Open AccessNormal Skeletal Development of Mice Lacking Matrilin 1: Redundant Function of Matrilins in Cartilage?
Author(s) -
Attila Aszódi,
John F. Bateman,
Emilio Hirsch,
Mária Baranyi,
Ernst B. Hunziker,
Nik Hauser,
Zsuzsa Bösze,
Reinhard Fässler
Publication year - 1999
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.19.11.7841
Subject(s) - cartilage , extracellular matrix , biology , microbiology and biotechnology , cartilage oligomeric matrix protein , mutant , fibril , aggrecan , matrix (chemical analysis) , mutation , gene , genetics , pathology , anatomy , osteoarthritis , chemistry , medicine , articular cartilage , alternative medicine , chromatography
Matrilin 1, or cartilage matrix protein, is a member of a novel family of extracellular matrix proteins. To date, four members of the family have been identified, but their biological role is unknown. Matrilin 1 and matrilin 3 are expressed in cartilage, while matrilin 2 and matrilin 4 are present in many tissues. Here we describe the generation and analysis of mice carrying a null mutation in theCrtm gene encoding matrilin 1. Anatomical and histological studies demonstrated normal development of homozygous mutant mice. Northern blot and biochemical analyses show no compensatory up-regulation of matrilin 2 or 3 in the cartilage of knockout mice. Although matrilin 1 interacts with the collagen II and aggrecan networks of cartilage, suggesting that it may play a role in cartilage tissue organization, studies of collagen extractability indicated that collagen fibril maturation and covalent cross-linking were unaffected by the absence of matrilin 1. Ultrastructural analysis did not reveal any abnormalities of matrix organization. These data suggest that matrilin 1 is not critically required for cartilage structure and function and that matrilin 1 and matrilin 3 may have functionally redundant roles.