We have identified and initially characterized a novel collagen, type XXII, a member of the FACIT collagen family. Collagen XXII was produced as a recombinant protein, antibodies were prepared and the expression was investigated in murine, human and zebra fish cells and tissues. A striking hallmark of this new protein is its uniquely restricted expression at tissue junctions. It is found in the basement membrane zone of myotendinous junctions and the hair follicle-dermis junction in the skin, but also in the extrafibrillar matrix at the surface of articular cartilage, in the zonula fibers of the eye and the chordae tendinae in the heart. Interestingly, in the skin, the expression is hair cycle- dependent. To elucidate the functions of collagen XXII, generation of knockout mice was initiated and morpholino oligonucleotides were used to generate pathological phenotypes in zebra fish embryos. Here we propose further functional characterization of collagen XXII and elucidation of its involvement in pathological processes. The restricted tissue expression in several organs predicts a role for collagen XXII in inherited or acquired human syndromes involving a number of tissues.
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