Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0032285 (pneumonia)
 54,520 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Physico-chemical properties of gamma-globulin fraction and immunoglobulins G (IgG) were studied, using temperature-perturbational differential spectrophotometry and ion exchange chromatography on DEAE cellulose, in blood serum of 118 patients with impairments of thyroid gland and of 28 patients with chronic pneumonia. Amount of tyrosine residues, perturbated by temperature, was decreased and an alkaline subfraction was increased in IgG of patients with toxic goiter and chronic pneumonia; the increase in the alkaline subfraction was more distinct in impairments of thyroid gland. The data obtained suggest that the alkaline subfraction is characterized by an increased rigidity and apparently by altered structural properties in toxic goiter. The tyrosine residues in IgG enable to evaluate effectively the availability of a cavity between variable domains (antigen-antibody site) of the immunoglobulin.
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PMID:[Subfractional composition and structural characteristics of G immunoglobulins in pathological states]. 44 82

The p28 core polypeptides of four isolates of caprine arthritis-encephalitis virus (CAEV) from goats was compared with those of visna virus (VV) and progressive pneumonia virus (PPV) from sheep. Monoclonal antibodies recognized p28 epitopes common to all six retrovirus isolates, a p28 epitope on four CAEV isolates, but not VV and PPV isolates, a p28 epitope on four CAEV isolates and VV, but not PPV and a p28 epitope unique to the CAEV isolate used for immunizing the mouse spleen donor. Comparison of two-dimensional maps of tyrosine containing tryptic peptides of p28 demonstrated that three CAEV isolates had similar maps while a fourth CAEV isolate, VV and PPV had several different from the three closely related CAEV p28s and from each other.
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PMID:Antigenic and structural variation of the p28 core polypeptide of goat and sheep retroviruses. 244 Sep 85

The primary antibody response of mice to phosphorylcholine (PC) is dominated by antibodies using the T15 L chain. Anti-PC antibodies using the 511 L chain are prominent only in secondary responses to PC coupled to proteins, are somatically mutated, and all have an extra amino acid at the Vh-D junction, compared with T15 antibodies. The aim of the experiments reported here was to determine if the extra junctional amino acid alone was sufficient to generate a 511 PC-binding antibody, or if somatic mutation or other junctional changes were also necessary. We also wished to determine if unmutated 511 antibodies had sufficient affinity for PC to appear in the primary response. To increase the frequency of primary 511 antibodies, we generated a series of hybridomas from M167 L chain transgenic mice immunized 4 days earlier with either Streptococcus pneumonia R36a or PC-keyhole limpet hemocyanin (KLH). We determined the relative affinity of the antibodies, and sequenced their H chain V regions. The results showed that: 1) somatic mutations are not required for 511 antibodies to bind PC; 2) primary 511 antibodies all had lower relative affinities for PC than T15 while having similar affinities to T15 for TNP-aminophenyl PC, and higher affinities for the PC analogs nitrophenyl PC and choline; 3) all antibodies had the 511-specific insertion of an extra amino acid, usually Ala, at the VhD junction, compared with T15; 4) immunization with R36a, but not PC-hemocyanin, elicited antibodies with a specific Tyr----Asp substitution in the D region, indicating Ag selection based on fine specificity differences; 5) the total length of CDR3 was conserved in most anti-PC-hemocyanin antibodies, whereas the anti-R36a antibodies predominantly had longer CDR3 sequences; and 6) there were unique substitutions in most antibodies, including significant sequence heterogeneity in the D-Jh junction. We conclude that Ag selection on the basis of affinity for PC biases the primary anti-PC response in favor of T15, and that 511 precursors with their alternative fine specificities contribute the precursors that are expanded in the secondary anti-PC-KLH responses.
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PMID:Sequence and fine specificity analysis of primary 511 anti-phosphorylcholine antibodies. 251 48

Four strains of nutritionally variant streptococci (NVS) were isolated from the milk of mastitic cows and one strain from the lungs of a laboratory Norway rat which died from suppurative pneumonia. In primary cultivation NVS grew aerobically and anaerobically within 48-hour incubation at a temperature of 37 degrees C as minute nonhemolytic satellite colonies around a previously overlaid S. aureus strain or around other gram-positive and gram-negative bacteria. In the first subcultures NVS were growing in nutrient media enriched with 10% bovine serum and 5% staphylococcal filtrate, or 0.02% to 0.002% pyridoxal hydrochloride. All isolates did not grow in presence of 10%, 40% bile, and 6.5% of sodium chloride, neither did they grow at a temperature of 45 degrees C, they did not hydrolyze sodium hippurate, esculin, arginine, they did not produce levane and dextran from saccharose, they produced acid from mannitol, sorbitol, inulin, lactose, raffinose, trehalose, glucose, saccharose and maltose. Two strains produced acid from xylose and four strains from salicin. The strains isolated from mastitis did not have different biochemical properties from those isolated from a laboratory Norway rat with pneumonia. All strains of NVS were sensitive to chloramphenicol, ampicillin, gentamycin, lincomycin and cephalothin, four strains were sensitive to erythromycin and tyrosine, two to penicillin and one to streptomycin, oxytetracycline, chlortetracycline and novobiocin. All strains were resistant to neomycin, tetracycline, oxacillin and sulphonamides. The antigen prepared from the isolated strains by the method of Fuller did not react with any streptococcal group serum A-Z.
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PMID:[Isolation and characteristics of nutritional variants of streptococci of animal origin]. 275 16

A new biotype of L. dumoffii was isolated from lung and sputum samples of an immunosuppressed patient with pneumonia. This strain differs from other described strains of L. dumoffii in that it fails to produce browning of tyrosine-containing buffered yeast extract medium.
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PMID:A new biotype of Legionella dumoffii. 398 5

We investigated a T-cell activation deficiency in a 3-month-old boy with protracted diarrhea, serious cytomegalovirus pneumonia, and a family history (in a brother) of cytomegalovirus infection and toxoplasmosis. In spite of detection of normal number of peripheral lymphocytes, T cells did not proliferate after activation by anti-CD3 and anti-CD2 antibodies, although proliferation induced by antigens was detectable. We sought to determine the origin of this defect as it potentially represented a valuable tool to analyze T-cell physiology. T-cell activation by anti-CD3 antibody or phytohemagglutinin (PHA) led to reduced interleukin-2 (IL-2) production and abnormal nuclear factor-activated T cell (NF-AT; a complex regulating the IL-2 gene transcription) binding activity to a specific oligonucleotide. T-cell proliferation was restored by IL-2. Early events of T-cell activation, such as anti-CD3 antibody-induced cellular protein tyrosine phosphorylation, p59fyn and p56lck kinase activities, and phosphoinositide turnover, were found to be normal. In contrast, anti-CD3 antibody-induced Ca2+ flux was grossly abnormal. Release from endoplasmic reticulum stores was detectable as tested in the presence of anti-CD3 antibody or thapsigargin after cell membrane depolarization in a K+ rich medium, whereas extracellular entry of Ca2+ was defective. The latter abnormality was not secondary to defective K+ channel function, which was found to be normal. A similar defect was found in other hematopoietic cell lineages and in fibroblasts as evaluated by both cytometry and digital video imaging experiments at a single-cell level. This primary T-cell immunodeficiency appears, thus, to be due to defective Ca2+ entry through the plasma membrane. The same abnormality did not alter B-cell proliferation, platelet function, and polymorphonuclear neutrophil (PMN) function. Elucidation of the mechanism underlying this defect would help to understand the physiology of Ca2+ mobilization in T cells.
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PMID:A primary T-cell immunodeficiency associated with defective transmembrane calcium influx. 753 12

Bone marrow cells of various animal species and humans produce a group of bioregulatory peptides called myelopeptides (MPs). MPs have been isolated and purified, and their physico-chemical properties have been investigated. MPs have a wide spectrum of functional activities: immunoregulatory, differentiating, and opiate-like. A new immunocorrective drug, Myelopidum, which is used effectively in clinical practice for treating diseases accompanied by immunodeficiency, has been created on the basis of MPs. Administration of Myelopidum after surgery prevents 50% to 70% of postsurgical complications, particularly postsurgery pneumonia, and also normalizes the number and balance of T-helper cells, T-suppressor cells, and B-lymphocytes in patients with chronic pulmonary diseases, resulting in a beneficial clinical effect, including a significant prolongation of remission periods. Myelopidum is also used in veterinary medicine for prophylaxis and treatment of pneumonia and enteritis in newborn and young animals. The primary structure of several myelopeptides is established. The functional activities of two, MP-1 (Phe-Leu-Gly-Phe-Pro-Thr) and MP-2 (Leu-Val-Val-Tyr-Pro-Trp), are being investigated.
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PMID:Myelopeptides: new immunoregulatory peptides. 856 25

We previously demonstrated that hematopoietic cell protein-tyrosine phosphatase is one of the molecules that can transduce Fas-mediated apoptosis signals in lymphoid cells. The present study analyzed the effect of defective Fas signaling on the T cell phenotype and apoptosis function in hematopoietic cell protein-tyrosine phosphatase-deficient motheaten mice. Viable motheaten (me(v)/me(v)) mice exhibited increased T cell proliferation and defective activation-induced apoptosis of Fas+ T cells in the lymph node, which was not ascribed to defective Fas ligand function. Furthermore, the Fas-mediated apoptosis defect in activated T cells from me(v)/me(v) mice was confirmed by their resistance to anti-Fas-induced apoptosis. No protein tyrosine dephosphorylation signal was delivered after anti-Fas cross-linking in the lymph node cells of me(v)/me(v) mice as revealed by 32Pi labeling of protein phosphatase substrates. The defective activation-induced apoptosis of Fas+ T cells in me(v)/me(v) mice led to lymphadenopathy with an accumulation of CD4- CD8- B220+ CD3+ T cells. Pneumonitis in me(v)/me(v) mice was associated with infiltration of cycling T cells detected by bromodeoxyuridine uptake in vivo. Thus, T cells from me(v)/me(v) mice are resistant to Fas-mediated apoptosis which results in lymphoproliferative disease and tissue infiltration.
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PMID:Hematopoietic cell protein-tyrosine phosphatase-deficient motheaten mice exhibit T cell apoptosis defect. 866 88

4 wk after intraperitoneal inoculation of 0.2 LD50 (50% lethal dose) of murine cytomegalovirus (MCMV) in adult BALB/c mice, MCMV remained detectable in the salivary glands, but not in the lungs or other organs. When the T cells of these mice were activated in vivo by a single injection of anti-CD3 monoclonal antibody, interstitial pneumonitis was induced in the lungs that were free of the virus with an excessive production of the cytokines. In the lungs of such mice persistently infected with MCMV, the mRNA of the cytokines such as IL-2, IL-6, TNF-alpha, and IFN-gamma were abundantly expressed 3 h after the anti-CD3 injection, and the elevated levels continued thereafter. A marked expression of inducible nitric oxide synthetase (iNOS) was then noted in the lungs, suggesting that such cytokines as TNF-alpha and IFN-gamma may have induced iNOS. Although the increase in NO formation was demonstrated by the significant elevation of the serum levels of nitrite and nitrate, the interstitial pneumonitis was not associated with either increased superoxide formation or peroxynitrite-induced tyrosine nitration. Nevertheless, the administration of an NO antagonist also alleviated the interstitial pneumonitis provoked by anti-CD3 mAb. Based on these findings, it was concluded that MCMV-associated pneumonitis is mediated by a molecule of cytokine-induced NO other than peroxynitrite.
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PMID:Nitric oxide mediates murine cytomegalovirus-associated pneumonitis in lungs that are free of the virus. 931 83

A 60-year-old woman was admitted in June 1993, because of anemia and purpura and given a diagnosis of acute myelogenous leukemia with trilineage dysplasia. She entered partial remission (PR) after three courses of low-dose Ara-C and G-CSF, but never reached complete remission (CR) in spite of additional chemotherapy. In October 1994, the number of leukocytes, myeloblasts, and erythroblasts in the patient's peripheral blood increased, and her clinical condition deteriorated. The disease was resistant to other therapy. The patient had pneumonia and died of septic shock in December 1994. A chromosomal analysis performed on admission showed 46,XX,t(3;5) (q21;q31) [9/9]. As an additional chromosomal abnormality, deletion of the X chromosome was observed in January, 1994. Analysis of the p53 gene by the polymerase chain reaction-single strand conformation polymorphism method showed one base transposition, from TAT to TGT (Tyr to Cys), at codon 220 of exon 6. Karyotype evolution and p53 gene mutation were observed during the disease course and may have been related to progression of the disease.
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PMID:[t(3;5) (q21;q31) chromosomal abnormality in a patient with acute myelogenous leukemia with trilineage myelodysplasia]. 979 99


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