Cloning and expression of the chicken immunoglobulin joining (J)-chain cDNA.

Abstract:

:The J chain is a component of polymeric immunoglobulin (Ig) molecules and may play an important role in their polymerization and the transport of polymeric Ig across epithelial cells. In this study, the primary structure of the chicken J chain was determined by sequencing cDNA clones. The cDNA had an open reading frame of 476 nucleotides encoding a putative protein of 158 amino acid residues including the signal sequence. The 3' untranslated region consisted of 1216 nucleotides and a poly(A) tail. The deduced amino acid sequence of the chicken J chain had a high degree of homology to that of human, cow, rabbit, mouse, frog, and earthworm, with eight conserved Cys residues identical to the mammalian J chains. Northern blot hybridization performed with total RNA from various chicken tissues revealed high levels of J-chain mRNA expression in spleen, intestine, Harderian gland, and bursa of Fabricius, and low levels in the thymus. The J chain was expressed in the bursa as early as day 15 of embryogenesis. These data indicated that the chicken J-chain gene displays a high degree of homology with that of other species, and is expressed at an early stage of development of the chicken immune system.

journal_name

Immunogenetics

journal_title

Immunogenetics

authors

Takahashi T,Iwase T,Tachibana T,Komiyama K,Kobayashi K,Chen CL,Mestecky J,Moro I

doi

10.1007/s002510050016

subject

Has Abstract

pub_date

2000-02-01 00:00:00

pages

85-91

issue

2

eissn

0093-7711

issn

1432-1211

pii

00510085.251

journal_volume

51

pub_type

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