Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Several haptens coupled to dipalmitoylphosphatidylethanolamine (DPPE) were inserted into the liposome membrane with a base composition of an equimolecular mixture of dimyristoylphosphatidylcholine (DMPC) and cholesterol (Chol). Haptens used were trinitrophenyl (TNP)-DPPE, TNP-aminocaproyl (TNP-Cap)-DPPE, dinitrophenyl (DNP)-DPPE, DNP-aminocaproyl (DNP-Cap)-DPPE, fluoresceinthiocarbamyl (Fl)-DPPE, azobenzenarsonate-tyrosyl (ABA-Tyr)-DPPE, dansyl (DNS)-DPPE, dabsyl (DABS)-DPPE, dithiopyridyl (DTP)-DPPE and maleimidobenzoyl (MB)-DPPE. Reactivity of those haptenized liposomes with complement via the alternative pathway was assessed by release of trapped fluorescent marker from the liposomes following incubation with dilutions of guinea-pig and human sera in a diluent containing MgCl2 and ethyleneglycol-bis(beta-aminoethyl ether)N,N'-tetraacetate (EGTA). In the diluent (Mg-EGTA-GVB), complement activation via the alternative pathway proceeds while that via the classical pathway is inhibited. Fl-liposomes were found to be extremely sensitive to guinea-pig complement, being lysed by guinea pig serum dilutions of up to 1:76 in Mg-EGTA-GVB. Guinea-pig serum could lyse TNP-Cap-liposomes, DNP-Cap-liposomes, TNP-liposomes, DTP-liposomes, MB-liposomes, DNP-liposomes and ABA-Tyr-liposomes, with the reactivity of the liposomes decreasing in this order. However, the only haptenized liposomes sensitive to human serum in Mg-EGTA-GVB were DTP- and MB-liposomes; the other liposomes including Fl-liposomes being unreactive via the alternative pathway in reaction with human complement.
Mol Immunol 1983 Aug
PMID:Differing reactivities of human and guinea-pig complement on haptenized liposomes via the alternative pathway. 619 29

Bifunctional antigens composed of one L-tyrosine-p-azobenzenearsonate (Tyr-ABA) carrier epitope and one dinitrophenyl (DNP) haptenic epitope separated by 6-aminocaproyl or polyprolyl spacers induced weak IgM anti-DNP plaque-forming cell (PFC) responses in the spleens of mice immunized intraperitoneally, without detectable IgG PFC. However, the same antigens introduced into the footpads induced IgG PFC responses in the draining lymph nodes which rose to levels greater than 100/10(6) viable lymphocytes. Moreover, the response in the lymph nodes to booster injections of antigen was characteristic of secondary T-dependent antibody responses, whereas the splenic secondary response simply mirrored the primary. The magnitude of the IgG PFC response was influenced by the size of the spacer and by the strain of mice, although genetic control did not map to the major histocompatibility complex. Prior i.p. immunization suppressed the IgG response to subsequent immunization in the footpads. This suppression could be transferred to normal syngeneic recipient mice with spleen cells from suppressed donors. Suppressor activity was eliminated by treating the spleen cells with anti-Thy-1 antibody prior to transfer, establishing the T-cell dependency of suppression. Suppression was also induced by Tyr-ABA itself, but not by DNP-lysine, indicating the epitope specificity of the suppressor cells. Thus, bifunctional antigens induce dominant suppression in the spleen but significant help in lymph nodes.
Mol Immunol 1984 Jun
PMID:Differential induction of help and suppression in mice by bifunctional antigens administered via different routes. 620 50

The structural components of antigen molecules that interact with class II major histocompability complex (MHC) molecules on antigen-presenting cells (APCs) (agretopes) and with antigen receptors of T-lymphocytes (epitopes) in class II restricted T-cell responses have not been precisely defined. This issue was addressed here using murine T-cell clones specific for the simple immunogen L-tyrosine-p-azobenzenearsonate (ABA-tyr) and a series of analogs of the homologous antigen. Two experimental approaches were used. First, APCs were pulsed with analogs and used to stimulate T-cell proliferation. The patterns of stimulation segregated the clones into two specificity groups and indicated that the epitope recognized by the T-cell included the arsonate group and elements in the side chain of tyrosine. Furthermore, the clones manifest different sensitivities to antigen. Second, non-stimulatory analogs were used to block the presentation of ABA-tyr in an effort to define the agretope. Compounds containing the azophenyl group blocked presentation of ABA-tyr in a dose-dependent fashion, whereas p-arsanilic acid and L-tyrosine were ineffective. The blocking was specific inasmuch as the compounds had no effect on the antigen-induced proliferative responses of giant keyhole limpet hemocyanin (KLH) or hen egg white lysozyme (HEL)-reactive T-cell clones. The blocking pattern indicated that the feature required for productive association with the APC centered on the planar structure of the azo-linked aromatic rings, with little or no contribution from either the arsonate moiety or the tyrosyl side chain. We propose that this structure forms an agretope for this family of compounds.
Mol Immunol 1984 Oct
PMID:The anatomy of an antigen molecule: functional subregions of L-tyrosine-p-azobenzenearsonate. 620 67

Two monoclonal anti-p-azobenzene-arsonate antibodies produced by cell fusion of A/J spleen lymphocytes were selected. It had previously been shown that they both expressed the cross-reactive idiotype (CRI) and that the amino terminal sequence of their heavy chain variable region differed by only one amino acid substitution within the first 55 residues, at residue 41 in the second framework region. A novel, sensitive peptide-mapping method had indicated that the light chain of these two antibodies differed by at least three amino acid substitutions. Here, the complete amino acid sequence of the light chain variable region is presented. There are only 3 amino acid substitutions between the two antibodies, located in the first and second complementarity determining regions and the third framework region respectively. Although the variable region of the light chains of these two monoclonal antibodies show such a high degree of homology they differ by 26 and 27 substitutions from the reference sequence of the light chain of CRI+ anti-ABA serum antibodies. In addition, they are homologous to 4 other such CRI+ monoclonal antibody light chain sequences published so far, in which only 2 of the above 3 substitutions are not represented. The contribution of the light chain to the CRI is discussed.
Mol Immunol 1983 Feb
PMID:The complete amino acid sequence of the light chain variable region of two monoclonal anti-p-azobenzene-arsonate antibodies bearing the cross-reactive idiotype. 640 99

The nucleotide sequence and derived amino acid sequence were determined for a full-length version of the tomato cDNA clone, pTOM75, the mRNA for which has previously been shown to accumulate in roots, ripening fruit and senescing leaves. Computer analysis of the predicted protein product, which we have named tomato ripening-associated membrane protein (TRAMP) indicates strong homology to known transmembrane channel proteins from other organisms. Northern analysis showed that this gene was induced by waterstress and that this induction was unaffected in an ABA-deficient genetic background.
Plant Mol Biol 1994 Feb
PMID:Nucleotide sequence and expression of a ripening and water stress-related cDNA from tomato with homology to the MIP class of membrane channel proteins. 751 Jan 35

We have isolated two Rare Cold-Inducible (RCI1 and RCI2) cDNAs by screening a cDNA library prepared from cold-acclimated etiolated seedlings of Arabidopsis thaliana with a subtracted probe. RNA-blot hybridizations revealed that the expression of both RCI1 and RCI2 genes is induced by low temperature independently of the plant organ or the developmental stage considered. However, RCI1 mRNA accumulates faster and at higher levels than the RCI2 one indicating that these genes have differential responsiveness to cold stress. Additionally, when plants are returned to room temperature, RCI1 mRNA decreases faster than RCI2. In contrast to most of the cold-inducible plant genes characterized, the expression of RCI1 and RCI2 is not induced by ABA or water stress. The nucleotide sequences of RCI1 and RCI2 cDNAs predict two acidic polypeptides of 255 and 251 amino acids with molecular weights of 29 and 28 kDa respectively. The alignment of these polypeptides indicates that they have 181 identical amino acids suggesting that the corresponding genes have a common origin. Sequence comparisons reveal no similarities between the RCI proteins and any other cold-regulated plant protein so far described. Instead, they demonstrate that the RCI proteins are highly homologous to a family of proteins, known as 14-3-3 proteins, which are thought to be involved in the regulation of multifunctional protein kinases.
Plant Mol Biol 1994 Jul
PMID:Two related low-temperature-inducible genes of Arabidopsis encode proteins showing high homology to 14-3-3 proteins, a family of putative kinase regulators. 752 Mar 1

The pea (Pisum sativum) gene Cyp15a encodes a protein with sequence similarity to cysteine proteases. Expression of Cyp15a was investigated during pea seedling development and in response to environmental stress. Cyp15a shows increased transcription and elevated mRNA levels in plant tissues that are partially dehydrated or treated with 0.6 M mannitol. Cyp15a mRNA levels also increase in seedlings treated with 0.2-0.25 M NaCl or KCl. During development, Cyp15a mRNA levels increase within 6 to 12 h in cotyledons and axes during germination and continue to increase for at least 96 h. Illumination of dark-grown seedlings increased Cyp15a mRNA abundance in elongating and non-elongating stem tissues. GA and ABA, which modulate the abundance of many seed-localized cysteine proteases, did not significantly modulate Cyp15a mRNA levels in stems. The protein encoded by Cyp15a contains a typical amino-terminal secretory targeting domain. This domain is followed by a pro-sequence containing ca. 110 amino acids that is found in other cysteine proteases. Polyclonal antibodies, directed against CYP15a, recognized both the larger pro-form and the cleaved mature form of CYP15a on western blots. Immunolocalization assays indicated that both forms of the protein are located in cell walls of stem cortical cells.
Plant Mol Biol 1995 Sep
PMID:A salt- and dehydration-inducible pea gene, Cyp15a, encodes a cell-wall protein with sequence similarity to cysteine proteases. 754 23

cDNA fragments from ten different protein kinases expressed in Avena sativa aleurone cells were amplified from mRNA by RT-PCR with degenerate primers. These could be classified into five groups: Aspk1-3 showed homology to the Snf1-related protein kinases, Aspk4-5 to a wheat ABA up-regulated protein kinase, Aspk6-8 to the Ca-dependent, calmodulin-independent protein kinase family, Aspk9 encoded a MAP kinase and Aspk10 was closely related to a novel Arabidopsis ribosomal protein kinase. GA caused a rapid increase in transcripts hybridising to Aspk10, while inhibiting the dramatic accumulation of transcripts hybridising to Aspk9 that occurred in the absence of GA.
Plant Mol Biol 1995 Mar
PMID:Gibberellin-regulated expression in oat aleurone cells of two kinases that show homology to MAP kinase and a ribosomal protein kinase. 776 74

A cDNA clone, RGA1, was isolated by using a GPA1 cDNA clone of Arabidopsis thaliana G protein alpha subunit as a probe from a rice (Oryza sativa L. IR-36) seedling cDNA library from roots and leaves. Sequence analysis of genomic clone reveals that the RGA1 gene has 14 exons and 13 introns, and encodes a polypeptide of 380 amino acid residues with a calculated molecular weight of 44.5 kDa. The encoded protein exhibits a considerable degree of amino acid sequence similarity to all the other known G protein alpha subunits. A putative TATA sequence (ATATGA), a potential CAAT box sequence (AGCAATAC), and a cis-acting element, CCACGTGG (ABRE), known to be involved in ABA induction are found in the promoter region. The RGA1 protein contains all the consensus regions of G protein alpha subunits except the cysteine residue near the C-terminus for ADP-ribosylation by pertussis toxin. The RGA1 polypeptide expressed in Escherichia coli was, however, ADP-ribosylated by 10 microM [adenylate-32P] NAD and activated cholera toxin. Southern analysis indicates that there are no other genes similar to the RGA1 gene in the rice genome. Northern analysis reveals that the RGA1 mRNA is 1.85 kb long and expressed in vegetative tissues, including leaves and roots, and that its expression is regulated by light.
Plant Mol Biol 1995 Mar
PMID:Molecular cloning and characterization of RGA1 encoding a G protein alpha subunit from rice (Oryza sativa L. IR-36). 776 94

Ten normal human trabecular meshworks were examined by electron microscopy using avidin-biotin complex in order to investigate the localization of binding sites of eight lectins. The tissue specimens were fixed in paraformaldehyde and glutaraldehyde mixture and embedded in Lowicryl K4M at low temperature. The ultrathin sections were stained with biotin labelled lectins and colloidal gold labelled streptoavidin and were observed with the conventional transmission electron microscope. Some lectins such as ABA, ConA and DSA were localized on fine fibrils underneath the endothelium of the trabecular wall of the Schlemm's canal, electron-dense cores of elastic fibers, fine granular like materials, basement membranes, collagen fibers and the long-spacing fibers. However, the other lectins such as DBA, SBA, Lotus, UEA-I and RCA60 were not specifically localized in these tissues. From the results it was demonstrated that the differential ultrastructural localization of glycoconjugate residues in the human trabecular meshworks can be revealed using this lectin staining.
Cell Mol Biol (Noisy-le-grand) 1995 Mar
PMID:Electron microscopic lectin histochemistry of the trabecular meshworks in human eyes. 778 42


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