Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0024530 (malaria)
 44,886 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. We have measured plasma concentrations of alpha 1-acid glycoprotein (AGP) in 18 healthy children and 85 children with falciparum malaria in Malawi. In addition, we determined the degree of protein binding of quinine (QN) in the plasma of 52 of the patients and each of the healthy controls. 2. The mean plasma AGP concentration was higher in patients than in controls (P less than 0.0001) and remained elevated 3 weeks after complete resolution of malaria infection. 3. The mean unbound QN fraction was significantly less (P less than 0.00001) in patients with malaria (0.128 +/- 0.037) than in controls (0.193 +/- 0.051) and significantly higher (P = 0.02) in convalescence (0.153 +/- 0.067) than during acute illness. 4. There were highly significant negative correlations between plasma AGP concentration and the free QN fraction in spiked plasma samples (r = -0.534, P less than 0.0001, n = 93) and in clinical samples (r = -0.484, P less than 0.00001, n = 225). There was a significant positive correlation between plasma concentrations of AGP and another acute phase reactant, C reactive protein (P less than 0.001).
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PMID:Effect of Plasmodium falciparum malaria infection on the plasma concentration of alpha 1-acid glycoprotein and the binding of quinine in Malawian children. 177 67

A latex card agglutination test for detection of antibodies in human African trypanosomiasis is presented. The latex was covalently coated with semipurified surface glycoprotein of Variable Antigen Type LiTat 1.6 of Trypanosoma brucei gambiense. Sera from 100 patients infected with T.b. gambiense, 26 patients infected with T.b. rhodesiense and 707 individuals without trypanosomiasis, including 132 malaria seropositives, have been tested. At serum dilution 1:16, sensitivity of the test was 91% for the T.b. gambiense and 42.3% for the T.b. rhodesiense group. Specificity was over 99%. The reagent remained stable at +/- 6 degrees C for at least 3 months. Reagent kept at 37 degrees C for 3 months retained its sensitivity and showed a slight decrease in specificity.
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PMID:An experimental latex agglutination test for antibody detection in human African trypanosomiasis. 178 2

Antibody responses to the glycoprotein precursor of the major merozoite surface antigens of Plasmodium falciparum (gp195) were investigated in acutely infected Thai adults. Specific IgG antibody was assayed by enzyme-linked immunosorbent assay using a recombinant fragment derived from the N-terminal region of gp195 as the capture antigen. Two control groups were found to be without significant cross-reacting antibody. Among occupationally exposed soldiers, 84 of 85 men developed positive antibody responses during acute falciparum malaria. Mean antibody levels began to increase at the time of diagnosis, peaking, often at high titers, within two weeks, and then decreased with an initial serum half-life of less than one month. The high frequency of gp195 antibody responses underscores a potential role in serodiagnosis, whereas the dynamic nature of the response suggests that a rigorous schedule of prospective serum sampling will be required to accurately assess the relationship between these antibodies and protection.
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PMID:Characterization of naturally acquired antibody responses to a recombinant fragment from the N-terminus of Plasmodium falciparum glycoprotein 195. 195 65

To determine whether isolates of Plasmodium falciparum have intrinsically different cytoadherent properties and whether these differences contribute to the clinical severity of human falciparum malaria, we studied the cytoadherence to C32 melanoma cells in vitro of 59 parasite isolates from patients with naturally acquired infections in Thailand. Parasitized erythrocytes adhere to these melanoma cells principally via the glycoprotein CD36, which is also expressed on most vascular endothelium. In vitro cytoadherence was significantly greater for isolates from patients with biochemical evidence of severe malaria. The cytoadherent properties of P. falciparum parasites may thus be a virulence factor in human falciparum malaria. However, there was no correlation between the degree of in vitro cytoadherence and cerebral symptoms, which suggests that other receptors and/or host factors may be important in the adherence of malaria parasites to cerebral vascular endothelium. The cytokines tumor necrosis factor, interleukin-1, and gamma interferon, which have been implicated in the pathogenesis of cerebral malaria and are known to promote intercellular adhesion in other systems, did not enhance the cytoadherence of P. falciparum isolates to C32 melanoma cells.
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PMID:Clinical correlates of in vitro Plasmodium falciparum cytoadherence. 199 37

Thrombospondin (TS) is a modular adhesive glycoprotein that contains three domains previously implicated in the attachment of cells to TS. These include the amino-terminal heparin-binding domain, the carboxy terminal cell or platelet-binding domain, and an RGDA sequence of TS. We have characterized a mAb against human TS, designated A4.1, which inhibits the attachment of human melanoma cells (G361) to TS. The epitope for A4.1 lies within the amino terminal half of the central stalklike region of TS which is distinct from the three known cell attachment sites. This region of TS is recovered in a 50-kD peptide after chymotryptic digestion of TS in EDTA. It contains the procollagen-like domain of TS as well as three type I repeats of a 60-residue segment homologous to two malarial proteins and the complement proteins properdin, and factors C6 through C9. The purified chymotryptic fragment is an effective attachment factor for G361 cells. A4.1 blocks adhesion to the 50-kD domain, as do some sulfated glycoconjugates. RGD (and RGE) peptides and mAbs against other domains of TS are not inhibitory. Peptides (19 mers) based on the core homology sequence of the three type I repeats of TS are potent attachment factors for these cells, and this adhesion is also inhibited by sulfated glycoconjugates. A polyclonal antibody raised against one of these peptides inhibits adhesion of G361 cells to the peptides, to the 50-kD fragment and to intact TS. Thus a new cell-adhesion site has been identified in TS whose sequence is very similar to the site identified in region II of the circumsporozoite protein of malaria parasites (Rich, K. A., F. W. George IV, J. L. Law, and W. J. Martin. 1990. Science (Wash. DC) 249:1574-1577. Thus there may be a common receptor which binds TS, malarial proteins, and properdin.
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PMID:The properdin-like type I repeats of human thrombospondin contain a cell attachment site. 199 54

Analysis of the blood serum of healthy and infected with malaria plasmodium mice showed a steep rise in content of linear double-stranded DNA (0.2-0.5 and 2-15 gamma/ml, respectively). Some physico-chemical properties of serum DNA and a DNA-associated glycoprotein (M approximately 40 kDa) are determined.
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PMID:[The nucleoprotein fraction of mouse serum in normal and pathological processes]. 206 23

Chloroquine remains the most commonly antimalaric drug utilized all around the world (340 t in 1988). Its efficiency is linked to its action on the digestive vacuole of plasmodium. Since 1957, the areas of resistance are spreading over of an alarming way, striking all continents. 3,000 cases of malaria are imported in France each year, and 90% of the strains tested in vitro by incorporating tritium hypoxanthine are resistant to chloroquine. The resistant parasites are able to exclude chloroquine from their cytoplasm and produce in great number two genes to synthetize a glycoprotein, probable agent of cellular exclusion of the antimalaric drug. Despite of it, to prescribe chloroquine in prophylaxis remains indispensable, because the risk of severe malaria due to some sensitive strains of Plasmodium falciparum.
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PMID:[Malaria: chloroquine resistance]. 207 46

The safety and kinetics of intramuscular quinine (10 mg salt/kg every 8 h for 3 doses) were assessed in Malawian children suffering from uncomplicated falciparum malaria, who were unable to take oral antimalarial drugs. Treatment was completed with oral pyrimethamine-sulfadoxine. The mean (+/- SD) peak plasma quinine concentration after the first injection was 9.0 (+/- 2.3) micrograms/ml, at 1.1 (+/- 0.7) h. Mean plasma concentrations increased further after the second and third doses to a maximum of 11.5 (+/- 2.6) micrograms/ml at 16.1 (+/- 3.2) h. No hypotension, hypoglycaemia or electrocardiographic abnormalities developed during quinine treatment. These results provide further evidence for the safety of intramuscular quinine in children with moderately severe malaria. Plasma concentrations of alpha 1-acid glycoprotein (AGP) were higher, and the degree of protein binding of quinine was greater, in acute malaria than in convalescence. There was a significant correlation between AGP concentration and the fraction of plasma quinine bound to plasma protein. These findings suggest a role for AGP in the binding of quinine in plasma in vivo and are of interest since unbound quinine is responsible for both the efficacy and toxicity of the drug.
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PMID:The safety and kinetics of intramuscular quinine in Malawian children with moderately severe falciparum malaria. 209 33

T lymphocyte clones (TLC) specific for P. falciparum gp200 (a glycoprotein precursor of the main merozoite surface component) were obtained from two individuals with past exposure to malaria. The 25 established TLC carried the CD4 antigen and proliferated in the presence of immunopurified gp200, crude lysate of the parasite and intact infected red blood cells. They were further tested in proliferation assays for their capacity to recognize the structural diversity displayed by gp200. The stimulating antigen used in these assays was either sonicated or viable preparations of schizonts from five P. falciparum isolates differing in their gp200. The majority of the TLC proliferated similarly in the presence of each of the isolates. One third of the TLC proliferated to a different extent depending on the isolate used for stimulation, while two clones gave isolate-specific responses. These results indicate that the majority of human TLC raised in vitro against gp200, is directed against common determinants. This also suggests that immunization with full length gp200 will not lead predominantly to T cell help restricted to isolate-specific determinant.
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PMID:Structural diversity of Plasmodium falciparum gp200 is detected by T cells. 220 87

To clarify the distribution of the antimalarial primaquine in human blood, we measured the drug separately in the liquid, cellular, and ultrafiltrate phases. Washed red cells resuspended at a hematocrit of 0.4 were exposed to a submaximal therapeutic level of 250 ng/ml of carbon 14-labeled primaquine. The tracer was recovered quantitatively in separated plasma and red cells. Over 75% of the total labeled drug was found in red cells suspended in saline solution, but only 10% to 30% in red cells suspended in plasma. The plasma effect was not mediated by albumin. Studies with alpha 1-acid glycoprotein (AGP), tris(2-butoxyethyl)phosphate, an agent that displaces AGP-bound drugs, and cord blood known to have decreased AGP established that primaquine binds to physiologic amounts of the glycoprotein in plasma. Red cell primaquine concentration increased linearly as AGP level fell and as the free drug fraction rose. We suggest that clinical blood levels of primaquine include the red cell fraction or whole blood level because (1) erythrocytic primaquine is a sizable and highly variable component of the total drug in blood; (2) this component reflects directly the free drug in plasma, and inversely the extent of binding to AGP; (3) the amount of free primaquine may influence drug transport into specific tissues in vivo; and (4) fluctuations of AGP, an acute-phase reactant that increases greatly in patients with malaria and other infections, markedly affect the partition of primaquine in blood. Because AGP binds many basic drugs, unrecognized primaquine-drug interactions may exist.
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PMID:Distribution of primaquine in human blood: drug-binding to alpha 1-glycoprotein. 224 61


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