The J Chain of Polymeric Immunoglobulins

Inman, F. P.; Městecký, Jiří

doi:10.1007/978-1-4684-2838-4_5

Cited by 42 publications

(19 citation statements)

References 80 publications

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“…It has been found to play a critical role at two different stages of the immune response, first in the synthesis of the primary antibody product, pentamer IgM, and later in the synthesis of the major secretory antibody, polymeric IgA (1,2). Studies of Ig polymer biosynthesis have shown that the J chain joins two monomer subunits by forming a disulfide bridge between penultimate cysteine residues in the monomer heavy chains (3,4).…”

mentioning

confidence: 99%

Primary structure of the immunoglobulin J chain from the mouse.

Cann¹,

Zaritsky²,

Koshland³

1982

Proc. Natl. Acad. Sci. U.S.A.

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The primary structure of the murine J chain was investigated by sequence analysis ofthe J chain cDNA inserts from two independently cloned chimeric plasmids. The sequence data showed that (i) the two cDNA inserts accounted for all but approximately 100 5' nucleotides of the J chain mRNA and (ii) the J chain mRNA encodes a prepeptide of at least 23 amino acids, a mature protein of 137 residues, and an untranslated 3' region of 707 nucleotides exclusive of the 3' poly(A) tract. The amino acid sequence deduced for the mature mouse J chain was found to be 74% identical with that previously determined for the human J chain. By analyzing the conserved features ofthe sequence, a twodomain structure was generated for the J chain which correlates well with its functions in the polymerization of IgM and IgA. Moreover, by comparing the homologies of the J and heavy chains in mouse and man, evidence was obtained that the structures involved in polymerization are the most conserved elements of immunoglobulin molecules.Considerable progress has been made in defining the functions of the immunoglobulin J chain. It has been found to play a critical role at two different stages of the immune response, first in the synthesis of the primary antibody product, pentamer IgM, and later in the synthesis of the major secretory antibody, polymeric IgA (1, 2). Studies of Ig polymer biosynthesis have shown that the J chain joins two monomer subunits by forming a disulfide bridge between penultimate cysteine residues in the monomer heavy chains (3, 4). In the case of IgM, the J chaincontaining dimer serves as a nucleating unit to promote disulfide bonding of other IgM monomers and to complete the pentamer structure. In the case of IgA, the J chain-containing dimer is usually secreted directly from the cell, but it can induce the formation of larger polymers (5). The J chain has also been found to play a critical role in the transport of polymeric IgA to the exocrine secretions (6). Only J chain-containing polymers appear to be capable of interacting with secretory component (7), the protein that ferries the immunoglobulin across the epithelial cell wall.In contrast, relatively little progress has been made in correlating the functions of J chain with its structure. Such studies have been hampered by the lack ofmutant forms of J chain that display altered function as well as by the difficulty in isolating enough J chain for detailed biochemical characterization. Because the J chain comprises a minor fraction of the polymer protein and is highly susceptible to enzymatic degradation (8), only the human J protein has been obtained in sufficient quantities to permit sequence determination (9). Finally, it has not been possible to study the native conformation ofJ chain as the sreducing conditions required to free the J chain from Ig polymers also reduce the intra-J chain disulfide bonds (10).The recent development of recombinant DNA technology has provided the means to overcome some of these difficulties.In this paper we report the prim...

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confidence: 99%

Primary structure of the immunoglobulin J chain from the mouse.

Cann¹,

Zaritsky²,

Koshland³

1982

Proc. Natl. Acad. Sci. U.S.A.

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“…4). The differences observed in the 3' noncoding sequences of mouse and human mRNA tend to be clustered, high in G+C content, and remote from the highly homologous regions near the A-A-U-A-A and the initial 3 …”

Section: Resultsmentioning

confidence: 96%

“…The solution was mixed for 10 min and centrifuged at 10,000 X g for 15 min at 20°C. The aqueous phase was precipitated with 3 cytoplasmic RNA was subjected to two rounds of oligo(dT)-cellulose chromatography with heating at 700C for 5 min prior to the second round (13). The polyadenylylated RNA was then fractionated by neutral 5-25% sucrose gradient centrifugation (8).…”

Section: And Light (L) Chainsmentioning

confidence: 99%

“…Circulating secreted IgM molecules are usually pentamers of the monomeric form, which are held together by a small J protein (3). Based on their primary structure, u chains isolated from secreted IgM have been subdivided into an NH2-terminal variable (V) region, four constant (C) region domains (C1, C2, C3, and C4), and a COOH-terminal sequence of 19 amino acids ending in tyrosine (4,5).…”

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confidence: 99%

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Cloning and partial nucleotide sequence of human immunoglobulin mu chain cDNA from B cells and mouse-human hybridomas.

Dolby¹,

Devuono²,

Croce³

1980

Proc. Natl. Acad. Sci. U.S.A.

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Purified mRNAs coding for # and K human immunoglobulin polypeptides were translated in vitro and their products were characterized. The p-specific mRNAs, derived from both human lymphoblastoid cells (GM607) and from a mouse-human somatic cell hybrid secreting human p chains (aD5-DH11-BC11), were copied into cDNAs and inserted into the plasmid pBR322. Several recombinant cDNAs that were obtained were identified by a combination of colony hybridization with labeled probes, in vitro translation of plasmidselected p mRNAs, and DNA nucleotide sequence determination. One recombinant DNA, for which the sequence has been partially determined, contains the codons for part of the C3 constant region domain through the carboxy-terminal piece (155 amino acids total) as well as the entire 3' noncoding sequence up to the poly(A) site of the human p mRNA. The sequence A-A-U-A-A occurs 12 nucleotides prior to the poly(A) addition site in the human p mRNA. Considerable sequence homology is observed in the mouse and human p mRNA 3' coding and noncoding sequences.

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“…Moreover, the polyethylene structure of this material would not be degraded by hydrolytic enzymes and it would not bind proteins by nonspecific adsorption [3,4]. However, the use of polyacrylamide beads in affinity chromatography is limited by the lack of simple and less time consuming procedures for activation and derivatization of the polyacrylamide.…”

Section: Introductionmentioning

confidence: 99%