title: Matrix metalloproteinases 15 and 19 are stromal regulators of colorectal             cancer development from the early stages.
abstract: Matrix metalloproteinases (MMPs) have been well characterized for their             ability to degrade extracellular matrix proteins and, thus, they have been studied             to elucidate their involvement in both tumor development and progression. In the             present study, attention was focused on MMP-15 and MMP-19, two less known members             of the MMP family. The expression profile of MMP-15 and -19 was assayed in samples             of normal colorectal mucosa, microadenomas and cancer using confocal analysis,             western blotting and quantitative reverse transcription polymerase chain reaction             (qRT-PCR). Both qRT-PCR and western blotting showed that MMP-15 and MMP-19 appeared             to be upregulated during colorectal tumorigenesis, with different expression patterns:             MMP-15 expression level increases from normal mucosa to microadenomas, with a             reduced level in cancer with respect to microadenomas; the semiquantitative immunofluorescence             analysis showed a stromal localization of this protein in the early phases of             neoplastic transformation. Increasing amount of MMP-19 mRNA and protein levels             were observed in the progression of colonic lesions; MMP-19 staining increased             in the normal mucosa-microadenoma-carcinoma sequence. Such different expression             patterns, are probably due to the different roles played in colorectal tumorigenesis             by these two molecules. Conflicting data on the role of these proteins in tumor             progression have been reported, thus, an improved understanding of the biological             roles of MMPs, in particular the lesser known members such as MMP-15 and 19, in             colorectal cancer may lead to a re-evaluation of the use of MMP inhibitors and             suggests the need of integrated translational studies on MMP expression patterns.
authors.affiliation: Department of Biomedical Sciences, Section of Human Morphology,                     University of Modena and Reggio Emilia, I-41125 Modena, Italy.
authors.forename: Paola
authors.initials: P
authors.lastname: Sena
authors.forename: Francesco
authors.initials: F
authors.lastname: Mariani
authors.forename: Laura
authors.initials: L
authors.lastname: Marzona
authors.forename: Marta
authors.initials: M
authors.lastname: Benincasa
authors.forename: Maurizio
authors.initials: M
authors.lastname: Ponz de Leon
authors.forename: Carla
authors.initials: C
authors.lastname: Palumbo
authors.forename: Luca
authors.initials: L
authors.lastname: Roncucci
mesh_terms: D000236:Adenoma / Q000201:enzymology* / Q000473:pathology; D002277:Carcinoma / Q000201:enzymology* / Q000473:pathology; D002471:Cell Transformation, Neoplastic; D015179:Colorectal Neoplasms / Q000201:enzymology* / Q000473:pathology; D004847:Epithelial Cells / Q000201:enzymology; D005109:Extracellular Matrix / Q000201:enzymology; D015971:Gene Expression Regulation, Enzymologic; D015972:Gene Expression Regulation, Neoplastic; D006801:Humans; D053517:Matrix Metalloproteinase 15 / Q000235:genetics / Q000378:metabolism*; D053505:Matrix Metalloproteinases, Secreted / Q000235:genetics / Q000378:metabolism*; D018613:Microscopy, Confocal; D014158:Transcription, Genetic
chemical_list: C507098:MMP15 protein, human; D053517:Matrix Metalloproteinase 15; D053505:Matrix Metalloproteinases, Secreted; C108362:matrix metalloproteinase 19