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(Received for publication, September 23,
1994; and in revised form, November 30, 1994) We showed previously that the alternative splicing of
chondroitin sulfate attachment domains (CS
Volume 270,
Number 8,
Issue of February 24, 1995 pp. 3914-3918
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
and CS
) yielded
multiforms of the PG-M core protein in mouse. A transcript encoding a
new short form of the core protein PG-M(V3) was found in various mouse
tissues using polymerase chain reaction. DNA sequences of the
polymerase chain reaction products suggested that PG-M(V3) had no
chondroitin sulfate attachment domain. PG-M(V3) was also detected in
various human tissues. The presence of a transcript for PG-M(V3) was
further supported by Northern blot analysis. Southern blot analysis
confirmed that multiforms of the PG-M core protein, including PG-M(V3),
were derived from a single genomic locus by an alternative splicing
mechanism. Because PG-M(V3) has no chondroitin sulfate attachment
region, which is the most distinctive portion of a proteoglycan
molecule, this form may have a unique function.
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