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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A DNA probe specific for the HLA-B locus has been isolated from a broadly cross-reactive HLA class I genomic clone. Locus specificity of the probe appears to be derived primarily from a stretch of approximately 180 nucleotides comprising the last (7th) intron of the original B7 gene. Use of the probe to analyze Southern blots of genomic DNA from unrelated individuals provides the first direct demonstration of intragenic localization of an HLA allele-specific restriction endonuclease site. Availability of this probe should make practicable the study of HLA-B locus restriction fragment length polymorphism as genetic markers of disease susceptibility, and should provide a model for developing probes specific for other HLA class I loci.
Mol Biol Med 1983 Dec
PMID:An HLA-B locus probe clarifies endonuclease polymorphism of major histocompatibility complex class I genes. 609 60

Alpha subunits from DC1 Ia molecules, when compared with DR alpha subunits, are shown to possess distinctive features revealed by differences in microfingerprinting patterns after peptic digestion. Alpha chains from BR4X7 molecules differ from DC1 alpha chains and are more similar to DR alpha chains. Since DC1 and BR4X7 beta chains (which carry the HLA-controlled alloantigenic determinants) associate with different alpha subunits, it is considered unlikely that they are controlled by alleles at the same locus. The proposed model implies the existence of three tightly linked HLA loci controlling the beta subunits of DR, DC and BR molecules respectively.
Mol Immunol 1983 Mar
PMID:Microfingerprinting analysis of human Ia molecules favours a three loci model. 619 Dec 4

Transformation of LMTK- murine fibroblast cells with purified HLA class I heavy chain genes resulted in the expression of serologically detectable HLA-A3 molecules. Surprisingly, such cells also react with a murine monoclonal antibody specific for a serological determinant notably not expressed by murine but by human beta 2-microglobulin. The human HLA molecules expressed by the transformed cells were characterized on two-dimensional gels. The heavy chain was shown to be associated with a murine beta 2-microglobulin molecule, which could be distinguished from human beta 2-microglobulin by its higher isoelectric point. This heterodimer molecule was immunoprecipitated with the mouse anti-human beta 2-microglobulin monoclonal antibody showing that indeed the complex of mouse beta 2-microglobulin and human heavy chain expresses a human beta 2-microglobulin determinant.
Mol Immunol 1984 Feb
PMID:Transformation of LMTK- cells with purified HLA class I genes--IV. A determinant on beta 2-microglobulin is controlled by HLA heavy chain in a mouse-human hybrid complex: a biochemical analysis. 620 Jul 74

A gene encoding the heavy chain of an HLA human histocompatibility antigen was isolated from a library of human DNA by recombination and selection in vivo. After insertion into a bovine papillomavirus (BPV) DNA expression vector, the gene was introduced into cultured mouse cells. Cells transformed with the HLA-BPV plasmids did not appear to contain extrachromosomal viral DNA, whereas BPV recombinants usually replicated as plasmids in transformed cell lines. Large amounts of HLA RNA were produced by the transformed cells, and the rate of synthesis of human heavy chain was several-fold higher than in the JY cell line, a well-characterized human lymphoblastoid cell line which expresses high levels of surface HLA antigen. Substantial amounts of human heavy chain accumulated in the transformed cells, and HLA antigen was present at the cell surface. These observations establish the feasibility of using BPV vectors to study the structure and function of HLA antigens and the expression of cloned HLA genes.
Mol Cell Biol 1984 Feb
PMID:High-level expression of a cloned HLA heavy chain gene introduced into mouse cells on a bovine papillomavirus vector. 632 59

The human cDNA probe pPGK824 , of Singer-Sam et al. [Singer-Sam, J., Simmer , R. L., Keith, D. H., Shively , L., Teplitz , M., Itakura , K., Gartler , S. M. & Riggs, A. D. (1983) Proc. Natl. Acad. Sci. USA 80, 802-806] was used to isolate a genomic clone lambda PGK-1 containing a portion of an autosomal locus for phosphoglycerate kinase (PGK). A unique sequence subclone (pGK-1) of lambda PGK-1 was then used to map this locus to the region p23-q12 of human autosome 6--i.e., to the interval that contains the major human histocompatibility locus (HLA). Since an autosomal gene coding for testis-specific PGK in the mouse has been shown to be closely linked to the H2 locus and to the T/t-complex locus [ Eicher , E. M., Cherry, M. & Flaherty , L. (1978) Mol. Gen. Genet. 158, 225-228], it is suggested that the lambda PGK-1 recombinant clone contains part of the human gene for the testis-specific isozyme of PGK. In addition, the subcloned pGK-1 detects an EcoRI restriction fragment length variant and may therefore prove useful for further genetical analysis of the HLA region and specifically for testing the hypothesis that spina bifida and anencephaly may be the human equivalent of the murine defects due to the T/t-complex locus. Our findings support the generally held hypothesis that a large number of structural loci clustered around the histocompatibility genes have been conserved in a close linkage association throughout a large evolutionary interval.
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PMID:A human autosomal phosphoglycerate kinase locus maps near the HLA cluster. 632 4

Influenza A virus-specific cytotoxic T lymphocytes (CTL) were induced by incubating human peripheral blood mononuclear cells with membranes prepared from influenza A virus-infected cells. The response obtained was equivalent to that given after sensitization in vitro with influenza A virus-infected lymphocytes. It was shown that this response was only obtained when stimulating membrane fragments and responding cells shared HLA-A or -B locus antigens. In order to analyse further the nature of the activating antigen, the membrane fragments were solubilized with detergent and then reconstituted by dialysing it out. This treatment destroyed their ability to stimulate virus-specific CTL although similar treatment of membranes from uninfected cells did not affect their capacity to stimulate a xenogeneic mouse CTL response. Liposomes constructed to contain defined virus and cell surface antigens also failed to stimulate CTL. These findings suggest that secondary induction of influenza virus-specific CTL in vitro requires the presence of the correct HLA antigen and that the virus-membrane association is irreversibly destroyed by detergent treatment.
Mol Biol Med 1983 Sep
PMID:Plasma membranes from influenza virus-infected cells induce in vitro human secondary virus-specific cytotoxic T lymphocyte responses. 633 15

Ionic strength has a strong influence on the binding of human Ia and HLA(A,B,C) molecules by the corresponding antibodies. A control system, BSA-anti-BSA, was influenced only minimally. The effect on the binding of anti-beta 2-microglobulin was very small when isolated chains were used, but more pronounced when using whole HLA(A,B,C) molecules. An inverse relationship exists between degree of inhibition and antibody concentration.
Mol Immunol 1983 Jun
PMID:Influence of ionic strength on the antibody binding of MHC products. 634 15

Site-specific antibodies to HLA class I molecules have been raised in rabbits immunized with a synthetic peptide with the same amino acid sequence as HLA residues 328-338, which corresponds to the highly conserved intracytoplasmic region. Antibodies were detected by radioimmunoassay and were able to recognize isolated HLA heavy chains blotted onto nitrocellulose as well as the biosynthetically labeled HLA-beta 2 microglobulin complexes solubilized by non-ionic detergents. The intracellular localization of the determinants recognized by the antibodies was shown by indirect immunofluorescence labeling and the specificity of the reaction confirmed by its inhibition with the synthetic peptide. No cross-reaction was seen with H-2 antigens on murine cells. These antibodies will be important for further characterization of HLA antigens and detection of their expression in mouse cells transfected with human genes.
Mol Immunol 1984 Jun
PMID:Induction with a synthetic peptide of antibodies to HLA class I C-terminal intracytoplasmic region. 637 15

An algorithm has been developed which identifies alpha-helices involved in the interactions of membrane proteins with lipid bilayers and which distinguishes them from helices in soluble proteins. The membrane-associated helices are then classified with the aid of the hydrophobic moment plot, on which the hydrophobic moment of each helix is plotted as a function of its hydrophobicity. The magnitude of hydrophobic moment measures the amphiphilicity of the helix (and hence its tendency to seek a surface between hydrophobic and hydrophilic phases), and the hydrophobicity measures its affinity for the membrane interior. Segments of membrane proteins in alpha-helices tend to fall in one of three regions of a hydrophobic moment plot: (1) monomeric transmembrane anchors (class I HLA transmembrane sequences) lie in the region of highest hydrophobicity and smallest hydrophobic moment; (2) helices presumed to be paired (such as the transmembrane M segments of surface immunoglobulins) and helices which are bundled together in membranes (such as bacteriorhodopsin) fall in the adjacent region with higher hydrophobic moment and smaller hydrophobicity; and (3) helices from surface-seeking proteins (such as melittin) fall in the region with still higher hydrophobic moment. alpha-Helices from globular proteins mainly fall in a region of lower mean hydrophobicity and hydrophobic moment. Application of these methods to the sequence of diphtheria toxin suggests four transmembrane helices and a surface-seeking helix in fragment B, the moiety known to have transmembrane function.
J Mol Biol 1984 Oct 15
PMID:Analysis of membrane and surface protein sequences with the hydrophobic moment plot. 650 7

A cDNA clone, pHLA-A, containing sequences specific for a human class I HLA antigen heavy chain, was isolated from a bank of clones made from partially purified HLA-ABC heavy chain mRNA from the human lymphoblastoid cell line Bristol 8 (HLA-A1, A2, B8, B16). The clone corresponded to sequence for the -COOH-terminal 117 amino acids of an HLA-ABC alpha-chain. It differed in at least 15 positions from the published HLA-B7 amino acid sequence but in only two residues when compared to the partial HLA-A2 protein sequence, and was identical to the HLA-A3 protein sequence derived from the nucleotide sequence of the gene. It also differed from some published human HLA-ABC sequences by the addition of three extra -COOH-terminal amino acids: cysteine-lysine-valine. The clone may correspond to either the HLA-A1 allele, for which independent sequence information is not available, or to HLA-A2, in which case there are possible explanations for the discrepancies. Comparison of the pHLA-A sequence with genomic HLA sequences suggests variations in splicing at the end of the protein coding region in some HLA-ABC heavy chain genes, and the use of alternative poly(A) addition sites.
Mol Biol Med 1984 Feb
PMID:Isolation and sequencing of a cDNA clone for a human HLA-ABC antigen. 654 41


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