Assignment of the gene for beta 2-microglobulin (B2m) to mouse chromosome 2.

Cox, David; Sawicki, Janet A.; Yee, Della; Appella, Ettore; Epstein, Charles J.

doi:10.1073/pnas.79.6.1930

Cited by 22 publications

(5 citation statements)

References 32 publications

(27 reference statements)

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“…The MyK-103 integration site maps within 11.6 centimorgans of the T-cell receptor p-chain locus with 95% confidence (46) and is positioned on the proximal half of mouse chromosome 6 (11). We also used the Bam 1.5 and the Bgl 1.6 probes to screen DNA from a panel of Chinese hamster-mouse somatic cell hybrid clones which segregated mouse chromosomes (16 (18). In transgenic mice, the foreign DNA also integrates as tandem head-to-tail arrays, as deduced by Southern blotting experiments after digestion with enzymes that cut only once within the injected DNA.…”

Section: Resultsmentioning

confidence: 99%

Analysis of the integrant in MyK-103 transgenic mice in which males fail to transmit the integrant.

Wilkie¹,

Palmiter²

1987

Mol. Cell. Biol.

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Males in the transgenic mouse pedigree MyK-103, although fertile, do not transmit the integrant to offspring.The integrant is on chromosome 6 near the T-cell receptor D-chain locus. It contains four fragments of the plasmid pMK (a metallothionein-thymidine kinase fusion gene) and a 532-base-pair fragment of displaced mouse DNA originating from a previously uncharacterized repetitive DNA family. The integration complex is flanked on either side by a 5-kilobase duplication of mouse DNA normally found in a single copy at this locus. Sequence analysis of the six novel junctions and their donor sequences shows that plasmid-plasmid junctions occurred at patches of limited homology, whereas chromosome-plasmid junctions were nonhomologous.

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Section: Resultsmentioning

confidence: 99%

Analysis of the integrant in MyK-103 transgenic mice in which males fail to transmit the integrant.

Wilkie¹,

Palmiter²

1987

Mol. Cell. Biol.

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“…[ 3 ] The human β2M shows 70% amino acid sequence similarity to the murine protein and both of them locate on the syntenic chromosomes. [ 1 4 ] The secondary structure of β2M consists of seven β-strands which are organized into two β-sheets linked by a single disulfide bridge, presenting a classical β-sandwich typical of the immunoglobulin (Ig) domain. [ 5 6 7 ] β2M has no transmembrane region and contains a distinctive molecular structure called a constant-1 Ig superfamily domain, sharing with other adaptive immune molecules including major histocompatibility complex (MHC) class I and class II.…”

Section: Introductionmentioning

confidence: 99%

The Implication and Significance of Beta 2 Microglobulin

Dong²,

Wang

2016

Chinese Medical Journal

123

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Objective:This review focuses on the current knowledge on the implication and significance of beta 2 microglobulin (β2M), a conservative immune molecule in vertebrate.Data Sources:The data used in this review were obtained from PubMed up to October 2015. Terms of β2M, immune response, and infection were used in the search.Study Selections:Articles related to β2M were retrieved and reviewed. Articles focusing on the characteristic and function of β2M were selected. The exclusion criteria of articles were that the studies on β2M-related molecules.Results:β2M is critical for the immune surveillance and modulation in vertebrate animals. The dysregulation of β2M is associated with multiple diseases, including endogenous and infectious diseases. β2M could directly participate in the development of cancer cells, and the level of β2M is deemed as a prognostic marker for several malignancies. It also involves in forming major histocompatibility complex (MHC class I or MHC I) or like heterodimers, covering from antigen presentation to immune homeostasis.Conclusions:Based on the characteristic of β2M, it or its signaling pathway has been targeted as biomedical or therapeutic tools. Moreover, β2M is highly conserved among different species, and overall structures are virtually identical, implying the versatility of β2M on applications.

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“…The comparison of the B2M protein sequences of different species indicated that B2M does not show strong sequence conservation among species. The human B2M protein shares 70% sequential identity with that of mice [ 33 ]. Furthermore, interestingly, no intraspecific genetic polymorphisms have been observed in human B2M [ 34 ], suggesting that changes in the B2M protein sequence could be undesirable to the host.…”

Section: Introductionmentioning

confidence: 99%

β2-microglobulin gene duplication in cetartiodactyla remains intact only in pigs and possibly confers selective advantage to the species

Truong

et al. 2017

PLoS ONE

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Several β2-microglobulin (B2M) -bound protein complexes undertake key roles in various immune system pathways, including the neonatal Fc receptor (FcRn), cluster of differentiation 1 (CD1) protein, non-classical major histocompatibility complex (MHC), and well-known MHC class I molecules. Therefore, the duplication of B2M may lead to an increase in the biological competence of organisms to the environment. Based on the pig genome assembly SSC10.2, a segmental duplication of ~45.5 kb, encoding the entire B2M protein, was identified in pig chromosome 1. Through experimental validation, we confirmed the functional duplication of the B2M gene with a completely identical coding sequence between two copies in pigs. Considering the importance of B2M in the immune system, we performed the phylogenetic analysis of B2M duplication in ten mammalian species, confirming the presence of B2M duplication in cetartioldactyls, like cattle, sheep, goats, pigs and whales, but non-cetartiodactyl species, like mice, cats, dogs, horses, and humans. The density of long interspersed nuclear element (LINE) at the edges of duplicated blocks (39 to 66%) was found to be 2 to 3-fold higher than the average (20.12%) of the pig genome, suggesting its role in the duplication event. The B2M mRNA expression level in pigs was 12.71 and 7.57 times (2-ΔΔCt values) higher than humans and mice, respectively. However, we were unable to experimentally demonstrate the difference in the level of B2M protein because species specific anti-B2M antibodies are not available. We reported, for the first time, the functional duplication of the B2M gene in animals. The identification of partially remaining duplicated B2M sequences in the genomes of only cetartiodactyls indicates that the event was lineage specific. B2M duplication could be beneficial to the immune system of pigs by increasing the availability of MHC class I light chain protein, B2M, to complex with the proteins encoded by the relatively large number of MHC class I heavy chain genes in pigs. Further studies are necessary to address the biological meaning of increased expression of B2M.

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Assignment of the gene for beta 2-microglobulin (B2m) to mouse chromosome 2.

Cited by 22 publications

References 32 publications

Analysis of the integrant in MyK-103 transgenic mice in which males fail to transmit the integrant.

Analysis of the integrant in MyK-103 transgenic mice in which males fail to transmit the integrant.

The Implication and Significance of Beta 2 Microglobulin

β2-microglobulin gene duplication in cetartiodactyla remains intact only in pigs and possibly confers selective advantage to the species

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