Molecular cloning, mapping to human chromosome 1 q21-q23, and cell binding characteristics of Spα, a new member of the scavenger receptor cysteine-rich (SRCR) family of proteins

Abstract

CD5 and CD6, two type I cell surface antigens predominantly expressed by T cells and a subset of B cells, have been shown to function as accessory molecules capable of modulating T cell activation. Here we report the cloning of a cDNA encoding Spα, a secreted protein that is highly homologous to CD5 and CD6. Spα has the same domain organization as the extracellular region of CD5 and CD6 and is composed of three SRCR (scavenger receptor cysteine rich) domains. Chromosomal mapping by fluorescence in situ hybridization and radiation hybrid panel analysis indicated that the gene encoding Spα is located on the long arm of human chromosome 1 at q21-q23 within contig WCl.17. RNA transcripts encoding Spα were found in human bone marrow, spleen, lymph node, thymus, and fetal liver but not in non-lymphoid tissues. Cell binding studies with an Spα immunoglobulin (Spα-mIg) fusion protein indicated that Spα is capable of binding to peripheral monocytes but not to T or B cells. Spα-mIg was also found to bind to the monocyte precursor cell lines K-562 and weakly to THP-1 but not to U937. Spα-mIg also bound to the B cell line Raji and weakly to the T cell line HUT-78. These findings indicate that Spα, a novel secreted protein produced in lymphoid tissues, may regulate monocyte activation, function, and/or survival.