2006
DOI: 10.1016/j.gene.2006.02.001
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Identification and expression of novel isoforms of human stromal cell-derived factor 1

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Cited by 194 publications
(199 citation statements)
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“…[15][16][17] Of note, a second receptor, CXCR7/RDC1, has recently been identified in several cell types and although CXCR7 binds SDF-1 with high affinity, typical chemokine signaling has not been demonstrated. 18 SDF-1, which is highly conserved among species, has six identified splice variants (SDF-1a, -b, -g, -d, -e, -u) derived from the same gene 7,8,19 and its N-terminal residues 1-8 are required to form the binding domain for CXCR4. 20,21 The two most abundant splice variants, SDF-1a and SDF-1b, share identical amino acid sequences except for the presence of four additional amino acids at the C-terminus of SDF-1b.…”
Section: Introductionmentioning
confidence: 99%
“…[15][16][17] Of note, a second receptor, CXCR7/RDC1, has recently been identified in several cell types and although CXCR7 binds SDF-1 with high affinity, typical chemokine signaling has not been demonstrated. 18 SDF-1, which is highly conserved among species, has six identified splice variants (SDF-1a, -b, -g, -d, -e, -u) derived from the same gene 7,8,19 and its N-terminal residues 1-8 are required to form the binding domain for CXCR4. 20,21 The two most abundant splice variants, SDF-1a and SDF-1b, share identical amino acid sequences except for the presence of four additional amino acids at the C-terminus of SDF-1b.…”
Section: Introductionmentioning
confidence: 99%
“…[8][9][10] The physiological receptors of CXCL12 are CXCR4 and CXCR7, 8 but only CXCR4 is involved in haematopoiesis. CXCR4 is a G-protein-coupled seven-transmembrane receptor present on the CD34 þ cells.…”
Section: Introductionmentioning
confidence: 99%
“…Crystal structure and NMR studies have demonstrated that hSDF-1α binds to CXCR4 in its monomeric form, and the eight amino acids of the N-terminus form an important receptor binding region, whereas the C-terminus of SDF-1 is not involved in receptor binding (7). Yu et al (8) studied NEK293 cells transfected with SDF-1δ, which has an additional 50 amino acids on the C-terminals, and therefore is >50% longer than hSDF-1α. The study showed the presence of secreted protein at ~14 kDa, the correct molecular size to be the intact protein, suggesting that the C-terminals of SDF-1δ were not cleaved.…”
Section: Discussionmentioning
confidence: 99%
“…The Gen Bank accession numbers for these different cDNAs and their associate proteins are SDF-1α, SDF-1β, SDF-1γ, SDF-1δ, SDF-1ε and SDF-1ϕ. hSDF-1α is an 89-amino-acid protein while SDF-1β, SDF-1γ, SDF-1δ, SDF-1ε and SDF-ϕ encode 93, 119, 120, 90 and 100-amino-acid proteins, in all of which the first 89 amino acids are identical to those of SDF-1α (7,8). The full-length cDNA of hSDF-1α, which encodes 89 amino acids including the N-terminal signal peptide, is ~270 bp.…”
Section: Introductionmentioning
confidence: 99%