Extracellular Matrix Degradation

Alexander, Caroline M.; Werb, Zena

doi:10.1007/978-1-4615-3770-0_9

Cited by 171 publications

(107 citation statements)

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“…A comprehensive picture of the molecular machinery that can participate in matrix turnover has emerged from in vitro studies of degradative enzymes and their natural inhibitors (Mignatti and Rifkin, 1993;StetlerStevenson et al, 1993;Alexander and Werb, 1991). However, most of the current literature that deals with the roles of proteinases in tumour invasion and metastasis has come from studies of transformed or tumour-derived cell lines in culture.…”

Section: Discussionmentioning

confidence: 99%

“…Over the past two decades, there has been an explosion of information about the molecular processes involved in ECM breakdown (reviewed in Liotta et al, 1991;Mignatti et al, 1986;Mignatti and Rifkin, 1993;Stetler-Stevenson et al, 1993;Alexander and Werb, 1991). The picture of normal ECM remodelling that has emerged is of a highly regulated process involving: (1) multiple secreted proteinases from different families; (2) the controlled local activation of these enzymes; and (3) the actions of specific proteinase inhibitors.…”

mentioning

confidence: 99%

“…The picture of normal ECM remodelling that has emerged is of a highly regulated process involving: (1) multiple secreted proteinases from different families; (2) the controlled local activation of these enzymes; and (3) the actions of specific proteinase inhibitors. The family of zinc-dependent matrix metalloproteinases (MMPs) that includes collagenases, stromelysins and gelatinases (also known as type IV collagenases) has achieved pre-eminence since in vitro work has shown that, in many situations, they are the principal players responsible for the actual attack on ECM components (Alexander and Werb, 1991;Mignatti et al, 1986). In particular, several family members, including the 72 kDa and 92 kDa type IV gelatinases A and B (MMP-2 and MMP-9) can degrade basement membrane components and have been shown to be instrumental in tumour invasion in vitro Mignatti and Rifkin, 1993;Stetler-Stevenson et al, 1993;Collier et al, 1988;Wilhelm et al, 1989;Nakajima et al, 1987;Watanabe et al, 1993;Juarez et al, 1993).…”

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confidence: 99%

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Comparative analysis of the expression patterns of metalloproteinases and their inhibitors in breast neoplasia, sporadic colorectal neoplasia, pulmonary carcinomas and malignant non-Hodgkin's lymphomas in humans

Kossakowska

Huchcroft²,

Urbanski³

et al. 1996

Br J Cancer

119

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Summary Matrix metalloproteinases (MMPs) and their inhibitors (tissue inhibitors of metalloproteinases, TIMPs) play essential roles in the remodelling of the extracellular matrix (ECM). Results of in vivo and in vitro studies suggest that the balance between MMPs and TIMPs is altered in neoplasia, contributing to the invasive and metastatic properties of malignant tumours. In this study we have analysed the expression of five MMP genes and TIMP-1 and TIMP-2 in 37 benign and malignant lesions of human breast using Northern blot analysis. MMP-9 (92 kDa gelatinase) and MMP-l (stromelysin 3) were most consistently expressed by carcinomas. Based on detection of either MMP-9 or MMP-l mRNAs, we were able to distinguish between malignant and benign disease with a predictive accuracy of 90% with 94% sensitivity and 85% specificity. Subsequently, these results were compared with results for carcinomas of colon and lung and malignant nonHodgkin's lymphomas (NHL). Elevated MMP-9 and TIMP-1 expression was observed in all four systems. MMP-l characterised all carcinomas as well as carcinomas in situ but was not detectable in NHL. Our data therefore argue that there are remarkably similar patterns of specific functions involved in ECM remodelling that correlate with malignancy in different human tumours of different histogenesis. However, MMP-l expression is a characteristic of tumours of epithelial origin that is not found in lymphoid neoplasia. Thus it suggests that MMP-l may play a regulatory role in the invasion and metastasis of carcinomas.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Comparative analysis of the expression patterns of metalloproteinases and their inhibitors in breast neoplasia, sporadic colorectal neoplasia, pulmonary carcinomas and malignant non-Hodgkin's lymphomas in humans

Kossakowska

Huchcroft²,

Urbanski³

et al. 1996

Br J Cancer

119

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“…MMPs are Zn 2+ -dependent proteinases that are extracellular or bound to plasma membrane [36][37][38][39][40]. They can cleave specific proteinaceous components of the extracelluar matrix (ECM) and non-ECM proteins.…”

Section: Early Th Response Genesmentioning

confidence: 99%

Thyroid hormone regulation of apoptotic tissue remodeling during anuran metamorphosis

Shi

Hsia

et al. 2001

Cell Res

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Anuran metamorphosis involves systematic transformations of individual organs in a thyroid hormone (TH)-dependent manner. Morphological and cellular studies have shown that the removal of larval organs/ tissues such the tail and the tadpole intestinal epithelium is through programmed cell death or apoptosis. Recent molecular investigations suggest that TH regulates metamorphosis by regulating target gene expression through thyroid hormone receptors (TRs), which are DNA-binding transcription factors. Cloning and characterization of TH response genes show that diverse groups of early response genes are induced by TH. The products of these TH response genes are believed to directly or indirectly affect the expression and/or functions of cell death genes, which are conserved at both sequence and function levels in different animal species. A major challenge for future research lies at determining the signaling pathways leading to the activation of apoptotic processes and whether different death genes are involved in the regulation of apoptosis in different tissues/organs to effect tissue-specific transformations.

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“…The extracellular protease stromelysin-3 (ST3) is a member of the matrix metalloproteinase (MMP) family, a large family of zinc-dependent, extracellular or membrane-bound proteolytic enzymes [1][2][3][4][5]. MMPs have different but often overlapping substrate specificities [3,6,7].…”

Section: Introductionmentioning

confidence: 99%

The matrix metalloproteinase stromelysin-3 cleaves laminin receptor at two distinct sites between the transmembrane domain and laminin binding sequence within the extracellular domain

Amano

Kwak

et al. 2005

Cell Res

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The matrix metalloproteinase (MMP) stromelysin-3 (ST3) has long been implicated to play an important role in extracellular matrix (ECM) remodeling and cell fate determination during normal and pathological processes. However, like other MMPs, the molecular basis of ST3 function in vivo remains unclear due to the lack of information on its physiological substrates. Furthermore, ST3 has only weak activities toward all tested ECM proteins. Using thyroid hormone-dependent Xenopus laevis metamorphosis as a model, we demonstrated previously that ST3 is important for apoptosis and tissue morphogenesis during intestinal remodeling. Here, we used yeast two-hybrid screen with mRNAs from metamorphosing tadpoles to identify potential substrate of ST3 during development. We thus isolated the 37 kd laminin receptor precursor (LR). We showed that LR binds to ST3 in vitro and can be cleaved by ST3 at two sites, distinct from where other MMPs cleave. Through peptide sequencing, we determined that the two cleavage sites are in the extracellular domain between the transmembrane domain and laminin binding sequence. Furthermore, we demonstrated that these cleavage sites are conserved in human LR. These results together with high levels of human LR and ST3 expression in carcinomas suggest that LR is a likely in vivo substrate of ST3 and that its cleavage by ST3 may alter cell-extracellular matrix interaction, thus, playing a role in mediating the effects of ST3 on cell fate and behavior observed during development and pathogenesis.

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Extracellular Matrix Degradation

Cited by 171 publications

References 130 publications

Comparative analysis of the expression patterns of metalloproteinases and their inhibitors in breast neoplasia, sporadic colorectal neoplasia, pulmonary carcinomas and malignant non-Hodgkin's lymphomas in humans

Comparative analysis of the expression patterns of metalloproteinases and their inhibitors in breast neoplasia, sporadic colorectal neoplasia, pulmonary carcinomas and malignant non-Hodgkin's lymphomas in humans

Thyroid hormone regulation of apoptotic tissue remodeling during anuran metamorphosis

The matrix metalloproteinase stromelysin-3 cleaves laminin receptor at two distinct sites between the transmembrane domain and laminin binding sequence within the extracellular domain

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