J chain immunoglobulin

Cattaneo, A. and Neuberger, M.S., Polymeric immunoglobulin M is secreted by transfectants of non-lymphoid cells in the absence of immunoglobulin J chain, EMBO ]., 6, 2753-2758, 1987. 

Immunoglobulins (J chain, IgD) J-chain is a 15-kD acidic protein synthesized by B cells and plasma cells that secrete polymeric immunoglobulins. J-chain expression has thus been observed in most H/RSCs in NLPHL, but not in H/RSCs of CHL with dysregulated Ig genes. 

Chaperones. Figure 2 The multiple roles of BiP in the biogenesis of the secretory proteins. BiP, immunoglobulin heavy chain binding protein ER, endoplasmic reticulum ERAD, ER-associated degradation ERj, resident ER protein with J-domain Sec61, core subunit of the protein translocase UPR, unfolded protein response that involves several signal transduction pathways that are activated in order to increase the biosynthetic capacity and decrease the biosynthetic burden of the ER... 

Helms LR, Wetzel R. Specificity of abnormal assembly in immunoglobulin light chain deposition disease and amyloidosis. J Mol Biol 1996 ... 

Blobel, G., and Dobberstein, B. (1975a). Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J. Cell Biol. 67, 835—851. 

Figure 1.13. Schematic representation of an IgA molecule. Each IgA molecule comprises immunoglobulin molecules joined to each other via a J chain. The heavy chains possess three constant regions (Co1 Cce). The secretory chain (SC) is secreted by epithelial cells and binds to the IgA dimer via disulphide bonds (indicated by wriggly lines).

Chillaron J, Haas IG (2000) Dissodation from BiP and retrotranslocation of unassembled immunoglobulin light chains are tightly coupled to proteasome activity. Mol Biol Cell 11 217-226... 

In nature, mammalian antibodies occur in five distinct classes IgG, IgA, IgM, IgD, and IgE. These differ in structure, size, amino acid composition, charge, and carbohydrate components. The basic structure of each of the classes of immunoglobulins consists of two identical polypeptide chains linked by disulfide bonds to two identical heavy chains. Differences between classes and subclasses are determined by the makeup of the respective heavy chains. IgG is the major serum immunoglobulin and occurs as a single molecule IgA also occurs as a single molecule but also polymerizes, primarily as a dimer and also associates with a separate protein when secreted. IgM occurs in the serum as a pentamer, with monomers linked by disulfide bonds and the inclusion of an additional polypeptide component, the J-chain. IgD and IgE occur primarily as membrane-bound monomers on -cells, or basophils and mast cells, respectively. 

Kenten, J.H., Molgaard, H.V., Houghton, M., et al. (1982). Cloning and sequence determination of the gene for the human immunoglobulin e chain expressed in a myeloma cell line. Proc. Natl. Acad. Sci. USA, 79, 6661-6665. 

Kodaira, M., Kinashi, T., Umemura, I., et al. (1986). Organization and evolution of variable region genes of the human immunoglobulin heavy chain. J. Mol. Biol., 190,529-541. 

Matsuda, E, Shin, E.K., Hirabayashi, Y., et al. (1990). Organization of variable region segments of the human immunoglobulin heavy chain, duplication of the D5 cluster within the locus and interchromosomal translocation of variable region segments. EMBO J., 9, 2501-2506. 

Pascual, V., Capra, J.D. (1991). Human immunoglobulin heavy-chain variable region genes, organization, polymorphism, and expression. Adv. Immunol., 49, 1-74. 

Raaphorst, F.M., Timmers, E., Renter, M.J.H., et al. (1992). Restricted utilization of germline VH3 genes and short diverse third complementarity-determining regions (CDR3) in human fetal B-lymphocyte immunoglobulin heavy chain rearrangements. Eur. J. Immunol., 22, 247-251. 

Schroeder, H.W., Wang, J.Y. (1990). Preferential utilization of conserved immunoglobulin heavy chain variable gene segments during human fetal life. Proc. Natl. Acad. Sci. USA, 87, 6146-6150. 

Becker L et al. (2005) Preprotein translocase of the outer mitochondrial membrane reconstituted Tom40 forms a characteristic TOM pore. J Mol Biol 353 1011-1020 Blobel G, Dobberstein (1975a) Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J Cell Biol 67 835-851 Blobel G, Dobberstein (1975b) Transfer to proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components. J Cell Biol 67 852-862... 

Kobayashi, K., Vaerman, J. P., Bazin, H and Lebaq-Verheyden, A. M. 1973. Identification of J-chain in polymeric immunoglobulins from a variety of species by crossreaction with rabbit antisera to human J-chain. J. Immunol 111, 1590-1594. 

Komar, R. and Mukkur, T. K. S. 1974. Isolation and characterization of J-chain from bovine colostral immunoglobulin M. Can, J. Biochem, 53, 943-949. 

Immunoglobulins of classes IgGl, IgG2, IgA, and IgM are measurable in milk. IgG has the familiar immunoglobulin structure, with two heavy and two light chains. IgA is found in milk as a dimer of two IgA complexes, linked by one J and one SC chain. Negative IgM is a pentamer of IgM complexes attached to one J chain (Walstra and Jenness 1984). 

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