Monoclonal antibodies against two epitopes in the human alpha 1 (IX) collagen chain.

Type IX collagen is a component of cartilage and vitreous humor. Its structure and matrix localization suggest it may serve to mediate interactions between fibrillar collagen, proteoglycan and other matrix components. Consequently, abnormalities in type IX collagen may result in chondrodysplasia. In this paper we describe the preparation and use of two monoclonal antibodies which recognize peptide sequences within the human cartilage alpha 1 (IX) collagen chain. Antibody 23-5D1 is highly sensitive and highly specific. It permits the immunoblot detection of type IX collagen extracted from milligram amounts of normal and chondrodysplastic cartilage; it also identifies the "short" form of the alpha 1 (IX) chain in human vitreous humor. Antibody 37-10H7 is highly specific, but of low sensitivity. It was used to make the new observation that an N-linked oligosaccharide is present in the amino-terminal globular domain of the alpha 1 (IX) chain. We anticipate that these antibodies may be valuable tools in the study of human and other mammalian chondrodysplasias.