A novel isoform of human Golgi complex-localized glycoprotein-1 (also known as E-selectin ligand-1, MG-160 and cysteine-rich fibroblast growth factor receptor) targets differential subcellular localization.

The initial step in trafficking of leukocytes through the vascular endothelium is mediated by an adhesive interaction between molecules of the selectin family and their cognate receptors. Previously, a putative murine E-selectin ligand-1 (ESL-1) was identified and found to be identical to Golgi complex-localized glycoprotein-1 (GLG1), also known as MG-160, and to a previously identified basic fibroblast growth factor (bFGF)-binding protein known as cysteine-rich FGF receptor (CFR). We report here a novel variant of the human GLG1 gene product that we call GLG2, cloned from a human monocyte cDNA library. GLG2 encodes a polypeptide identical to GLG1 except with a unique 24-amino-acid extension at the C-terminus of its cytoplasmic domain. Transfection of chimeric constructs into human embryonic kidney epithelial 293 cells revealed that the cytoplasmic domains of GLG1 and GLG2 targeted the expression of each chimeric protein differentially, GLG1 to the cell surface and GLG2 to the Golgi. Genetic analysis suggests that GLG1 and GLG2 are the products of a single gene, the mRNA of which can be processed by alternative splicing to generate two different transcripts encoding either GLG1 or GLG2. Northern blot analysis showed that the relative amounts of the mRNAs for either isoform differ in a cell- and species-specific manner. These data suggest that alternative splicing of the GLG1 gene transcript might regulate the function of its product.