| http://purl.uniprot.org/citations/15296947 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15296947 | http://www.w3.org/2000/01/rdf-schema#comment | "Matrilins are putative adaptor proteins of the extracellular matrix (ECM) which can form both collagen-dependent and collagen-independent filamentous networks. While all known matrilins (matrilin-1, -2, -3, and -4) are expressed in cartilage, only matrilin-2 and matrilin-4 are abundant in non-skeletal tissues. To clarify the biological role of matrilin-2, we have developed a matrilin-2-deficient mouse strain. Matrilin-2 null mice show no gross abnormalities during embryonic or adult development, are fertile, and have a normal lifespan. Histological and ultrastructural analyses indicate apparently normal structure of all organs and tissues where matrilin-2 is expressed. Although matrilin-2 co-localizes with matrilin-4 in many tissues, Northern hybridization, semiquantitative RT-PCR, immunohistochemistry and biochemical analysis reveal no significant alteration in the steady-state level of matrilin-4 expression in homozygous mutant mice. Immunostaining of wild-type and mutant skin samples indicate no detectable differences in the expression and deposition of matrilin-2 binding partners including collagen I, laminin-nidogen complexes, fibrillin-2 and fibronectin. In addition, electron microscopy reveals an intact basement membrane at the epidermal-dermal junction and normal organization of the dermal collagen fibrils in mutant skin. These data suggest that either matrilin-2 and matrilin-2-mediated matrix-matrix interactions are dispensable for proper ECM assembly and function, or that they are efficiently compensated by other matrix components including wild-type levels of matrilin-4."xsd:string |
| http://purl.uniprot.org/citations/15296947 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.matbio.2004.05.003"xsd:string |
| http://purl.uniprot.org/citations/15296947 | http://purl.uniprot.org/core/author | "Aszodi A."xsd:string |
| http://purl.uniprot.org/citations/15296947 | http://purl.uniprot.org/core/author | "Kiss I."xsd:string |
| http://purl.uniprot.org/citations/15296947 | http://purl.uniprot.org/core/author | "Deak F."xsd:string |
| http://purl.uniprot.org/citations/15296947 | http://purl.uniprot.org/core/author | "Morgelin M."xsd:string |
| http://purl.uniprot.org/citations/15296947 | http://purl.uniprot.org/core/author | "Mates L."xsd:string |
| http://purl.uniprot.org/citations/15296947 | http://purl.uniprot.org/core/author | "Nicolae C."xsd:string |
| http://purl.uniprot.org/citations/15296947 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15296947 | http://purl.uniprot.org/core/name | "Matrix Biol"xsd:string |
| http://purl.uniprot.org/citations/15296947 | http://purl.uniprot.org/core/pages | "195-204"xsd:string |
| http://purl.uniprot.org/citations/15296947 | http://purl.uniprot.org/core/title | "Mice lacking the extracellular matrix adaptor protein matrilin-2 develop without obvious abnormalities."xsd:string |
| http://purl.uniprot.org/citations/15296947 | http://purl.uniprot.org/core/volume | "23"xsd:string |
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