Expression of PG-M(V3), an alternatively spliced form of PG-M without a chondroitin sulfate attachment in region in mouse and human tissues

J Biol Chem. 1995 Feb 24;270(8):3914-8. doi: 10.1074/jbc.270.8.3914.


We showed previously that the alternative splicing of chondroitin sulfate attachment domains (CS alpha and CS beta) 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alternative Splicing*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blotting, Southern
  • Chondroitin Sulfate Proteoglycans / chemistry
  • Chondroitin Sulfate Proteoglycans / genetics*
  • Chondroitin Sulfates / chemistry
  • DNA Primers
  • Humans
  • Mice
  • Molecular Sequence Data


  • Chondroitin Sulfate Proteoglycans
  • DNA Primers
  • Chondroitin Sulfates

Associated data

  • GENBANK/D32039
  • GENBANK/D32040