Identification of a human CD36 isoform produced by exon skipping. Conservation of exon organization and pre-mRNA splicing patterns with a CD36 gene family member, CLA-1.

During an examination of different cell types for CD36 mRNA splice variants, a partial cDNA from HEL cells was isolated and characterized. This CD36 cDNA had a 309-base pair deletion following the region encoding the first putative transmembrane domain of CD36. The open reading frame of the deleted CD36 cDNA was retained and was predicted to yield a protein lacking 103 amino acid residues. The presence of this variant was confirmed in RNA pools from placental tissue by a reverse transcriptase-coupled polymerase chain reaction assay. Comparison of the HEL CD36 cDNA with the genomic sequence revealed that the mRNA represented by this variant CD36 cDNA was produced by a pre-mRNA splicing reaction that excluded exons 4 and 5. Transient expression of the variant CD36 cDNA in COS-1 cells showed that CD36 immunoreactive protein was expressed on the cell surface but lacked an antigenic epitope defined by amino acid residues 41-143. This cell surface glycoprotein (M(r) approximately 57,000) was of identical molecular weight as a CD36 isoform observed on the surface of HEL cells. The exclusion of exons during CD36 pre-mRNA processing appears to be conserved within one other CD36 gene family member, CLA-1.