Cloning and complete nucleotide sequence of mouse immunoglobulin γ1 chain gene

Honjo, Tasuku; Obata, Masahiro; Yamawaki-Kataoka, Yuriko; Kataoka, Takao; Kawakami, Toshiaki; Takahashi, Nobutaka; Mano, Yoshitake

doi:10.1016/0092-8674(79)90072-2

Cited by 227 publications

(117 citation statements)

References 33 publications

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“…Crude total cellular RNAs were extracted from CTLL and YAC-1 cells and TEPC 15 tumor and poly(A) RNAs were purified by oligo(dT) cellulose column chromatography as described (18,19). High molecular weight DNA was extracted from Balb/c mouse liver or normal human placenta as described (20).…”

Section: Biological Materialsmentioning

confidence: 99%

“…Restriction enzyme digestion of DNA and transfer of digests to nitrocellulose filters were done as described (20,23). mRNAs were treated with glyoxal and transferred to nitrocellulose filters as described (24).…”

Section: Biological Materialsmentioning

confidence: 99%

“…mRNAs were treated with glyoxal and transferred to nitrocellulose filters as described (24). Pre-hybridization and hybridization were done as described (20) (26,27). Insert fragments of pmIL-2R-1 were subcloned into pUC18 and pUC19 plasmid vectors and plasmid DNAs were denatured with alkali just before annealing to primer.…”

Section: Biological Materialsmentioning

confidence: 99%

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Nucleotide sequence of mouse IL-2 receptor cDNA and its comparison with the human IL-2 receptor sequence

Shimuzu¹,

Kondo²,

Takeda³

et al. 1985

Nucl Acids Res

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We have cloned cDNA encoding the mouse interleukin-2(IL-2) receptor from a murine T cell line, CTLL using human IL-2 receptor cDNA as probe. COS 7 cells transfected with the cDNA expressed the antigen recognized by the monoclonal antibody against the murine IL-2 receptor. The cDNA identified 4 species of mRNA (4.5, 3.5, 2.2 and 1.5 kb) of the mouse IL-2 receptor in CTLL cells. Difference in the length of mRNA seems to be ascribed to the variable length of the 3' untranslated sequence. Total nucleotide sequence ('1400 bp) of this cDNA was determined and compared with the human receptor. The nucleotide and amino acid sequences of the IL-2 receptor are 70% and 60%, respectively, homologous in average between the two species. The comparison has revealed several conserved regions localized to particular exons such as transmembrane and cytoplasmic portions, suggesting that these regions are important for receptor function and its regulation.

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Section: Biological Materialsmentioning

confidence: 99%

Section: Biological Materialsmentioning

confidence: 99%

See 1 more Smart Citation

Nucleotide sequence of mouse IL-2 receptor cDNA and its comparison with the human IL-2 receptor sequence

Shimuzu¹,

Kondo²,

Takeda³

et al. 1985

Nucl Acids Res

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“…The amino acid (21) and nucleic acid (22,23) sequence data on the hinge region also show that these nucleotides code only for a portion of a domain and therefore constitute a minigene. It has been suggested (22,23) that it evolved from a complete domain by a shift of a splice site followed by mutational divergence of the left end of the domain to become a portion of an intervening sequence with preservation of considerable homology in nucleotide sequence with the 5' flanking end of the CH 1 domain.…”

mentioning

confidence: 99%

“…It has been suggested (22,23) that it evolved from a complete domain by a shift of a splice site followed by mutational divergence of the left end of the domain to become a portion of an intervening sequence with preservation of considerable homology in nucleotide sequence with the 5' flanking end of the CH 1 domain.…”

mentioning

confidence: 99%

Evidence indicating independent assortment of framework and complementarity-determining segments of the variable regions of rabbit light chains. Delineation of a possible J minigene.

Kabat¹,

Wu²,

Bilofsky³

1980

The Journal of Experimental Medicine

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The variable (V) 1 regions of immunoglobulin light chains when aligned for maximum homology can be divided into four framework regions (FR) separated by three complementarity-determining (CDR) (hypervariable [1]) regions or segments (2, 3). The latter as predicted (1), together with the corresponding three CDR of the heavy chain (4), form the antibody-combining sites (3-11). Light chains FR1, FR2, FR3, and FR4 comprise residues 1-23, [35][36][37][38][39][40][41][42][43][44][45][46][47][48][49][98][99][100][101][102][103][104][105][106][107] CDR2,[50][51][52][53][54][55][56][89][90][91][92][93][94][95][96][97]. If the FR segments were grouped into sets of identical sequence and the members of each set were traced, it was shown (12) that members of a given FRI set could be associated with different FR2, FR3, and FR4 sets. This independent assortment suggested that the FR sets, and by implication the CDR sets, were under different genetic control, and the hypothesis was put forward that the individual FR and CDR sets were controlled by minigenes assembled somatically by recombination at the DNA level (12). A minigene is defined as a segment of DNA coding for a portion of a domain and which shows evidence of segregation as a functional unit independent of the rest of the DNA coding for the V region (13). Because we only assorted FR segments, the findings would be independent of whether one or two residues of a given CDR assorted with any FR segment. Studies by Tonegawa et al. with cloned mouse Vx (14, 15) and V~ (16) genes and by Seidman et al. (17,18) with mouse V, genes showed that in 12-d-old embryo DNA, genes

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Evidence for an early appearance of modern post-switch isotypes in mammalian evolution; cloning of IgE, IgG and IgA from the marsupialMonodelphis domestica

Aveskogh

Hellman

1998

Eur. J. Immunol.

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In birds, reptiles and amphibians the IgY isotype exhibits the functional characteristics of both of IgG and IgE. Hence, the gene for IgY most likely duplicated some time during early mammalian evolution and formed the ancestor of present day IgG and IgE. To address the question of when IgY duplicated and formed two functionally distinct isotypes, and to study when IgG and IgA lost their second constant domains, we have examined the Ig expression in a non-placental mammal, the marsupial Monodelphis domestica (grey short-tailed opossum). Screening of an opossum spleen cDNA library revealed the presence of all three isotypes in marsupials. cDNA clones encoding the entire constant regions of opossum IgE (epsilon chain), IgG (gamma chain) and IgA (alpha chain) were isolated, and their nucleotide sequences were determined. A comparative analysis of the amino acid sequences for IgY, IgA, IgE and IgG from various animal species showed that opossum IgE, IgG and IgA on the phylogenetic tree form branches clearly separated from their eutherian counterparts. However, they still conform to the general structure found in eutherian IgE, IgG and IgA. Our findings indicate that all the major evolutionary changes in the Ig isotype repertoire, and in basic Ig structure that have occurred since the evolutionary separation of mammals from the early reptile lineages, occurred prior to the evolutionary separation of marsupials and placental mammals.

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Cloning and complete nucleotide sequence of mouse immunoglobulin γ1 chain gene

Cited by 227 publications

References 33 publications

Nucleotide sequence of mouse IL-2 receptor cDNA and its comparison with the human IL-2 receptor sequence

Nucleotide sequence of mouse IL-2 receptor cDNA and its comparison with the human IL-2 receptor sequence

Evidence indicating independent assortment of framework and complementarity-determining segments of the variable regions of rabbit light chains. Delineation of a possible J minigene.

Evidence for an early appearance of modern post-switch isotypes in mammalian evolution; cloning of IgE, IgG and IgA from the marsupialMonodelphis domestica

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