Rat immunoglobulin delta heavy chain gene: nucleotide sequence derived from cloned cDNA

Sire, Joséphine; Auffray, Charles; Jordan, Bertrand

doi:10.1016/0378-1119(82)90206-2

Cited by 15 publications

(19 citation statements)

References 37 publications

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“…A high degree of sequence homology between rat and mouse C genes has been described for CE (38) and C, (37) as well as for the K light chain locus (39), a result that we confirm and extend here. Comparison of the se-quences of rat and mouse Ig heavy chain genes suggests that Ig heavy chain gene protein-encoding sequences and regulatory sequences (enhancer, joining, and splice sites) have diverged more slowly than most intron sequences.…”

supporting

confidence: 89%

“…The C8 gene is not included on our cosmids, but a partial C8 cDNA has been isolated (37), and a unique C,, gene has been described (38 gene is most closely related to Cyi, although it also crosshybridizes to Cy2a. This might imply that there are three closely related Cy genes in the rat: Cy2a and Cy1, as determined by sequence analysis, and Cy2c, as determined by cross-hybridization with the rat C,, probes.…”

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confidence: 99%

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Immunoglobulin heavy chain locus of the rat: striking homology to mouse antibody genes.

Brüggemann¹,

Free²,

Diamond³

et al. 1986

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

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DNA encoding the rat diversity segment (D), joining segment (JH), and constant (C) region mu, gamma 2a, gamma 1, gamma 2b, epsilon and alpha of the Ig heavy chain has been isolated from a cosmid library. Restriction mapping allowed us to identify two gene clusters: D-JH-C mu and C gamma 1-C gamma 2b-C epsilon-C alpha in addition to a single C gamma 2a gene. Analysis of genomic DNA by Southern blotting permitted identification of the C gamma 2c gene and led to the proposal of the following gene order for the rat Ig heavy chain locus: D-JH-C mu-C delta-(C gamma 2c, C gamma 2a)-C gamma 1-C gamma 2b-C epsilon-C alpha. There is striking homology between the rat and mouse Ig heavy chain loci as regards gene order and distance between CH genes. Partial DNA sequencing confirms this homology and shows that exon sequences are more conserved than are intron sequences. One of the most conserved intron regions between rat and mouse is that spanning the Ig heavy chain enhancer (91% homology). However, the relationship between the different C gamma subclasses in rat differs from that in mouse. Comparison of the C gamma CH3 domains shows that the rat C gamma 2b gene is most homologous to mouse C gamma 2a/b, whereas the rat C gamma 1 and C gamma 2a genes, both very similar to each other, are most homologous to the mouse C gamma 1 gene.

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supporting

confidence: 89%

mentioning

confidence: 99%

Immunoglobulin heavy chain locus of the rat: striking homology to mouse antibody genes.

Brüggemann¹,

Free²,

Diamond³

et al. 1986

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

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“…One exonencoded short hinges of IgD have previously been observed in rodents (5)(6)(7)25). However, in the mouse and rat genomic ␦ genes, no remnants of a second hinge exon can be identified.…”

Section: Discussionmentioning

confidence: 97%

The Porcine Ig δ Gene: Unique Chimeric Splicing of the First Constant Region Domain in its Heavy Chain Transcripts

Zhao

Pan‐Hammarström

Kacskovıcs

et al. 2003

The Journal of Immunology

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The pig δ gene is located ∼3.4 kb downstream of the second transmembrane exon of the μ gene and shows a similar genomic structure to its counterpart in cow with three exons encoding the CH1, CH2, and CH3 domains. The porcine genomic δCH1 exon has been replaced by a recent duplication of the μCH1 and its flanking sequences, a genetic event that also led to the formation of a short switch δ region, immediately upstream of the δ gene. The δCH1 exhibits a 98.7% similarity (314 of 318 bp) to the μCH1 at the DNA level, whereas the homologies between the δCH2 and μCH3, and the δCH3 and μCH4 are only 33.3 and 35.8%, respectively. Either of the two CH1 exons (μ and δ) could be observed in the expressed porcine IgD H chain cDNA sequences VDJ-μCH1-H-δCH2-δCH3 or VDJ-δCH1-H-δCH2-δCH3, showing a pattern that has not been observed previously in vertebrates. In addition, transfection of a human B cell line, using artificial constructs resembling the porcine Cμ-Cδ locus, also generated both VDJ-μCH1-δCH1-H1-δCH2 and VDJ -δCH1-H1-δCH2 transcripts. An examination of the pig δ genomic sequence shows a putative, second hinge region-encoding exon. Due to the lack of a normal branchpoint sequence for RNA splicing, this exon is not present in the normal pig δ cDNA. However, the exon could be spliced into most of the expressed transcripts in vitro in cell transfection experiments after introduction of a single T nucleotide to restore the branchpoint sequence upstream of the putative H2 exon.

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“…Little is known about the IgD in most species. Gene sequencing has indicated that the IgD of both the mouse (6) and the rat (14) have a three-domain structure with a deletion of C82 and a shortened hinge region. (16) and to the gag-encoded polypeptide of the simian sarcoma virus (17).…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, although the 8 hinges of the mouse (4) and the rat (14) are homologous to the human GalN-rich segment, the rodents lack the second hinge exon and the corresponding high-charge segment. There is no precedent for such a missing exon in other immunoglobulin isotypes.…”

Section: Discussionmentioning

confidence: 99%

Analysis of the mechanism, rate, and sites of proteolytic cleavage of human immunoglobulin D by high-pressure liquid chromatography.

Ishioka¹,

Takahashi²,

Putnam³

1987

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

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The high susceptibility of human immunoglobulin D to proteolytic degradation affects its biological function, metabolism, and immunoassay. High-pressure liquid chromatography was used to investigate the mechanism and rate of limited proteolytic cleavage of IgD and also to identify, isolate, and quantify the reaction products. Within 1 to 5 min, tryptic digestion of native IgD almost quantitatively yields a labile Fab fragment, a stable Fc fragment, and a highly charged peptide derived from the hinge region. A galactosamine-rich glycopeptide from the hinge region increases inversely as the Fab is largely degraded to a series of peptides within 1 hr. In contrast, the Fc and the high-charge peptide resist proteolysis for more than 24 hr. The initial sites of cleavage of IgD occur in the hinge region at exposed secondary structures predicted to be (-turns. Concomitant with removal of the galactosaminerich glycopeptide at its carboxyl terminus, the Fd fragment is rapidly and rather randomly degraded, but the light chain is somewhat more resistant than the Fd section of the 8 heavy chain. This study of the rapid rate of proteolysis ofIgD explains the rarity with which intact IgD is found in human sera. It also raises questions about immunoassay of IgD, which is usually measured with antisera against Fc. In vivo, proteolytic cleavage initiates the catabolism of circulating IgD and also affects the role and fate of IgD as an antigen receptor on the B-cell membrane.Unlike other immunoglobulins, human IgD has been little studied because its low concentration in normal serum and its great susceptibility to proteolytic degradation make it difficult to purify intact IgD for structural study. Nonetheless, the complete amino acid sequence of a human myeloma IgD protein has been determined in our laboratory (1)(2)(3) MATERIALS AND METHODS Materials. Human IgD was prepared from the plasma of patient WAH as described (7,8). In some experiments a second IgD, designated HUD, was used. The sources of trypsin and other enzymes and reagents (1,3,8) and of equipment, columns, and reagents for HPLC (9, 10) have been reported.Methods. Methods used in our laboratory for the determination of the primary structure of proteins and for their physical and immunochemical characterization (1,3,(7)(8)(9)(10) and the methods for computer analysis of sequence data (11) and for HPLC (9, 10) have been described.Most experiments on limited digestion were done under nondenaturing conditions with the WAH IgD and trypsin at an enzyme-to-substrate weight ratio of 1:100 in 0.1 M Tris HCl or 0.1 M ammonium bicarbonate (pH 8.0) at 37°C. In other experiments the temperatures ranged from 4°to 50°C. Digestion was stopped by addition of soybean trypsin inhibitor. In kinetic experiments the digestion times varied from 3 sec to 24 hr. In experiments with other proteolytic enzymes such as pepsin, plasmin, and kallikrein, conditions such as the pH and time of incubation were changed as seemed appropriate. Each digest was analyzed by NaDod-S04/PAGE (12-30% gr...

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Rat immunoglobulin delta heavy chain gene: nucleotide sequence derived from cloned cDNA

Cited by 15 publications

References 37 publications

Immunoglobulin heavy chain locus of the rat: striking homology to mouse antibody genes.

Immunoglobulin heavy chain locus of the rat: striking homology to mouse antibody genes.

The Porcine Ig δ Gene: Unique Chimeric Splicing of the First Constant Region Domain in its Heavy Chain Transcripts

Analysis of the mechanism, rate, and sites of proteolytic cleavage of human immunoglobulin D by high-pressure liquid chromatography.

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