular matrix following chronic liver injuries. In the extracellular space, the constant turnover of liver matrix is regulated by the matrix metalloproteinase (MMP) class of enzyme. To assess whether genetic variations in MMP would result in diversity of liver cirrhosis, a case-control study of 320 patients with hepatocellular carcinoma, with or without cirrhosis, was conducted. Ten single-nucleotide polymorphism markers from four potential fibrosis-associated genes were selected for genotyping. Among these genes, a nonsynonymous single-nucleotide polymorphism which generates the variation of Gly-137 and Asp-137 in the MMP-7 gene was found to be strongly associated with the development of liver cirrhosis. In contrast to MMP-7(Gly-137) that predominantly secretes out into the cell culture medium, the cirrhosis-associated MMP-7(Asp-137) variant is preferentially localized on the extracellular membranes where it exerts its proteolytic activity on pericellular substrates. Functional analysis demonstrated an increased ability of the MMP-7(Asp-137) variant to associate with the cell surface CD151 molecule. In wound-healing and Boyden chamber assays, cell motility was specifically enhanced with the expression of MMP-7(Asp-137) as compared to the cells expressing MMP-7(Gly-137). These results demonstrate that the MMP-7(Asp-137) variant confers a gain-of-function phenotype for MMP-7. Conclusion: We have identified a novel genetic association of MMP-7(Asp-137) variant with liver cirrhosis in patients with hepatocellular carcinoma. Whether the MMP-7 variant can be a new marker for liver cirrhosis will be further studied.

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Section: Discussionmentioning

confidence: 99%

A Novel Nonsynonymous Variant of Matrix Metalloproteinase-7 Confers Risk of Liver Cirrhosis†

Hung

Chang

et al. 2009

Hepatology

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“…48 Matrix metalloproteases (MMPs 7 and 20) have a central role in cell proliferation, migration, differentiation, angiogenesis, apoptosis and host defences and YAP1 is the critical downstream regulatory target in the Hippo signaling pathway, having a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. 49,50 By contrast, the genes contained in the 13q32.1 HZD have not been yet associated with a role in cancer disease. The HZD located at 8p11.23-p11.22 and found in two MGUS patients is also of particular interest, as it contains only the ADAM3A gene, in which HZD has recently been reported in pediatric high-grade glioma and diffuse intrinsic pontine gliomas.…”

Section: %mentioning

confidence: 98%

SNP-based mapping arrays reveal high genomic complexity in monoclonal gammopathies, from MGUS to myeloma status

et al. 2012

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Genetic events mediating transformation from premalignant monoclonal gammopathies (MG) to multiple myeloma (MM) are unknown. To obtain a comprehensive genomic profile of MG from the early to late stages, we performed high-resolution analysis of purified plasma cells from 20 MGUS, 20 smoldering MM (SMM) and 34 MM by high-density 6.0 SNP array. A progressive increase in the incidence of copy number abnormalities (CNA) from MGUS to SMM and to MM (median 5, 7.5 and 12 per case, respectively) was observed (P ¼ 0.006). Gains on 1q, 3p, 6p, 9p, 11q, 19p, 19q and 21q along with 1p, 16q and 22q deletions were significantly less frequent in MGUS than in MM. Although 11q and 21q gains together with 16q and 22q deletions were apparently exclusive of MM status, we observed that these abnormalities were also present in minor subclones in MGUS. Overall, a total of 65 copy number-neutral LOH (CNN-LOH) were detected. Their frequency was higher in active MM than in the asymptomatic entities (P ¼ 0.047). A strong association between genetic lesions and fragile sites was also detected. In summary, our study shows an increasing genomic complexity from MGUS to MM and identifies new chromosomal regions involved in CNA and CNN-LOH.

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“…During tissue remodeling, the γ2 subunit is further proteolyzed by MMP-2 to an 80 kD species [18]. The β3 laminin chain has also recently been found to be processed by the action of matrix metalloproteinase-7 (MMP-7, matrilysin-1) or membrane type1 (MT1)-MMP in several cell lines [19,20]. The proteolytic cleavage of the subunits of laminin-332 is biologically important and likely alters its interaction not only with cell-surface receptors but also with other ECM molecules [21].…”

Section: Subunits and Assembly Of Matrix Adhesive Complexesmentioning

confidence: 99%

“…MMP-3, MMP-12, MMP-13, MMP-19, and MMP-20 have also been reported to cleave the γ2 laminin subunit, and enhance epithelial cell migration [80,81]. With regard to the laminin β3 chain, MMP-7 (matrilysin) cleaves the laminin β3 chain into a 90-kD subunit at Ala(515)-Ile(516) [19,82]. This 90-kD product has been reported to stimulate the migration of colon carcinoma cells [19].…”

Section: Relation To Cancermentioning

confidence: 99%

“…With regard to the laminin β3 chain, MMP-7 (matrilysin) cleaves the laminin β3 chain into a 90-kD subunit at Ala(515)-Ile(516) [19,82]. This 90-kD product has been reported to stimulate the migration of colon carcinoma cells [19]. Protease cleavage sites within the subunits of laminin-332 are summarized in Table 1 [16][17][18][19]21,77,78,81,82].…”

Section: Relation To Cancermentioning

confidence: 99%

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Laminin-332-Integrin Interaction: A Target For Cancer Therapy?

Tsuruta

Kobayashi²,

Imanishi³

et al. 2008

CMC

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For many years, extracellular matrix (ECM) was considered to function as a tissue support and filler. However, we now know that ECM proteins control many cellular events through their interaction with cell-surface receptors and cytoplasmic signaling pathways. For example, they regulate cell proliferation, cell division, cell adhesion, cell migration, and apoptosis. We focus in this review on a laminin isoform, laminin-332 (formerly termed laminin-5), a major component of the basement membrane (BM) of skin and other epithelial tissues. It is composed of 3 subunits (α3, β3, and γ2) and interacts with at least two integrin receptors expressed by epithelial cells (α3β1 and α6β4 integrin). Mutations in either laminin-332 or integrin α6β4 result in junctional epidermolysis bullosa, a blistering skin disease, while targeting of laminin-332 by autoantibodies in cicatricial pemphigoid leads to dysadhesion of epithelial cells from their underlying connective tissue. Abnormal expression of laminin-332 and its integrin receptors is also a hallmark of certain tumor types and is believed to promote invasion of colon, breast and skin cancer cells. Moreover, there is emerging evidence that laminin-332 and its protease degradation products are not only found at the leading front of several tumors but also likely induce and/or promote tumor cell migration. Thus, in this review, we focus specifically on the role of laminin-332 and its integrin receptors in adhesion, proliferation, and migration/invasion of cancer cells. Finally, we discuss strategies for the development of laminin-332-based antagonists for the treatment of malignant tumors.

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Matrilysin 1 Influences Colon Carcinoma Cell Migration by Cleavage of the Laminin-5 β3 Chain

Cited by 64 publications

References 33 publications

A Novel Nonsynonymous Variant of Matrix Metalloproteinase-7 Confers Risk of Liver Cirrhosis†

A Novel Nonsynonymous Variant of Matrix Metalloproteinase-7 Confers Risk of Liver Cirrhosis†

SNP-based mapping arrays reveal high genomic complexity in monoclonal gammopathies, from MGUS to myeloma status

Laminin-332-Integrin Interaction: A Target For Cancer Therapy?

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