Joining J Chain

Jiri Mestecky, Department of Microbiology, University of Alabama at Birmingham, Alabama, USA Itaru Moro, Department of Pathology, Nihon University School of Dentistry, Tokyo, Japan

Copyright © 1998 Elsevier Ltd. All Rights Reserved.

Although J (joining) chain was detected earlier as a polypeptide with high electrophoretic mobility in the light (L)-chain fraction from human colostral IgA, its existence as a third polypeptide typical of polymeric immunoglobulins (Igs), distinct from H and 1. chains, was established in the early seventies. Subsequent studies revealed that J chain, a glycosylated polypeptide with a molecular mass of 15-16 kDa, displays a fast electrophoretic mobility and is linked by disulfide bridges to the Fc fragment of polymeric IgM or IgA of secretory and serum (myeloma) origin. Based on the given criteria (molecular mass, fast electrophoretic mobility, characteristic amino acid composition and sequence, immunochemical cross-reactivity, and sequence of DNA) the presence of J chain has been established, with variable degrees of confidence, in polymeric Ig from many vertebrate species, including mammals (human, monkey, rabbit, mouse, pig, dog, goat, cat, cow, horse, rat, guinea pig and sheep), birds (chicken and pheasant), reptiles (turtle), amphibians (frog and toad) and fishes (catfish, sardine and shark). Recently, mRNA for J chain has been detected in various species of invertebrates, including earthworm, silkworm, spider, shrimp, crab, oyster, clam, sea squirt and sea cucumber.

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