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Volume 272, Number 14, Issue of April 4, 1997 pp. 9325-9331
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Alternative Splicing of the Unique "PLUS" Domain of Chicken PG-M/Versican Is Developmentally Regulated

(Received for publication, May 15, 1996, and in revised form, December 26, 1996)

From the Institute for Molecular Science of Medicine, Aichi Medical University, Nagakute, Aichi 480-11, Japan

We investigated the occurrence of alternatively spliced forms (V0, V1, V2, and V3) of PG-M/versican, a large chondroitin sulfate proteoglycan in developing chicken retinas, using the reverse transcription-polymerase chain reaction. We characterized the PLUS domain, which is apparently unique to the chicken molecule and is regulated by alternative splicing. PG-M in chicken retinas consisted of four forms with (V0, V1, V2, and V3) and two forms without (V1 and V3) the PLUS domain (PG-M⁺ and PG-M, respectively). The four forms of PG-M⁺ were found in all samples examined, but the occurrence of the two PG-M forms was regulated developmentally. Genomic analysis has revealed that the PLUS and CS- domains are encoded by a single exon, and this exon has an internal alternative 5-splice donor site, allowing alternative spliced forms that do not include the 3-end of the exon. Sequences corresponding to the chicken PLUS domain (plus) were not found in mouse and human and may have disappeared during evolution. Sequence similarity suggests that the PLUS domain corresponds to the keratan sulfate attachment domain of aggrecan and that it has a distinct function in the chicken eye.

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