Equine demineralized bone matrix, particle size 2 to 4 mm, was implanted SC and IM in 4 foals and 4 adult horses. The implants were removed between 5 and 8 weeks after implantation. Bone formation was induced by SC and IM implantations in all animals. The implantation site had a marked effect on the amount of bone that developed, bone being formed earlier and in greater amounts when the matrix was implanted IM. The amount of bone formed increased with increasing time after matrix implantation at both sites. Demineralized bone matrix implantation also led to formation of small amounts of chondroid tissue; this tissue was more common in IM than SC matrix implants, and increased in amount with increasing time after implantation. Formation of this chondroid tissue did not precede the formation of bone, and there was no evidence that implantation of demineralized bone matrix in horses induced endochondral ossification. Age of the host did not appear to affect the response.

Investigation of the structure of equine articular cartilage link protein (LP) from individuals ranging in age from 1 to 15 years identified 3 distinct isoforms having molecular weights of 46,000, 43,000, and 41,000. The relative amounts of each of the 3 isoforms altered with age. The largest form did not change with age; however, amounts of the Mr 43,000 and 41,000 forms increased with increasing age. The results suggested that an accumulation, in the extracellular matrix of cartilage, of these 2 smaller products may have arisen from proteolytic cleavage. The complete amino acid sequence of the protein core was determined from complementary DNA products prepared by polymerase chain reaction amplification of cartilage LP mRNA. The sequence had 96% similarity with human LP and with that of other species for which the primary structure has been determined. This high degree of sequence conservation and the isoform data indicate that extracellular processing of LP occurs by similar mechanisms in various species. At the transcription level, equine chondrocytes were found to express LP as 2 abundant mRNA of 5.0 and 3.0 kb, and a smaller mRNA of 1.5 kb. Processing of the LP mRNA in horses, thus, appears to be similar to that found in other species investigated, and although multiple transcripts are present, the coding region remains unaltered and only 1 protein product is made.

Of 143 Greyhounds necropsied consecutively, 6 (4%) had chondrocalcinosis of the scapulohumeral joint; lesions were identified in 6 additional dogs. Lesions were seen exclusively in the humeral head, mainly in the plateau region. The lesions in the dogs of the initial group were unilateral, but 2 of the 6 additional dogs had bilateral lesions. Focal mineralization of articular cartilage appeared as a white raised nidus, sometimes surrounded by a translucent halo in the opaque cartilage. Circular, small translucent cartilage foci, with or without beginning mineralization, were adjacent to definitive chondrocalcinosis lesions. Chondrocyte necrosis and matrix degradation were considered to antedate appearance of matrical mineral granules; mineralization of the cartilage was considered a secondary process, but not necessarily an epiphenomenon. Scanning electron microscopy indicated that the chondrocalcinosis lesion was composed of deposits of irregularly fused stone material that, in scanning and transmission electron micrographs, was composed of irregular spheroids, 0.05 to 0.5 micrometer in diameter. The spheroids contained poorly formed needle-like crystals of apatite. Sparse transformation of the mineral phase into hydroxyapatite was considered to be attributable to a biological mechanism that inhibited phase transition. Cartilage degeneration and chondrocalcinosis of the plateau region of the humeral head appear to be unique lesions that develop in young Greyhounds. It is possible that these lesions are the result of the biomechanical stress of training and racing.

Investigation of the structure of equine articular cartilage link protein (LP) from individuals ranging in age from 1 to 15 years identified 3 distinct isoforms having molecular weights of 46,000, 43,000, and 41,000. The relative amounts of each of the 3 isoforms altered with age. The largest form did not change with age; however, amounts of the Mr 43,000 and 41,000 forms increased with increasing age. The results suggested that an accumulation, in the extracellular matrix of cartilage, of these 2 smaller products may have arisen from proteolytic cleavage. The complete amino acid sequence of the protein core was determined from complementary DNA products prepared by polymerase chain reaction amplification of cartilage LP mRNA. The sequence had 96% similarity with human LP and with that of other species for which the primary structure has been determined. This high degree of sequence conservation and the isoform data indicate that extracellular processing of LP occurs by similar mechanisms in various species. At the transcription level, equine chondrocytes were found to express LP as 2 abundant mRNA of 5.0 and 3.0 kb, and a smaller mRNA of 1.5 kb. Processing of the LP mRNA in horses, thus, appears to be similar to that found in other species investigated, and although multiple transcripts are present, the coding region remains unaltered and only 1 protein product is made.