Abstract
Type XIX collagen is a poorly characterized member of the fibril-associated collagens with an interrupted triple helices (FACIT) class of collagen molecules. As a first step toward elucidating its function, we have isolated full size cDNA clones from the mouse alpha1(XIX) collagen gene (Col19a1) and established its pattern of expression in the developing embryo and adult organism. Col19a1 transcripts can be detected as early as 11 days of gestation and in all embryonic tissues, except the liver, of an 18-day postcoitum mouse. In contrast, only a few adult tissues, brain, eye, and testis, seem to accumulate Col19a1 mRNA. Col19a1 transcripts are at least 10 times more abundant in adult than fetal brain and significantly less in adult than fetal muscle and skin. Consistent with the RNA data, polyclonal antibodies for alpha1(XIX) collagen reacted with a 150-kDa protein in the neutral salt extraction of adult mouse brain tissues. We therefore propose that type XIX collagen plays a distinct role from the other FACIT molecules, particularly in the assembly of embryonic matrices and in the maintenance of specific adult tissues.
Highlights
Collagenous networks play a critical role in the morphogenesis of the embryo and in the maintenance of tissue architecture of adult tissues
Type XIX collagen was originally discovered through cDNA cloning of RNA transcripts from the human rhabdomyosarcoma cell line RD (CCL 136) [7]
We isolated overlapping cDNA clones coding for the entire mouse a1(XIX) chain; we examined the pattern of mRNA accumulation in the tissues of both the developing and adult mice; and we identified the a1(XIX) protein in adult brain tissues
Summary
Collagenous networks play a critical role in the morphogenesis of the embryo and in the maintenance of tissue architecture of adult tissues. One of the most interesting and less characterized collagen subgroups is the one of the so-called FACIT1 (fibrilassociated collagens with interrupted triple helices) which includes types IX, XII, XIV, XVI, and XIX collagen. Available evidence suggests that FACIT may play an important role in providing tissue-specific molecular links between collagen. The abbreviations used are: FACIT, fibril-associated collagens with interrupted triple helices; bp, base pairs; kb, kilobases; d.p.c., days postcoitum; RT-PCR, reverse transcription-polymerase chain reaction; COL, collagenous; NC, noncollagenous; MBP, maltose binding protein; PAGE, polyacrylamide gel electrophoresis. Type XIX collagen was originally discovered through cDNA cloning of RNA transcripts from the human rhabdomyosarcoma cell line RD (CCL 136) [7]. Aside from the rhabdomyosarcoma cell line, there is currently no information about the tissue distribution of type XIX collagen and, about its possible function
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