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1.
Mem. Inst. Oswaldo Cruz ; 108(6): 679-685, set. 2013. graf
Article in English | LILACS | ID: lil-685490

ABSTRACT

Leishmania parasites expose phosphatidylserine (PS) on their surface, a process that has been associated with regulation of host's immune responses. In this study we demonstrate that PS exposure by metacyclic promastigotes of Leishmania amazonensis favours blood coagulation. L. amazonensis accelerates in vitro coagulation of human plasma. In addition, L. amazonensis supports the assembly of the prothrombinase complex, thus promoting thrombin formation. This process was reversed by annexin V which blocks PS binding sites. During blood meal, Lutzomyia longipalpis sandfly inject saliva in the bite site, which has a series of pharmacologically active compounds that inhibit blood coagulation. Since saliva and parasites are co-injected in the host during natural transmission, we evaluated the anticoagulant properties of sandfly saliva in counteracting the procoagulant activity of L. amazonensis . Lu. longipalpis saliva reverses plasma clotting promoted by promastigotes. It also inhibits thrombin formation by the prothrombinase complex assembled either in phosphatidylcholine (PC)/PS vesicles or in L. amazonensis . Sandfly saliva inhibits factor X activation by the intrinsic tenase complex assembled on PC/PS vesicles and blocks factor Xa catalytic activity. Altogether our results show that metacyclic promastigotes of L. amazonensis are procoagulant due to PS exposure. Notably, this effect is efficiently counteracted by sandfly saliva.


Subject(s)
Animals , Humans , Blood Coagulation/physiology , Leishmania/metabolism , Phosphatidylserines/metabolism , Psychodidae/parasitology , Saliva/metabolism , Anticoagulants/metabolism , Cysteine Endopeptidases , Factor V/antagonists & inhibitors , Factor X/antagonists & inhibitors , Factor Xa/antagonists & inhibitors , Insect Vectors/parasitology , Neoplasm Proteins/antagonists & inhibitors , Partial Thromboplastin Time , Phosphatidylcholines/metabolism , Psychodidae/metabolism , Thrombin/antagonists & inhibitors , Tissue Extracts/metabolism
2.
J Environ Biol ; 2005 Jul; 26(3): 603-8
Article in English | IMSEAR | ID: sea-113950

ABSTRACT

The effect of Kraft black liquor on the lipid peroxidation of rat homogenates was examined. The lipid peroxidation of homogenates from different organs (kidney, brain, lung, and liver) was induced by Fenton's reagent. The products of lipid peroxidation, lipid hydroperoxides and TBARS were measured by FOX method and TBA assay, respectively. It was found that black liquor significantly reduced the concentration of TBARS, but not the concentration of lipid hydroperoxides. This inhibition was directly proportional to the concentration of Kraft black liquor and the incubation temperature. Conclusively, the black liquor from pulp and paper industry exhibited an antioxidant activity.


Subject(s)
Analysis of Variance , Animals , Antioxidants/chemistry , Hydrogen Peroxide , Iron , Lignin/chemistry , Lipid Peroxidation/drug effects , Lipid Peroxides/metabolism , Paper , Rats , Temperature , Thiobarbituric Acid Reactive Substances/metabolism , Tissue Extracts/metabolism , Waste Products
3.
J Environ Biol ; 2005 Jul; 26(3): 567-9
Article in English | IMSEAR | ID: sea-113274

ABSTRACT

Enzymatic and histological change in the testicular cells of rats treated orally and intradermally for 45 days with gibberellic acid (GBA) in independent studies is reported. Assay of hexokinase (HK), acid phosphatase (AcP) and alkaline phosphatase (AkP) in rat testicular tissue homogenate preparations yielded results that suggested changes in these enzyme activities relative to their respective controls. Histological studies showed loss of germ cells, derangement of the germinal cells, and reduction in the size of the seminiferous tubules and dystrophy of Leydig cells. More importantly decreased sperm count in the lumen was observed. A dysregulatory role is thus established for GBA in rat testicular cell function. This compound may serve as an inhibitor of testicular cell function.


Subject(s)
Acid Phosphatase/metabolism , Alkaline Phosphatase/metabolism , Animals , Gibberellins/toxicity , Hexokinase/metabolism , Male , Rats , Spermatogenesis/drug effects , Testis/cytology , Tissue Extracts/metabolism
4.
Yonsei Medical Journal ; : 409-416, 1998.
Article in English | WPRIM | ID: wpr-81590

ABSTRACT

It is widely known that the cockroach is an inhalant allergen in atopic asthma and allergic rhinitis. Even though Bla g I and Bla g II are considered as the major allergens, several relatively high-molecular weight (MW) cockroach allergens have also been recently identified by IgE-immunoblot in western countries. However, the environmental control and diagnostic tests mainly focussed on Bla g I and Bla g II. Furthermore there is no data about major IgE-binding cockroach antigens in Korea. We performed this study to identify the major German cockroach allergens in Korean atopic children. By the results of allergy skin tests, 14 children with atopic asthma (9 were cockroach-sensitive and 5 were cockroach-nonsensitive atopics) were enrolled in this study. We conducted IgE immunoblot and autoradiographic analysis using Yonsei-extract of German cockroach antigen produced in our laboratory, individual sera from 9 cockroach- sensitive children, and the pooled sera of 5 house-dust-mites-only-sensitive children. We performed an allergic skin test to cockroach mix, and a radioallergosorbent test (RAST) using German cockroach crude extract on all subjects. German cockroach-specific IgE was detected in 6 out of 9 subjects by RAST. We identified at least 15 IgE-binding protein bands, and among them, the components of MWs of 76, 64, 50, 38, and <14 kilodaltons (kDa) were the major German cockroach allergens in study subjects. Therefore, Bla g I (25-30 kDa) and Bla g II (36 kDa) could not be the absolute indicators of German cockroach sensitization and parameters of environmental control.


Subject(s)
Child , Child, Preschool , Female , Humans , Male , Adolescent , Allergens/analysis , Animals , Asthma/metabolism , Asthma/immunology , Asthma/complications , Cockroaches/immunology , Cockroaches/chemistry , Hypersensitivity/metabolism , Hypersensitivity/immunology , Hypersensitivity/complications , Immunoglobulin E/metabolism , Korea , Tissue Extracts/metabolism
5.
Acta physiol. pharmacol. latinoam ; 39(2): 189-95, 1989. tab
Article in English | LILACS | ID: lil-76794

ABSTRACT

Con el objeto de estudiar el efecto de la adenosina sobre la producción de melatonina, se incubaron durante 6 h explantos de pineales de rata con adenosina o 2-cloroadenosina 10**-4 M en presencia y ausencia de noradrenalina (NE) (5 x 10**-5 M). El contenido de melatonina en las glándulas pineales y en los medios se determinó por RIA. Tanto adenosina como 2-cloroadenosina estimularon la producción de melatonina entre 3 y 4 veces e incrementaron aquella inducida por NE en un 30-40%. El agregado de adenosina deaminasa previo a NE redujo el incremento en la liberación de melatonina inducido por NE en un 40-46%. El tratamiento con 2-cloroadenosina contrarrestó dicho efecto de la enzima. La adenosina y su agonista Al, ciclohexiladenosina (CHA), disminuyeron en un 20-22% la liberación del neurotransmisor-3H inducida por estímulo despolarizante de K+ en pineales de rata preincubadas con 3H-NE. Estos resultados sugieren que la adenosina modula mecanismos pineales pre- y post-sinápticos


Subject(s)
Rats , Animals , Male , Adenosine/metabolism , Melatonin/biosynthesis , Norepinephrine/metabolism , Pineal Gland/metabolism , Adenosine Deaminase/metabolism , Analysis of Variance , Periodicity , Tissue Extracts/metabolism
6.
Rev. paul. med ; 103(4): 176-81, jul.-ago. 1985. ilus, tab
Article in Portuguese | LILACS | ID: lil-2024

ABSTRACT

Acredita-se que o desarranjo metabólico celular existente no bócio simples possa ser conseqüência de um desequilíbrio das açöes do TSH sobre a glândula tiróide. Já que a ligaçäo do TSH ao seu receptor é a primeira etapa na gênese de seus efeitos biológicos a nível da célula alvo, objetivou-se na presente investigaçäo caracterizar a ligagçäo de 125 ITSH ao seu receptor em fragmentos de tiróides humanas de pacientes portadores de nódulo "frio" e anatomopatológico de hiperplasia folicular benigna. Os tecidos foram obtidos no ato cirúrgico e imediatamente armazenados em nitrogênio líquido. Após determinaçäo das condiçöes ótimas de incubaçäo (duraçäo, pH do meio e concentraçäo protéica) e empregando-se a análise de Scatchard, verificou-se näo haver diferenças significativas quanto à capacidade de ligaçäo dos receptores de TSH, quando comparada à do tecido normal paranodular. Por outro lado, observou-se nítida diminuiçäo da constante de dissociaçäo desses receptores, indicando maior afinidade pelo TSH. Sabe-se que o iodo intracelular pode interferir nas açöes do TSH sobre a célula folicular tiroidiana. Supöe-se que isto seja decorrente de um efeito de ligaçäo do TSH ao seu receptor. Devido à sua incapacidade de organificaçäo do iodo, os módulos "frios" apresentam diminuiçäo do conteúdo de iodo intracelular. Assim, acredita-se que as alteraçöes encontradas no presente estudo sejam conseqüência do baixo conteúdo de iodo da célula folicular hiperplásica


Subject(s)
Adult , Humans , Female , Tissue Extracts/metabolism , Thyrotropin/metabolism , Receptors, Cell Surface/metabolism , Iodine Radioisotopes/metabolism , Thyroid Gland/metabolism , Radioligand Assay , Goiter/metabolism , Hyperplasia/metabolism , Thyroid Gland/pathology
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