Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0153470 (Spleen)
 4,015 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of related and unrelated compounds on the specific binding of dinitrophenyl-coupled bacteriophage (DNP-T4) to lymphoid cell receptors has been examined and compared with the effect on the neutralization of DNP-T4 by anti-DNP serum. Spleen cells and sera from Balb/c mice immunized with DNP-bovine serum albumin were used. The binding of DNP-T4 to the cells was inhibited by DNP-eAcp, di-DNP-Lys, DNP-Tyr, DNP-p(Ornith) and DNP-BSA (among the DNP-derivatives tested), TNP-BSA, ARS-p(Tyr) and TGA. In addition with the above named DNP and TNP compounds, the DNP-T4neutralization by antiserum was also prevented by DNP-derivatives with either L-cysteic acid, alanine, glutamine or poly-L-glutamic acid, while ARS-p(Tyr) and TGA were not effective. Plain carriers (BSA, HSA, poly-ornithine, polylysine and polyglutaminc acid) and cell-mitogens (ConA, LPS and PPD) had no significant inhibitory effect. The results obtained indicate the occurrence of differences between cell-bound receptors and circulating antibodies in what concerning their specific reaction with the dinitrophenyl determinant.
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PMID:Inhibition of specific binding of DNP (dinitrophenyl) determinant to lymphoid-cell receptors by related and unrelated compounds : quantitative studies in vitro. 6 Sep 7

The possibility was investigated that Ir genes regulate the function of cells other than T or B cells in the primary IgM responses to the synthetic antigens trinitrophenylated poly-L-(Tyr,Glu)-poly-D,L-Ala--poly-L-Lys [TNP-(T,G)-A--L]and trinitrophenylated poly-,-(His,Glu)-poly-D, L-Ala--poly-L-Lys [TNP-(H,G)-A--L]. The primary responses of (B10 x B10.A)F(1) spleen cells to both antigens were abrogated by Sephadex G-10 passage, and restored by the addition of spleen adherent cells. The cell type in the spleen adherent cell population active in reconstituting the responses to TNP-(T,G)-A--L and TNP-(H,G)-A--L was a non-T, non-B, radiation-resistant, glass-adherent spleen cell. The responses of Sephadex G-10-passed (responder x nonresponder)F(1) spleen cells to TNP-(T,G)-A--L or TNP-(H,G)-A--L were reconstituted by spleen adherent cells from only responder strains. Spleen adherent cells from F(1) mice reconstituted the responses to both antigens. Spleen adherent cells from each of the strains tested reconstituted the non- Ir gene-controlled response to a third antigen, TNP-keyhole limpet hemocyanin. The inability of spleen adherent cells from nonresponder strains to reconstitute the responses to either TNP-(T,G)-A--L or TNP-(H,G)-A--L was not a result of active suppression induced by the presence of nonresponder adherent cells, since a mixture of responder and nonresponder spleen adherent cells reconstituted the responses to both antigens. The use of spleen adherent cells from recombinant strains demonstrated that the autosomal dominant genes controlling the ability of spleen adherent cells to function as accessory cells in the responses to TNP-(T,G)-A--L and TNP-(H,G)-A--L are located in the K or I-A regions of the responder H-2 complex, the same region(s) of H-2 as the Ir genes controlling overall in vitro and in vivo responsiveness to these antigens.
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PMID:Cellular and genetic control of antibody responses in vitro. III. Immune response gene regulation of accessory cell function. 9 11

Anaerobic diphtheroids possessing lympho-reticular stimulatory properties may differ considerably in their peptidoglycan composition. Spleen weight-increasing activity of strains directly parallels their antitumour properties. P. granulosum strains, inactive in assays for lympho-reticular stimulation, appear to have a higher cell wall alanine content than most of the P. acnes and P. avidum strains tested. Two P. acnes strains, however, had equivalently high alanine ratios and were stimulatory. The presence of galactose does not appear to be required for activity since P. acnes II strains which lack this sugar can be fully stimulatory. The existence of the species P. lymphophilum (Torrey) is further supported by the finding of two more serologically identical strains which do not cross react serologically with the other species in the group. These organisms are fully stimulatory but have lysine rather than DAP as their cell wall diamino acid.
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PMID:Comparative studies on the cell wall composition of some anaerobic coryneforms of varying lympho-reticular stimulatory activity. 60 97

Spleen cell suspensions from AKR and CD-1 mice contain peroxidase activity as determined by guaiacol oxidation. This activity is found predominately in the 20,000 x g pellet fraction of spleen cell homogenates. In the presence of H(2)O(2) and chloride ion at acidic pH, splenic peroxidase mediates the oxidation of d- or l-alanine to CO(2), NH(3), and acetaldehyde. The same reaction mixture without added amino acid can kill both gram-positive and gram-negative bacteria. The conditions for both reactions are similar. Both have an absolute requirement for H(2)O(2) and chloride ion, neither is active at neutral or alkaline pH, and both are inhibited by the sulfonic amino acid taurine. In these aspects, splenic peroxidase is qualitatively similar in its activity to myeloperoxidase (MPO) from polymorphonuclear leukocytes. It is quantitatively different from MPO in that the latter is more potent on a per guaiacol unit basis with respect to both amino acid oxidation and bactericidal activity. Still another quantitative difference is that splenic peroxidase requires 0.1 m NaCl for activity, whereas MPO functions with as little as 0.005 m NaCl. Splenic peroxidase and MPO both appear to differ qualitatively from horseradish peroxidase in that the latter enzyme does not mediate amino acid oxidation.
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PMID:Mouse splenic peroxidase and its role in bactericidal activity. 463 63

The existence of T cells specific for soluble antigens in association with unique F(1) or recombinant major histocompatibility complex (MHC) gene products was first postulated from studies on the proliferative response of whole T cell populations to the antigen poly(Glu(55)Lys(36)Phe(9))(n) (GLphi). In this paper we use the newly developed technology of T lymphocyte cloning to establish unequivocally the existence of such cells specific for GLphi and to generalize their existence by showing that F(1)- specific cells can be isolated from T cell populations primed to poly(Glu(60)Ala(30)Tyr(10))(n) (GAT) where such clones represent only a minor subpopulation of cells. Gl.4b-primed B10.A(5R) and GAT-primed (B10.A x B10)F(1) lymph node T cells were cloned in soft agar, and the colonies that developed were picked and expanded in liquid culture. The GLphi-specific T cells were then recloned under conditions of high-plating efficiency to ensure that the final colonies originated from single cells. T cells from such rigorously cloned populations responded to stimulation with GILphi but only in the presence of nonimmune, irradiated spleen cells bearing (B10.A x B10)F(1) or the syngeneic B 10.A(5R) recombinant MHC haplotype. Spleen cells from either the B10 or B 10.A parental strains failed to support a proliferative response, even when added together. (B10 x B10.D2)F(1) and (B10 x B10.RIII)F(1) spleen cells also supported a proliferative response but (B10 x B10.Q)F(1) and (B10 X B10.S)F(1) spleen cells did not. These results suggested that the T cell clones were specific for GL[phi} in association with the beta(AE)(b)-alpha(E) (k,d,r,) Ia molecule and that recognition required both gene products to be expressed in the same antigen-presenting cells. Support for this interpretation was obtained from inhibition experiments using the monoclonal antibody Y-17 specific for a determinant on the beta(AE)(b)-alphaE Ia molecule. Y-17 completely inhibited the proliferative response of a GLphi-specific clone but had no effect on the response of either a PPD-specific or GAT-specific clone, both of which required the beta(A)-alpha(A) Ia molecule as their restriction element. No evidence could be found for the involvement of suppressor T cells in this inhibition. We therefore conclude that the phenomenon of F(1)-restricted recognition by proliferating T cells results from the presence of antigen- specific clones that must recognize unique F(1) or recombinant Ia molecules on the surface of antigen-presenting cells in addition to antigen in order to be stimulated.
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PMID:Antigen-specific T cell clones restricted to unique F1 major histocompatibility complex determinants. Inhibition of proliferation with monoclonal anti-Ia antibody. 616 4

Using a synthetic peptide (Glu-Asp-Ala-Glu-Tyr-Ala-Ala-Arg-Arg-Arg-Gly) as a substrate, various normal tissues from the rat were probed for tyrosine protein kinase activity. Spleen was shown to contain much higher tyrosine protein kinase activity than other rat tissues (lung, brain, testes, liver, kidney, heart, and thymus, in decreasing order of specific activity). Most of the tyrosine protein kinase activity of the various rat tissues (greater than 80%) was present in the particulate fraction, and Nonidet P-40, a nonionic detergent, could activate the particulate form of the enzyme 2-20-fold in many of the tissues. Epidermal growth factor (1 microgram/ml), cyclic AMP, cyclic GMP, or Ca2+ did not increase spleen tyrosine protein kinase activity. Half-maximal enzyme activity was observed at 60-80 microM MgATP and at 2.2 mM peptide, and both Mg2+ (10 mM) and Mn2+ (0.5-1.0 mM) were effective divalent metal ions for the expression of activity. When the particulate fraction of spleen was incubated with [gamma-32P]ATP followed by polyacrylamide gel electrophoresis in the presence of Na dodecyl SO4, a number of alkali-stable bands were identified by autoradiography. Two major bands at Mr = 53,000 and 56,000 were shown to contain phosphotyrosine. Two similar alkali-stable bands containing phosphotyrosine but with lower amounts of 32P labeling were also observed in the particulate fractions of various other tissues (lung, brain, kidney, and testes). The particulate form of tyrosine protein kinase of rat spleen could be solubilized by using high concentrations of Nonidet P-40 (5%) at an alkaline pH (pH 9.0). Partial purification and subsequent filtration on Sephacryl S-200 yielded a peak of tyrosine protein kinase activity with an apparent molecular weight of 55,000. The two major phosphorylated bands of Mr = 53,000 and 56,000 co-migrated with the peak of enzyme activity. The solubilized and partially purified enzyme preparation phosphorylated only tyrosine residues when either endogenous proteins or casein were used as substrates. These results suggest that relatively high activities of tyrosine protein kinase exist in a normal tissue (rat spleen). Major endogenous substrates of the enzyme(s) appear to be represented by two proteins of Mr = 53,000 and 56,000; one or both of these substrates may be the tyrosine protein kinase itself.
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PMID:Tyrosine protein kinase activity of rat spleen and other tissues. 668 16

Three point mutations on the Np(b) allele of the purine nucleoside phosphorylase locus in the mouse have been recovered by male germ cell mutagenesis. The mutants were backcrossed, 12-14 generations, and are designated in increasing order of severity of enzyme deficiency and phenotype: B6-NPE, Met-87 --> Lys; B6-NPF, Ala-228 --> Thr; and B6-NPG, Trp-16 --> Arg. A marked decline in total cell numbers per thymus occurs between 2 and 3 months for the more severe B6-NPF and B6-NPG mutants (35% and 52%, respectively) and by 8 months for the less severe B6-NPE mutation. The thymocyte population is thereafter characterized by a 3- or 8-fold expanded precursor, CD4-CD8- double-negative population and 15% or 55% reduced CD4+CD8+ double-positive cells for the B6-NPF and B6-NPG strains, respectively. Spleen lymphocyte Thy-1+ cells are reduced by 50% and spleen lymphocyte response to T cell mitogen and interleukin 2 is reduced by 80%. Increases of thymocyte dGTP pools of 5- and 2.5-fold for B6-NPF and B6-NPG mutants, respectively, are observed. The purine nucleoside phosphorylase-deficient mouse exhibits age-dependent progressive perturbations in thymocyte differentiation, reduced numbers of thymocytes, and reduced splenic T cell numbers and response. The progressive T cell deficit is similar to the human disorder.
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PMID:Point mutations at the purine nucleoside phosphorylase locus impair thymocyte differentiation in the mouse. 912 28

Spleen cells from BALB/c or BALB-Igb mice immunized against the determinant oligo-D-alanine were transferred to the following recipients: normal BALB/c; lethally irradiated BALB/c; and congenitally athymic BALB/c-nu. Irradiated as well as nude recipients permitted the development of a strong adoptive antibody response, while the response in normal BALB/c recipients was very low ("isogeneic barrier"). Using allotypically marked spleen cells from BALB-Igb donors it was shown that the antibodies in irradiated as well as in nude recipients were produced by donor cells. The same conclusion was drawn by assessing isoelectric focusing spectra, which in each transfer displayed the individually characteristic pattern of the donor. In addition to specific antibodies, the donor cells produced considerable levels of IgG, as characterized by allotype, but again only in nude and in irradiated recipients. The ready permissiveness of nude recipients towards congenic memory cells could be abolished when prospective recipients were restored, some time prior to transfer, by BALB/c thymus or BALB/c spleen cells. The results are interpreted to suggest that the isogeneic barrier in normal recipients is due to a thymus-dependent suppression or rejection of memory cells by the recipients.
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PMID:Permissiveness of athymic ("nude") mice towards congenic memory cells. 1199 24

Podophyllotoxin, 10(-3) (M), inhibits the respiration in vitro of rat lymph nodes, thymus, kidney, tumor, spleen, liver, brain, testis, and chicken embryo. Lymph node and spleen respiration are most sensitive, and the degree of inhibition increases with time. The injection of podophyllotoxin into tumor-bearing mice (20 mg. per kg.) causes a dramatic reduction in the respiration of tumor slices. Within 6 hours, the respiration approaches zero. Inhibition is evident 2 hours after injection of the drug. Spleen respiration is reduced 50 per cent within 6 hours. Kidney and liver respirations remain within normal limits. Marked reductions in the respiration of spleen, lymph nodes, and thymus glands of normal rats are produced by the injection of 15 mg. per kg. Thymus gland is the most sensitive of these three tissues, and its respiration is reduced 66 per cent 24 hours after injection of the drug. The injection of 0.8 microgram podophyllotoxin into the yolk sac of chicken eggs bearing 5 day embryos has no effect on the respiration of the embryo within 8 hours, although this is a sufficiently toxic dose to kill 80 per cent of the embryos (within 24 hours). Kidney respiration in the presence of acetate, glucose, alanine, and glutamate is inhibited to approximately the same degree as in the absence of added substrate. Succinate and pyruvate oxidation by rat kidney slices appear to be less sensitive. Oxidation of acetate and butyrate by rabbit kidney homogenate is more sensitive to podophyllotoxin than oxidation by rabbit kidney homogenate without added substrate. Glucose oxidation by this preparation is not inhibited by 10(-3)M podophyllotoxin. The anaerobic glycolysis of chicken embryo, rat brain, and rat testis is stimulated by 10(-5) and 10(-6)M podophyllotoxin, and is inhibited by 10(-3)M. The following enzymes are not inhibited by 10(-3)M podophyllotoxin: succinoxidase from pigeon breast muscle, choline, xanthine and tyrosine oxidase from rat liver homogenate, and leucine oxidase from Proteus vulgaris; alkaline and acid phosphatase from dog serum; adenosine triphosphatase from rat liver; choline esterase from rat brain homogenate; ribonucleodepolymerase from spleen mince and thymonucleodepolymerase from dog serum. High concentrations of podophyllotoxin do not influence the viscosity and degree of polymerization of thymonucleic acid.
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PMID:The effect of podophyllotoxin on tissue metabolism and enzyme systems. 1539 71