Identification and characterization of a new splicing variant of vascular endothelial growth factor: VEGF183

Biochim Biophys Acta. 1998 Dec 22;1443(3):400-6. doi: 10.1016/s0167-4781(98)00240-1.

Abstract

We report the discovery of a new splicing variant of vascular endothelial growth factor named VEGF183. It is six amino acids shorter than its closest relative, VEGF189, due to the utilization of a conserved alternate splicing donor site within exon 6a. Highly expressed in heart tissue, VEGF183 is detected in transiently transfected COS cells as 28-32-kDa monomers under reduced condition, and 46-kDa dimers under non-reduced condition - the functional unit for all VEGF isoforms.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alternative Splicing*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blotting, Western
  • COS Cells / cytology
  • COS Cells / metabolism
  • DNA, Complementary / chemistry
  • DNA, Complementary / genetics
  • DNA, Complementary / metabolism
  • Endothelial Growth Factors / analysis
  • Endothelial Growth Factors / genetics*
  • Genetic Variation
  • Humans
  • Lymphokines / analysis
  • Lymphokines / genetics*
  • Molecular Sequence Data
  • Sequence Alignment
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Sequence Homology, Nucleic Acid
  • Tissue Distribution
  • Vascular Endothelial Growth Factor A
  • Vascular Endothelial Growth Factors

Substances

  • DNA, Complementary
  • Endothelial Growth Factors
  • Lymphokines
  • VEGFA protein, human
  • Vascular Endothelial Growth Factor A
  • Vascular Endothelial Growth Factors

Associated data

  • GENBANK/AJ010438