Overview of expression of matrix metalloproteinases (MMP-17, MMP-18, and MMP-20) in cultured human cells

Grant, George M.; Giambernardi, Troy A.; Grant, Anne M. S.; Klebe, Robert J.

doi:10.1016/s0945-053x(99)00003-7

Cited by 69 publications

(59 citation statements)

References 9 publications

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“…These differences are most likely correlated with the protease profile of each cell line. 27,28 None of the cell lines tested spontaneously produced fragments of the size of ES that were reactive with an anti-ES antibody (Fig. 5c).…”

Section: Proteolytic Processing Of the L36 Scfv-collagen XVIII Nc1 Esmentioning

confidence: 99%

Enhanced antiangiogenic therapy with antibody‐collagen XVIII NC1 domain fusion proteins engineered to exploit matrix remodeling events

Lobo¹,

Cuesta²,

Sanz³

et al. 2006

Intl Journal of Cancer

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Antiangiogenic therapy is nowadays one of the most active fields in cancer research. The first strategies, aimed at inhibiting tumor vascularization, included upregulation of endogenous inhibitors and blocking of the signals delivered by angiogenic factors. But interaction between endothelial cells and their surrounding extracellular matrix also plays a critical role in the modulation of the angiogenic process. This study introduces a new concept to enhance the efficacy of antibody-based antiangiogenic cancer therapy strategies, taking advantage of a key molecular event occurring in the tumor context: the proteolysis of collagen XVIII, which releases the endogenous angiogenesis inhibitor endostatin. By fusing the collagen XVIII NC1 domain to an antiangiogenic singlechain antibody, a multispecific agent was generated, which was efficiently processed by tumor-associated proteinases to produce monomeric endostatin and fully functional trimeric antibody fragments. It was demonstrated that the combined production in the tumor area of complementary antiangiogenic agents from a single molecular entity secreted by gene-modified cells resulted in enhanced antitumor effects. These results indicate that tailoring recombinant antibodies with extracellular matrix-derived scaffolds is an effective approach to convert tumor progression associated processes into molecular clues for improving antibody-based therapies. ' 2006 Wiley-Liss, Inc.Key words: antibody-based cancer therapy; angiogenesis inhibition; cancer; angiogenesis; antibody engineering; multivalent and multispecific angiogenesis inhibitors It is widely accepted that tumors cannot grow or metastasize to another organ without the recruitment of new blood vessels, and a broad array of antiangiogenic strategies interfering at various levels of the angiogenic pathway has been reported. 1 However, preclinical and clinical studies suggest that the use of single-agent antiangiogenic strategies may be associated with a number of limitations. 2 We recently proposed a novel antiangiogenic approach based on the blocking of cell binding sites present in the extracellular matrix, and demonstrated that L36, a single-chain Fv (scFv) antibody against laminin, a major basement membrane (BM) component, inhibits tumor angiogenesis and growth in vivo. 3 Vascular BM, a sheet-like highly organized extracellular matrix, is an important structural component of blood vessels and has been shown to interact with and modulate endothelial cell (EC) behavior during angiogenesis. 4 The epitope recognized by L36 is located in a highly flexible area in the middle part of the triple coiled-coil domain, which interacts with a2b1 integrin on the EC surface, with the disruption of this interaction being responsible for the effect of L36 on capillary morphogenesis. 5,6 During the inductive phase of tumor angiogenesis, the BM undergoes many degradative and structural changes, which expose cryptic protein modules that act as local angiogenesis inhibitors. The best characterized among these is endostatin (...

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Section: Proteolytic Processing Of the L36 Scfv-collagen XVIII Nc1 Esmentioning

confidence: 99%

Enhanced antiangiogenic therapy with antibody‐collagen XVIII NC1 domain fusion proteins engineered to exploit matrix remodeling events

Lobo¹,

Cuesta²,

Sanz³

et al. 2006

Intl Journal of Cancer

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“…Furthermore, those tumors that develop despite the lack of MMP-9 tend to be more aggressive than usual, suggesting that MMP-9-de®ciency provides pressure for the selection of less di erentiated cancers that are better able to overcome the absence of MMP-9 (unpublished observations). Other MMPs that are highly expressed in malignant disease, such as MMP-19 (Grant et al, 1999), may also in¯uence cancer progression, but remain essentially unexplored. (Because the GenBank sequences submitted as human MMP-18 and 19 are identical but substantially di erent from the Xenopus MMP-18 sequence, they are designated as MMP-19).…”

Section: Other Mmps Can Promote Carcinogenesismentioning

confidence: 99%

The matrix metalloproteinase stromelysin-1 acts as a natural mammary tumor promoter

2000

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Extracellular matrix-degrading matrix metalloproteinases (MMPs) are invariably upregulated in epithelial cancers and are key agonists in angiogenesis, invasion and metastasis. Yet most MMPs are secreted not by the cancer cells themselves, but by stromal cells within and around the tumor mass. Because the stromal environment can in¯uence tumor formation, and because MMPs can alter this environment, MMPs may also contribute to the initial stages of cancer development. Several recent studies in MMP-overexpressing and MMP-de®cient mice support this possibility, but have required carcinogens or pre-existing oncogenic mutations to initiate tumorigenesis. Here we review the spontaneous development of premalignant and malignant lesions in the mammary glands of transgenic mice that express an autoactivating form of MMP-3/stromelysin-1 under the control of the whey acidic protein gene promoter. These changes were absent in nontransgenic littermates and were quenched by co-expression of a human tissue inhibitor of metalloproteinases-1 (TIMP-1) transgene. Thus by altering the cellular microenvironment, stromelysin-1 can act as a natural tumor promoter and enhance cancer susceptibility.

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“…7 Asimismo, muy pocas líneas celulares expresan MMP-20, como el diente en desarrollo y el intestino grueso, pero no se halló expresión en tejidos como el intestino delgado, riñón, hígado, páncreas, cerebro, pulmón, bazo o estómago. 8 Esta MMP fue localizada en algunas condiciones patológicas not been classified in any of the abovementioned groups, including enamelysin (MMP-20) which is responsible for amelogenin degradation. 5 In recent years, it has been shown that the protein component of mature enamel significantly decreases in comparison with immature enamel.…”

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“…Also, very few cell lines express MMP-20, such as tooth development and the large intestine, but its expression has not been found in tissues such as small intestine, kidney, liver, pancreas, brain, lung, spleen, or stomach. 8 This MMP was found in some pathological como en quistes odontogénicos calcificantes, tumores odontogénicos, células del carcinoma de lengua humana. [9][10][11] Por estas razones, es considerada una MMP específica del diente.…”

mentioning

confidence: 99%

El papel de la enamelisina (MMP-20) en el desarrollo dentario. Revisión sistemática

Rivas

Ramos

2015

Rev Fac Odontol Univ Antioq

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Abstract. Introduction: ameloblasts are cells responsible for the production and mineralization of the organic matrix of enamel through several stages: pre-secretory, secretory, transition, and maturation. The organic matrix components are produced in the secretory phase. In the maturation phase, the organic component is removed and the mineralization process starts. This process requires the involvement of matrix metalloproteinase 20 introdUcción Amelogénesis La morfogénesis de los órganos dentarios inicia a la sexta semana de vida intrauterina en seres humanos (aproximadamente a los cuarenta y cinco días), y en el ratón inicia en el estadio E12.5 1 . El primer indicio consiste en la diferenciación de la lámina dental o listón dentario, originado del ectodermo que reviste la cavidad oral. El ectomesénquima induce a las células basales del epitelio oral a proliferar y formar dos nuevas estructuras: la lámina vestibular y la lámina dentaria. La lámina vestibular formará el surco vestibular y la lámina dentaria dará origen a los crecimientos epiteliales correspondientes a los futuros dientes; 20 deciduos y 32 gérmenes de dentición permanente. De acuerdo a su morfología, los gérmenes dentales seguirán una evolución en: estadio de brote macizo (o yema), estadio de casquete, estadio de campana y estadio de folículo dentario, terminal o maduro.Es en el estadio de campana el órgano del esmalte presenta una nueva capa, el estrato intermedio, ubicado entre el retículo estrellado y el epitelio interno. Al finalizar esta etapa de campana, inicia la histogénesis o aposición de los tejidos duros dentarios (dentina y esmalte). Las células que conforman el epitelio interno, también llamadas preameloblastos, se diferencian en ameloblastos jóvenes y serán las encargadas de la producción del esmalte.El esmalte, también conocido con el nombre de sustancia o tejido adamantino, está ubicado en la porción coronal cubriendo la dentina subyacente. Se origina del ór-gano del esmalte, y es el tejido más duro del organismo. Está constituido por los prismas de esmalte, los cuales están altamente mineralizados, ubicados desde la conexión amelodentinal (CAD) a la superficie externa o libre en contacto con la cavidad oral. La matriz inorgánica del esmalte la conforman los cristales de hidroxiapatita y representa un 95%. Estos están constituidos por fosfato de calcio y se encuentran densamente compactados. La matriz orgánica del esmalte es de naturaleza proteica;

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Overview of expression of matrix metalloproteinases (MMP-17, MMP-18, and MMP-20) in cultured human cells

Cited by 69 publications

References 9 publications

Enhanced antiangiogenic therapy with antibody‐collagen XVIII NC1 domain fusion proteins engineered to exploit matrix remodeling events

Enhanced antiangiogenic therapy with antibody‐collagen XVIII NC1 domain fusion proteins engineered to exploit matrix remodeling events

The matrix metalloproteinase stromelysin-1 acts as a natural mammary tumor promoter

El papel de la enamelisina (MMP-20) en el desarrollo dentario. Revisión sistemática

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