Chondroadherin (CHAD)

Chondroadherin (CHAD) was initially described by Larsson et al. (1991) as a 36-kD matrix protein isolated from bovine cartilage. It was shown to mediate chondrocyte-matrix interactions. Analysis of cDNA generated from a bovine chondrocyte mRNA demonstrated that chondroadherin belongs to the family of leucine-rich repeat (LRR) proteins. Of the LRR proteins, chondroadherin is most closely related to the proteoglycans decorin, biglycan, fibromodulin, and lumican, and the matrix protein PRELP.

Each of these molecules is present in the extracellular matrix of cartilage, each possesses 10 adjacent LRR regions flanked by disulfide-bonded domains, and each possesses consensus motifs within the LRR regions for N-linked glycosylation.