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

      Biochimica et Biophysica Acta
      Alternative Splicing, Amino Acid Sequence, Animals, Base Sequence, Blotting, Western, COS Cells, cytology, metabolism, DNA, Complementary, chemistry, genetics, Endothelial Growth Factors, analysis, Genetic Variation, Humans, Lymphokines, 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

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          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.

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