Abstract
The human transmembrane secretory component (SC) acts as the epithelial poly-Ig receptor (PIGR), mediating the translocation of J-chain-containing polymeric IgA (poly- IgA) and pentameric IgM into exocrine secretions.1 SC thus exerts a key role in antibody-mediated protection of mucosal surfaces.2 Primary SC deficiency has not been convincingly documented3; this might be explained by the crucial functional role of this receptor protein. However, it is also possible that its gene might be under positive selection pressure exerted by tight linkage to some other essential gene(s) whose absence or dysfunction is incompatible with survival of the species. Such linkage was examined in the present study. Moreover, characterization of the SC gene, in addition to its chromosomal localization, was performed to supplement present knowledge about its structural organization as part of the Ig supergene family.4
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Krajci, P., Kvale, D., Brandtzaeg, P. (1995). Cloning, Chromosomal Localization, and Linkage Analysis of the Gene Encoding Human Transmembrane Secretory Component (The Poly-Ig Receptor). In: Mestecky, J., Russell, M.W., Jackson, S., Michalek, S.M., Tlaskalová-Hogenová, H., Šterzl, J. (eds) Advances in Mucosal Immunology. Advances in Experimental Medicine and Biology, vol 371. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1941-6_130
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DOI: https://doi.org/10.1007/978-1-4615-1941-6_130
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