Matrilins

Methods Cell Biol. 2018:143:429-446. doi: 10.1016/bs.mcb.2017.08.018. Epub 2017 Nov 13.

Abstract

Marilins mediate interactions between macromolecular components of the extracellular matrix, e.g., collagens and proteoglycans. They are composed of von Willebrand factor type A and epidermal growth factor-like domains and the subunits oligomerize via coiled-coil domains. Matrilin-1 and -3 are abundant in hyaline cartilage, whereas matrilin-2 and -4 are widespread but less abundant. Mutations in matrilin genes have been linked to chondrodysplasias and osteoarthritis and recently characterization of matrilin-deficient mice revealed novel functions in mechanotransduction, regeneration, or inflammation. Due to their intrinsic adhesiveness and partially also low abundance, the study of matrilins is cumbersome. In this chapter, we describe methods for purification of matrilins from tissue, analysis of matrilins in tissue extracts, recombinant expression, and generation of matrilin-specific antibodies.

Keywords: Adaptor protein; Cartilage; Chondrodysplasia; Coiled coil; EGF domain; Matrilin; Osteoarthritis; VWA domain.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies / immunology
  • Antibodies / isolation & purification
  • Cartilage / chemistry
  • Cell Culture Techniques / instrumentation
  • Cell Culture Techniques / methods*
  • Chromatography, Affinity / instrumentation
  • Chromatography, Affinity / methods*
  • Collagen / metabolism
  • Extracellular Matrix / metabolism*
  • Immunization / methods
  • Matrilin Proteins / analysis
  • Matrilin Proteins / chemistry
  • Matrilin Proteins / isolation & purification*
  • Matrilin Proteins / physiology
  • Mechanotransduction, Cellular
  • Protein Domains / physiology
  • Proteoglycans / metabolism
  • Recombinant Proteins / analysis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Regeneration

Substances

  • Antibodies
  • Matrilin Proteins
  • Proteoglycans
  • Recombinant Proteins
  • Collagen