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Mario H Rodriguez – One of the best experts on this subject based on the ideXlab platform.

  • Ecdysis-related pleiotropic neuropeptides expression during Anopheles albimanus development.
    Salud Publica De Mexico, 2017
    Co-Authors: Alejandro Alvarado-delgado, Ken Moran-francia, Guillermo Perales-ortiz, Mario H Rodriguez, Humberto Lanz-mendoza

    Abstract:

    Abstract: Objective: To analyze the transcription pattern of neuropeptides in the ontogeny of a malaria vector, the mosquito Anopheles albimanus. Materials and methods: The transcription pattern of Crustacean CardioActive peptide (CCAP), corazonin, Ecdysis Triggering Hormone (ETH), allatostatin-A, orcokinin, Insulin Like Peptide 2 (ILP2), Insulin Like Peptide 5 (ILP5) and bursicon was evaluated using qPCR on larvae (1st – 4th instar), pupae and adult mosquitoes. Results: Unlike in other insects, transcripts of CCAP (70.8%), ETH (60.2%) and corazonin (76.5%) were expressed in 4th instar larvae, probably because these three neuropeptides are associated with the beginning of ecdysis. The neuropeptide ILP2 showed higher transcription levels in other stages and orcokinin decreased during the development of the mosquito. Conclusion: The CCAP, corazonin and ETH neuropeptides are potential targets for the design of control strategies aimed at disrupting An. albiamnus larval development.

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  • An antibody against an Anopheles albimanus midgut myosin reduces Plasmodium berghei oocyst development
    Parasites & vectors, 2016
    Co-Authors: Alba N. Lecona-valera, Mario H Rodriguez, Rhoel R. Dinglasan, Dingyin Tao, Tomás López, Maria Del Carmen Rodriguez

    Abstract:

    Background
    Malaria parasites are transmitted by Anopheles mosquitoes. Although several studies have identified mosquito midgut surface proteins that are putatively important for Plasmodium ookinete invasion, only a few have characterized these protein targets and demonstrated transmission-blocking activity. Molecular information about these proteins is essential for the development of transmission-blocking vaccines (TBV). The aim of the present study was to test three monoclonal antibodies (mAbs), A-140, A-78 and A-10, for their ability to recognize antigens and block oocyst infection of the midgut of Anopheles albimanus, a major malaria vector in Latin America.

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  • Antimicrobial properties of Anopheles albimanus pericardial cells.
    Cell and tissue research, 2012
    Co-Authors: Salvador Hernández-martínez, Humberto Lanz-mendoza, Jesús Martínez-barnetche, Mario H Rodriguez

    Abstract:

    Insect pericardial cells (PCs) are strategically located along the dorsal vessel where they encounter a high hemolymph flow enabling them to undertake their osmoregulatory, detoxifying, and scavenging functions. In this location, PCs also encounter foreign molecules and microorganisms. The response of PCs of the mosquito Anopheles albimanus, one of the most important Plasmodium vivax vectors in Mexico and Latin America, to Saccharomyces cerevisiae was analyzed by using biochemical, cellular, ultrastructural, and bioinformatics approaches. Immune gene transcripts were identified in the PC transcriptome of A. albimanus. PCs responded to the presence of yeast and zymosan with increased lysosomal and phosphatase activities and produced lytic activity against bacteria. Our results indicate that mosquito PCs play a key role in the neutralization and elimination of pathogens.

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José M. C. Ribeiro – One of the best experts on this subject based on the ideXlab platform.

  • NAD(P)H-dependent production of oxygen reactive species by the salivary glands of the mosquito Anopheles albimanus
    Insect biochemistry and molecular biology, 1996
    Co-Authors: José M. C. Ribeiro

    Abstract:

    Salivary gland homogenates of the adult female mosquito Anopheles albimanus, but not those of Aedes aegypti, induced light production in the presence of NADPH and luminol, indicating a NADPH oxidase activity producing reactive oxygen species (superoxide anion) by the anopheline salivary homogenate. Superoxide production by the anopheline salivary homogenate was also confirmed by the NADPH-dependent, superoxide dismutase inhibitable, reduction of cytochrome c. The NADPH oxidase reaction measured by light production in the presence of luminol was inhibited by superoxide dismutase and catalase. Both NADH and NADPH were substrates for the production of oxygen reactive species by the salivary homogenate. Activity, as measured by luminol-dependent light emission, was enhanced one order of magnitude in the presence of 1.6 mg/ml of either phosphatidylserine or bovine serum albumin. Molecular sieving and hydroxyapatite chromatography of the salivary homogenate showed coelution of the NADPH oxidase activity with the previously reported salivary peroxidase activity. It is suggested that the salivary peroxidase of Anopheles albimanus has the ability of producing superoxide in the presence of NADPH, and this may provide the peroxidase with substrates necessary for peroxidation of vasoconstrictor amines such as serotonin, released by aggregating platelets at the site of mosquito probing and feeding.

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  • the salivary catechol oxidase peroxidase activities of the mosquito Anopheles albimanus
    The Journal of Experimental Biology, 1993
    Co-Authors: José M. C. Ribeiro, Roberto H. Nussenzveig

    Abstract:

    Salivary gland homogenates from adult female Anopheles albimanus mosquitoes relaxed aortic rings preconstricted with noradrenaline (NA). This relaxation is slow and is due to destruction of NA. Incubation of NA with the homogenate yielded a product with a spectrum consistent with the corresponding adrenochrome. Oxidation of NA was enhanced by a superoxide generation system and inhibited by the combined action of superoxide dismutase and catalase. Additionally, peroxidase activity on both synthetic (o-dianisidine) and biologically active (serotonin) substrates was also present in the salivary gland homogenates, this latter activity requiring hydrogen peroxide. Noradrenaline oxidation, serotonin and o-dianisidine peroxidation and vasodilation all co-elute with a heme protein of relative molecular mass 50,000, as determined by molecular sieving chromatography. Peroxidase activity was localized in the posterior (female-specific) lobes of salivary glands and was also detected in nitrocellulose membranes probed by hungry mosquitoes. Protein and peroxidase activities were significantly lower in salivary glands of mosquitoes after probing and feeding on blood. It is suggested that adult female Anopheles albimanus mosquitoes contain a salivary heme peroxidase that functions during blood finding and blood feeding by destroying hemostatically active biogenic amines released by the vertebrate host during tissue destruction.

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  • The salivary catechol oxidase/peroxidase activities of the mosquito Anopheles albimanus
    The Journal of experimental biology, 1993
    Co-Authors: José M. C. Ribeiro, Roberto H. Nussenzveig

    Abstract:

    Salivary gland homogenates from adult female Anopheles albimanus mosquitoes relaxed aortic rings preconstricted with noradrenaline (NA). This relaxation is slow and is due to destruction of NA. Incubation of NA with the homogenate yielded a product with a spectrum consistent with the corresponding adrenochrome. Oxidation of NA was enhanced by a superoxide generation system and inhibited by the combined action of superoxide dismutase and catalase. Additionally, peroxidase activity on both synthetic (o-dianisidine) and biologically active (serotonin) substrates was also present in the salivary gland homogenates, this latter activity requiring hydrogen peroxide. Noradrenaline oxidation, serotonin and o-dianisidine peroxidation and vasodilation all co-elute with a heme protein of relative molecular mass 50,000, as determined by molecular sieving chromatography. Peroxidase activity was localized in the posterior (female-specific) lobes of salivary glands and was also detected in nitrocellulose membranes probed by hungry mosquitoes. Protein and peroxidase activities were significantly lower in salivary glands of mosquitoes after probing and feeding on blood. It is suggested that adult female Anopheles albimanus mosquitoes contain a salivary heme peroxidase that functions during blood finding and blood feeding by destroying hemostatically active biogenic amines released by the vertebrate host during tissue destruction.

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Roberto H. Nussenzveig – One of the best experts on this subject based on the ideXlab platform.

  • the salivary catechol oxidase peroxidase activities of the mosquito Anopheles albimanus
    The Journal of Experimental Biology, 1993
    Co-Authors: José M. C. Ribeiro, Roberto H. Nussenzveig

    Abstract:

    Salivary gland homogenates from adult female Anopheles albimanus mosquitoes relaxed aortic rings preconstricted with noradrenaline (NA). This relaxation is slow and is due to destruction of NA. Incubation of NA with the homogenate yielded a product with a spectrum consistent with the corresponding adrenochrome. Oxidation of NA was enhanced by a superoxide generation system and inhibited by the combined action of superoxide dismutase and catalase. Additionally, peroxidase activity on both synthetic (o-dianisidine) and biologically active (serotonin) substrates was also present in the salivary gland homogenates, this latter activity requiring hydrogen peroxide. Noradrenaline oxidation, serotonin and o-dianisidine peroxidation and vasodilation all co-elute with a heme protein of relative molecular mass 50,000, as determined by molecular sieving chromatography. Peroxidase activity was localized in the posterior (female-specific) lobes of salivary glands and was also detected in nitrocellulose membranes probed by hungry mosquitoes. Protein and peroxidase activities were significantly lower in salivary glands of mosquitoes after probing and feeding on blood. It is suggested that adult female Anopheles albimanus mosquitoes contain a salivary heme peroxidase that functions during blood finding and blood feeding by destroying hemostatically active biogenic amines released by the vertebrate host during tissue destruction.

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  • The salivary catechol oxidase/peroxidase activities of the mosquito Anopheles albimanus
    The Journal of experimental biology, 1993
    Co-Authors: José M. C. Ribeiro, Roberto H. Nussenzveig

    Abstract:

    Salivary gland homogenates from adult female Anopheles albimanus mosquitoes relaxed aortic rings preconstricted with noradrenaline (NA). This relaxation is slow and is due to destruction of NA. Incubation of NA with the homogenate yielded a product with a spectrum consistent with the corresponding adrenochrome. Oxidation of NA was enhanced by a superoxide generation system and inhibited by the combined action of superoxide dismutase and catalase. Additionally, peroxidase activity on both synthetic (o-dianisidine) and biologically active (serotonin) substrates was also present in the salivary gland homogenates, this latter activity requiring hydrogen peroxide. Noradrenaline oxidation, serotonin and o-dianisidine peroxidation and vasodilation all co-elute with a heme protein of relative molecular mass 50,000, as determined by molecular sieving chromatography. Peroxidase activity was localized in the posterior (female-specific) lobes of salivary glands and was also detected in nitrocellulose membranes probed by hungry mosquitoes. Protein and peroxidase activities were significantly lower in salivary glands of mosquitoes after probing and feeding on blood. It is suggested that adult female Anopheles albimanus mosquitoes contain a salivary heme peroxidase that functions during blood finding and blood feeding by destroying hemostatically active biogenic amines released by the vertebrate host during tissue destruction.

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