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Genome-wide identification of Xenopus matrix metalloproteinases: conservation and unique duplications in amphibians

BACKGROUND: Matrix metalloproteinases (MMPs) are members of the superfamily of Zn(2+ )dependent extracellular or membrane-bound endopeptidases which have been implicated to play critical roles in vertebrate development and human pathogenesis. A number of MMP genes have been found to be upregulated i...

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Autores principales: Fu, Liezhen, Das, Biswajit, Mathew, Smita, Shi, Yun-Bo
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2656525/
https://www.ncbi.nlm.nih.gov/pubmed/19222855
http://dx.doi.org/10.1186/1471-2164-10-81
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author Fu, Liezhen
Das, Biswajit
Mathew, Smita
Shi, Yun-Bo
author_facet Fu, Liezhen
Das, Biswajit
Mathew, Smita
Shi, Yun-Bo
author_sort Fu, Liezhen
collection PubMed
description BACKGROUND: Matrix metalloproteinases (MMPs) are members of the superfamily of Zn(2+ )dependent extracellular or membrane-bound endopeptidases which have been implicated to play critical roles in vertebrate development and human pathogenesis. A number of MMP genes have been found to be upregulated in some or all organs during frog metamorphosis, suggesting that different MMPs may have different functions in various organs/tissues. The recent advances in EST (expressed sequence tag) sequencing and the completion of the genome of Xenopus (X.) tropicalis prompted us to systematically analyze the existence of MMPs in the Xenopus genome. RESULTS: We examined X. laevis and X. tropicalis ESTs and genomic sequences for MMPs and obtained likely homologs for 20 out of the 25 MMPs known in higher vertebrates. Four of the five missing MMPs, i.e. MMPs 8, 10, 12 and 27, were all encoded on human Chromosome 11 and the other missing MMP, MMP22 (a chicken MMP), was also absent in human genome. In addition, we identified several novel MMPs which appears to be derived from unique duplications over evolution, are present in the genomes of both Xenopus species. CONCLUSION: We identified the homologs of most of the mammalian MMPs in Xenopus and discovered a number of novel MMPs. Our results suggest that MMP genes undergo dynamic changes over evolution. It will be of interest in the future to investigate whether MMP expression and functions during vertebrate development are conserved. The sequence information reported here should facilitate such an endeavor in the near future.
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spelling pubmed-26565252009-03-17 Genome-wide identification of Xenopus matrix metalloproteinases: conservation and unique duplications in amphibians Fu, Liezhen Das, Biswajit Mathew, Smita Shi, Yun-Bo BMC Genomics Research Article BACKGROUND: Matrix metalloproteinases (MMPs) are members of the superfamily of Zn(2+ )dependent extracellular or membrane-bound endopeptidases which have been implicated to play critical roles in vertebrate development and human pathogenesis. A number of MMP genes have been found to be upregulated in some or all organs during frog metamorphosis, suggesting that different MMPs may have different functions in various organs/tissues. The recent advances in EST (expressed sequence tag) sequencing and the completion of the genome of Xenopus (X.) tropicalis prompted us to systematically analyze the existence of MMPs in the Xenopus genome. RESULTS: We examined X. laevis and X. tropicalis ESTs and genomic sequences for MMPs and obtained likely homologs for 20 out of the 25 MMPs known in higher vertebrates. Four of the five missing MMPs, i.e. MMPs 8, 10, 12 and 27, were all encoded on human Chromosome 11 and the other missing MMP, MMP22 (a chicken MMP), was also absent in human genome. In addition, we identified several novel MMPs which appears to be derived from unique duplications over evolution, are present in the genomes of both Xenopus species. CONCLUSION: We identified the homologs of most of the mammalian MMPs in Xenopus and discovered a number of novel MMPs. Our results suggest that MMP genes undergo dynamic changes over evolution. It will be of interest in the future to investigate whether MMP expression and functions during vertebrate development are conserved. The sequence information reported here should facilitate such an endeavor in the near future. BioMed Central 2009-02-17 /pmc/articles/PMC2656525/ /pubmed/19222855 http://dx.doi.org/10.1186/1471-2164-10-81 Text en Copyright © 2009 Fu et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Fu, Liezhen
Das, Biswajit
Mathew, Smita
Shi, Yun-Bo
Genome-wide identification of Xenopus matrix metalloproteinases: conservation and unique duplications in amphibians
title Genome-wide identification of Xenopus matrix metalloproteinases: conservation and unique duplications in amphibians
title_full Genome-wide identification of Xenopus matrix metalloproteinases: conservation and unique duplications in amphibians
title_fullStr Genome-wide identification of Xenopus matrix metalloproteinases: conservation and unique duplications in amphibians
title_full_unstemmed Genome-wide identification of Xenopus matrix metalloproteinases: conservation and unique duplications in amphibians
title_short Genome-wide identification of Xenopus matrix metalloproteinases: conservation and unique duplications in amphibians
title_sort genome-wide identification of xenopus matrix metalloproteinases: conservation and unique duplications in amphibians
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2656525/
https://www.ncbi.nlm.nih.gov/pubmed/19222855
http://dx.doi.org/10.1186/1471-2164-10-81
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