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Gla-rich protein, a new player in tissue calcification?

2012-03Journal article Restricted access
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dc.contributor.authorCancela, Leonor
dc.contributor.authorConceição, N.
dc.contributor.authorLaizé, Vincent
dc.date.accessioned2014-06-12T13:33:52Z
dc.date.available2014-06-12T13:33:52Z
dc.date.issued2012-03
dc.date.updated2014-06-03T09:40:36Z
dc.description.abstractA novel g-carboxyglutamate (Gla)-containing protein, named Gla-rich protein (GRP) after its high content in Gla residues or upper zone of growth plate and cartilage matrix associated protein after its preferential expression by cartilage chondrocyte, was recently identified in sturgeon, mice, and humans through independent studies. GRP is the most densely g-carboxylated protein identified to date and its structure has been remarkably conserved throughout vertebrate evolution but is apparently absent from bird genomes. Several transcript and genomic variants affecting key protein features or regulatory elements were described and 2 paralogs were identified in the teleost fish genome. In the skeleton, most relevant levels of GRP gene expression were observed in cartilaginous tissues and associated with chondrocytes, suggesting a role in chondrogenesis. But GRP expression was also detected in bone cells, indicative of a more widespread role for the protein throughout skeletal formation. Although the molecular function of GRP is yet unknown, the high content of Gla residues and its accumulation at sites of pathological calcification in different human pathologies affecting skin or the vascular system and in breast cancer tumors suggest that GRP may function as a modulator of calcium availability. Because of its association with fibrillar collagens, GRP could also be involved in the organization and/or stabilization of cartilage matrix. Although transgenic mice did not reveal obvious phenotypic alterations in skeletal development or structure, zebrafish morphants lack craniofacial cartilage and exhibit limited calcification, suggesting a role for GRP during skeletal development, but additional functional data are required to understand its function.por
dc.identifier.citationLeonor Cancela, M.; Conceição, N.; Laizé, V.Gla-rich protein, a new player in tissue calcification?, Advances in Nutrition, 3, 2, 174-181, 2012.por
dc.identifier.doihttp://dx.doi.org/10.3945/an.111.001685
dc.identifier.issn2156-5376
dc.identifier.otherAUT: LCA00739
dc.identifier.urihttp://hdl.handle.net/10400.1/4283
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherThe American Society for Nutritionpor
dc.relation.publisherversionadvances.nutrition.orgpor
dc.titleGla-rich protein, a new player in tissue calcification?por
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage181por
oaire.citation.issue2por
oaire.citation.startPage174por
oaire.citation.titleAdvances in Nutritionpor
oaire.citation.volume3por
person.familyNameCancela
person.familyNameLaizé
person.givenNameM. Leonor
person.givenNameVincent
person.identifier.orcid0000-0003-3114-6662
person.identifier.orcid0000-0001-9565-9198
person.identifier.ridB-4463-2008
person.identifier.scopus-author-id6602982778
rcaap.rightsrestrictedAccesspor
rcaap.typearticlepor
relation.isAuthorOfPublicationb9bbfe32-3dfe-4131-ad14-a4394008447f
relation.isAuthorOfPublicationb51cd3d5-7ee4-47d8-9bc4-b3e297aa222f
relation.isAuthorOfPublication.latestForDiscoveryb51cd3d5-7ee4-47d8-9bc4-b3e297aa222f

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