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Ruy Pérez-tamayo - One of the best experts on this subject based on the ideXlab platform.

  • Pathogenesis of acute experimental Liver Amebiasis.
    Archives of medical research, 2006
    Co-Authors: Ruy Pérez-tamayo, Irmgard Montfort, Alfonso García, Espiridión Ramos, Carlos Barba Ostria
    Abstract:

    Classical descriptions of the pathology of Amebiasis portray the parasite as the cause of tissue damage and destruction, and in recent years a number of amebic molecules have been identified as virulence factors. In this review we describe a series of experiments that suggest a more complex host–parasite relation, at least during the early stages of acute experimental amebic Liver abscess in hamsters. The problems of extrapolating experiments in vitro to explain observations in vivo are discussed. The role of amebic cysteine proteases is examined and evidence presented to suggest that they are primarily related not to tissue damage but to amebic survival, which is required for the progression of the lesion. Inflammation is shown to be not only the major cause of tissue damage but also an absolute requirement for amebic survival in the Liver, whereas complement and ischemia are not involved in the disappearance of the parasite in the absence of inflammation.

  • Amebic cysteine proteinase 2 (EhCP2) plays either a minor or no role in tissue damage in acute experimental amebic Liver abscess in hamsters
    Parasitology Research, 2003
    Co-Authors: Alfonso Olivos-garcía, Irmgard Montfort, Augusto González-canto, Rosario López-vancell, Maria Del Carmen García León, Eusebio Tello, Mario Nequiz-avendaño, Ruy Pérez-tamayo
    Abstract:

    Amebic cysteine protease 2 (EhCP2) was purified from ethyl ether extracts of axenically grown trophozoites of Entamoeba histolytica strain HM1-IMSS. The purification procedure involved molecular filtration and electroelution. Sequence analysis of the purified product revealed EhCP2 and ubiquitin(s). Electrophoretic migration patterns, isoelectric point determination and Western blot studies failed to reveal other EhCP molecules. Polyclonal antibodies against the purified EhCP2 prepared in rabbits either stabilized or enhanced the enzyme activity in a dose-response manner. Purified EhCP2 was enclosed within inert resin microspheres (22–44 μm in diameter) and injected into the portal vein of normal hamsters. In the Liver, the microspheres caused mild acute inflammation and occasional minimal necrosis of short duration. Sections of the Liver were immunohistochemically stained with the anti-EhCP2 antibody and the microspheres were positive for only a very short period (1 h) after injection. Sections of experimental acute (1 day, 5 days) amebic Liver abscess produced in hamsters were also stained with the anti-EhCP2 antibody; and amebas were intensely positive but no staining was observed at any time in the surrounding necrotic structures. It is suggested that EhCP2 plays either a minor or no role in the causation of tissue damage in experimental acute Liver Amebiasis.

  • Amebic cysteine proteinase 2 (EhCP2) plays either a minor or no role in tissue damage in acute experimental amebic Liver abscess in hamsters.
    Parasitology research, 2003
    Co-Authors: Alfonso Olivos-garcía, Irmgard Montfort, Augusto González-canto, Rosario López-vancell, Eusebio Tello, Mario Nequiz-avendaño, Maria Del Carmen Garcia De Leon, Ruy Pérez-tamayo
    Abstract:

    Amebic cysteine protease 2 (EhCP2) was purified from ethyl ether extracts of axenically grown trophozoites of Entamoeba histolytica strain HM1-IMSS. The purification procedure involved molecular filtration and electroelution. Sequence analysis of the purified product revealed EhCP2 and ubiquitin(s). Electrophoretic migration patterns, isoelectric point determination and Western blot studies failed to reveal other EhCP molecules. Polyclonal antibodies against the purified EhCP2 prepared in rabbits either stabilized or enhanced the enzyme activity in a dose-response manner. Purified EhCP2 was enclosed within inert resin microspheres (22–44 μm in diameter) and injected into the portal vein of normal hamsters. In the Liver, the microspheres caused mild acute inflammation and occasional minimal necrosis of short duration. Sections of the Liver were immunohistochemically stained with the anti-EhCP2 antibody and the microspheres were positive for only a very short period (1 h) after injection. Sections of experimental acute (1 day, 5 days) amebic Liver abscess produced in hamsters were also stained with the anti-EhCP2 antibody; and amebas were intensely positive but no staining was observed at any time in the surrounding necrotic structures. It is suggested that EhCP2 plays either a minor or no role in the causation of tissue damage in experimental acute Liver Amebiasis.

Irmgard Montfort - One of the best experts on this subject based on the ideXlab platform.

  • Pathogenesis of acute experimental Liver Amebiasis.
    Archives of medical research, 2006
    Co-Authors: Ruy Pérez-tamayo, Irmgard Montfort, Alfonso García, Espiridión Ramos, Carlos Barba Ostria
    Abstract:

    Classical descriptions of the pathology of Amebiasis portray the parasite as the cause of tissue damage and destruction, and in recent years a number of amebic molecules have been identified as virulence factors. In this review we describe a series of experiments that suggest a more complex host–parasite relation, at least during the early stages of acute experimental amebic Liver abscess in hamsters. The problems of extrapolating experiments in vitro to explain observations in vivo are discussed. The role of amebic cysteine proteases is examined and evidence presented to suggest that they are primarily related not to tissue damage but to amebic survival, which is required for the progression of the lesion. Inflammation is shown to be not only the major cause of tissue damage but also an absolute requirement for amebic survival in the Liver, whereas complement and ischemia are not involved in the disappearance of the parasite in the absence of inflammation.

  • Amebic cysteine proteinase 2 (EhCP2) plays either a minor or no role in tissue damage in acute experimental amebic Liver abscess in hamsters
    Parasitology Research, 2003
    Co-Authors: Alfonso Olivos-garcía, Irmgard Montfort, Augusto González-canto, Rosario López-vancell, Maria Del Carmen García León, Eusebio Tello, Mario Nequiz-avendaño, Ruy Pérez-tamayo
    Abstract:

    Amebic cysteine protease 2 (EhCP2) was purified from ethyl ether extracts of axenically grown trophozoites of Entamoeba histolytica strain HM1-IMSS. The purification procedure involved molecular filtration and electroelution. Sequence analysis of the purified product revealed EhCP2 and ubiquitin(s). Electrophoretic migration patterns, isoelectric point determination and Western blot studies failed to reveal other EhCP molecules. Polyclonal antibodies against the purified EhCP2 prepared in rabbits either stabilized or enhanced the enzyme activity in a dose-response manner. Purified EhCP2 was enclosed within inert resin microspheres (22–44 μm in diameter) and injected into the portal vein of normal hamsters. In the Liver, the microspheres caused mild acute inflammation and occasional minimal necrosis of short duration. Sections of the Liver were immunohistochemically stained with the anti-EhCP2 antibody and the microspheres were positive for only a very short period (1 h) after injection. Sections of experimental acute (1 day, 5 days) amebic Liver abscess produced in hamsters were also stained with the anti-EhCP2 antibody; and amebas were intensely positive but no staining was observed at any time in the surrounding necrotic structures. It is suggested that EhCP2 plays either a minor or no role in the causation of tissue damage in experimental acute Liver Amebiasis.

  • Amebic cysteine proteinase 2 (EhCP2) plays either a minor or no role in tissue damage in acute experimental amebic Liver abscess in hamsters.
    Parasitology research, 2003
    Co-Authors: Alfonso Olivos-garcía, Irmgard Montfort, Augusto González-canto, Rosario López-vancell, Eusebio Tello, Mario Nequiz-avendaño, Maria Del Carmen Garcia De Leon, Ruy Pérez-tamayo
    Abstract:

    Amebic cysteine protease 2 (EhCP2) was purified from ethyl ether extracts of axenically grown trophozoites of Entamoeba histolytica strain HM1-IMSS. The purification procedure involved molecular filtration and electroelution. Sequence analysis of the purified product revealed EhCP2 and ubiquitin(s). Electrophoretic migration patterns, isoelectric point determination and Western blot studies failed to reveal other EhCP molecules. Polyclonal antibodies against the purified EhCP2 prepared in rabbits either stabilized or enhanced the enzyme activity in a dose-response manner. Purified EhCP2 was enclosed within inert resin microspheres (22–44 μm in diameter) and injected into the portal vein of normal hamsters. In the Liver, the microspheres caused mild acute inflammation and occasional minimal necrosis of short duration. Sections of the Liver were immunohistochemically stained with the anti-EhCP2 antibody and the microspheres were positive for only a very short period (1 h) after injection. Sections of experimental acute (1 day, 5 days) amebic Liver abscess produced in hamsters were also stained with the anti-EhCP2 antibody; and amebas were intensely positive but no staining was observed at any time in the surrounding necrotic structures. It is suggested that EhCP2 plays either a minor or no role in the causation of tissue damage in experimental acute Liver Amebiasis.

Alfonso Olivos-garcía - One of the best experts on this subject based on the ideXlab platform.

  • Amebic cysteine proteinase 2 (EhCP2) plays either a minor or no role in tissue damage in acute experimental amebic Liver abscess in hamsters
    Parasitology Research, 2003
    Co-Authors: Alfonso Olivos-garcía, Irmgard Montfort, Augusto González-canto, Rosario López-vancell, Maria Del Carmen García León, Eusebio Tello, Mario Nequiz-avendaño, Ruy Pérez-tamayo
    Abstract:

    Amebic cysteine protease 2 (EhCP2) was purified from ethyl ether extracts of axenically grown trophozoites of Entamoeba histolytica strain HM1-IMSS. The purification procedure involved molecular filtration and electroelution. Sequence analysis of the purified product revealed EhCP2 and ubiquitin(s). Electrophoretic migration patterns, isoelectric point determination and Western blot studies failed to reveal other EhCP molecules. Polyclonal antibodies against the purified EhCP2 prepared in rabbits either stabilized or enhanced the enzyme activity in a dose-response manner. Purified EhCP2 was enclosed within inert resin microspheres (22–44 μm in diameter) and injected into the portal vein of normal hamsters. In the Liver, the microspheres caused mild acute inflammation and occasional minimal necrosis of short duration. Sections of the Liver were immunohistochemically stained with the anti-EhCP2 antibody and the microspheres were positive for only a very short period (1 h) after injection. Sections of experimental acute (1 day, 5 days) amebic Liver abscess produced in hamsters were also stained with the anti-EhCP2 antibody; and amebas were intensely positive but no staining was observed at any time in the surrounding necrotic structures. It is suggested that EhCP2 plays either a minor or no role in the causation of tissue damage in experimental acute Liver Amebiasis.

  • Amebic cysteine proteinase 2 (EhCP2) plays either a minor or no role in tissue damage in acute experimental amebic Liver abscess in hamsters.
    Parasitology research, 2003
    Co-Authors: Alfonso Olivos-garcía, Irmgard Montfort, Augusto González-canto, Rosario López-vancell, Eusebio Tello, Mario Nequiz-avendaño, Maria Del Carmen Garcia De Leon, Ruy Pérez-tamayo
    Abstract:

    Amebic cysteine protease 2 (EhCP2) was purified from ethyl ether extracts of axenically grown trophozoites of Entamoeba histolytica strain HM1-IMSS. The purification procedure involved molecular filtration and electroelution. Sequence analysis of the purified product revealed EhCP2 and ubiquitin(s). Electrophoretic migration patterns, isoelectric point determination and Western blot studies failed to reveal other EhCP molecules. Polyclonal antibodies against the purified EhCP2 prepared in rabbits either stabilized or enhanced the enzyme activity in a dose-response manner. Purified EhCP2 was enclosed within inert resin microspheres (22–44 μm in diameter) and injected into the portal vein of normal hamsters. In the Liver, the microspheres caused mild acute inflammation and occasional minimal necrosis of short duration. Sections of the Liver were immunohistochemically stained with the anti-EhCP2 antibody and the microspheres were positive for only a very short period (1 h) after injection. Sections of experimental acute (1 day, 5 days) amebic Liver abscess produced in hamsters were also stained with the anti-EhCP2 antibody; and amebas were intensely positive but no staining was observed at any time in the surrounding necrotic structures. It is suggested that EhCP2 plays either a minor or no role in the causation of tissue damage in experimental acute Liver Amebiasis.

Augusto González-canto - One of the best experts on this subject based on the ideXlab platform.

  • Amebic cysteine proteinase 2 (EhCP2) plays either a minor or no role in tissue damage in acute experimental amebic Liver abscess in hamsters
    Parasitology Research, 2003
    Co-Authors: Alfonso Olivos-garcía, Irmgard Montfort, Augusto González-canto, Rosario López-vancell, Maria Del Carmen García León, Eusebio Tello, Mario Nequiz-avendaño, Ruy Pérez-tamayo
    Abstract:

    Amebic cysteine protease 2 (EhCP2) was purified from ethyl ether extracts of axenically grown trophozoites of Entamoeba histolytica strain HM1-IMSS. The purification procedure involved molecular filtration and electroelution. Sequence analysis of the purified product revealed EhCP2 and ubiquitin(s). Electrophoretic migration patterns, isoelectric point determination and Western blot studies failed to reveal other EhCP molecules. Polyclonal antibodies against the purified EhCP2 prepared in rabbits either stabilized or enhanced the enzyme activity in a dose-response manner. Purified EhCP2 was enclosed within inert resin microspheres (22–44 μm in diameter) and injected into the portal vein of normal hamsters. In the Liver, the microspheres caused mild acute inflammation and occasional minimal necrosis of short duration. Sections of the Liver were immunohistochemically stained with the anti-EhCP2 antibody and the microspheres were positive for only a very short period (1 h) after injection. Sections of experimental acute (1 day, 5 days) amebic Liver abscess produced in hamsters were also stained with the anti-EhCP2 antibody; and amebas were intensely positive but no staining was observed at any time in the surrounding necrotic structures. It is suggested that EhCP2 plays either a minor or no role in the causation of tissue damage in experimental acute Liver Amebiasis.

  • Amebic cysteine proteinase 2 (EhCP2) plays either a minor or no role in tissue damage in acute experimental amebic Liver abscess in hamsters.
    Parasitology research, 2003
    Co-Authors: Alfonso Olivos-garcía, Irmgard Montfort, Augusto González-canto, Rosario López-vancell, Eusebio Tello, Mario Nequiz-avendaño, Maria Del Carmen Garcia De Leon, Ruy Pérez-tamayo
    Abstract:

    Amebic cysteine protease 2 (EhCP2) was purified from ethyl ether extracts of axenically grown trophozoites of Entamoeba histolytica strain HM1-IMSS. The purification procedure involved molecular filtration and electroelution. Sequence analysis of the purified product revealed EhCP2 and ubiquitin(s). Electrophoretic migration patterns, isoelectric point determination and Western blot studies failed to reveal other EhCP molecules. Polyclonal antibodies against the purified EhCP2 prepared in rabbits either stabilized or enhanced the enzyme activity in a dose-response manner. Purified EhCP2 was enclosed within inert resin microspheres (22–44 μm in diameter) and injected into the portal vein of normal hamsters. In the Liver, the microspheres caused mild acute inflammation and occasional minimal necrosis of short duration. Sections of the Liver were immunohistochemically stained with the anti-EhCP2 antibody and the microspheres were positive for only a very short period (1 h) after injection. Sections of experimental acute (1 day, 5 days) amebic Liver abscess produced in hamsters were also stained with the anti-EhCP2 antibody; and amebas were intensely positive but no staining was observed at any time in the surrounding necrotic structures. It is suggested that EhCP2 plays either a minor or no role in the causation of tissue damage in experimental acute Liver Amebiasis.

Rosario López-vancell - One of the best experts on this subject based on the ideXlab platform.

  • Amebic cysteine proteinase 2 (EhCP2) plays either a minor or no role in tissue damage in acute experimental amebic Liver abscess in hamsters
    Parasitology Research, 2003
    Co-Authors: Alfonso Olivos-garcía, Irmgard Montfort, Augusto González-canto, Rosario López-vancell, Maria Del Carmen García León, Eusebio Tello, Mario Nequiz-avendaño, Ruy Pérez-tamayo
    Abstract:

    Amebic cysteine protease 2 (EhCP2) was purified from ethyl ether extracts of axenically grown trophozoites of Entamoeba histolytica strain HM1-IMSS. The purification procedure involved molecular filtration and electroelution. Sequence analysis of the purified product revealed EhCP2 and ubiquitin(s). Electrophoretic migration patterns, isoelectric point determination and Western blot studies failed to reveal other EhCP molecules. Polyclonal antibodies against the purified EhCP2 prepared in rabbits either stabilized or enhanced the enzyme activity in a dose-response manner. Purified EhCP2 was enclosed within inert resin microspheres (22–44 μm in diameter) and injected into the portal vein of normal hamsters. In the Liver, the microspheres caused mild acute inflammation and occasional minimal necrosis of short duration. Sections of the Liver were immunohistochemically stained with the anti-EhCP2 antibody and the microspheres were positive for only a very short period (1 h) after injection. Sections of experimental acute (1 day, 5 days) amebic Liver abscess produced in hamsters were also stained with the anti-EhCP2 antibody; and amebas were intensely positive but no staining was observed at any time in the surrounding necrotic structures. It is suggested that EhCP2 plays either a minor or no role in the causation of tissue damage in experimental acute Liver Amebiasis.

  • Amebic cysteine proteinase 2 (EhCP2) plays either a minor or no role in tissue damage in acute experimental amebic Liver abscess in hamsters.
    Parasitology research, 2003
    Co-Authors: Alfonso Olivos-garcía, Irmgard Montfort, Augusto González-canto, Rosario López-vancell, Eusebio Tello, Mario Nequiz-avendaño, Maria Del Carmen Garcia De Leon, Ruy Pérez-tamayo
    Abstract:

    Amebic cysteine protease 2 (EhCP2) was purified from ethyl ether extracts of axenically grown trophozoites of Entamoeba histolytica strain HM1-IMSS. The purification procedure involved molecular filtration and electroelution. Sequence analysis of the purified product revealed EhCP2 and ubiquitin(s). Electrophoretic migration patterns, isoelectric point determination and Western blot studies failed to reveal other EhCP molecules. Polyclonal antibodies against the purified EhCP2 prepared in rabbits either stabilized or enhanced the enzyme activity in a dose-response manner. Purified EhCP2 was enclosed within inert resin microspheres (22–44 μm in diameter) and injected into the portal vein of normal hamsters. In the Liver, the microspheres caused mild acute inflammation and occasional minimal necrosis of short duration. Sections of the Liver were immunohistochemically stained with the anti-EhCP2 antibody and the microspheres were positive for only a very short period (1 h) after injection. Sections of experimental acute (1 day, 5 days) amebic Liver abscess produced in hamsters were also stained with the anti-EhCP2 antibody; and amebas were intensely positive but no staining was observed at any time in the surrounding necrotic structures. It is suggested that EhCP2 plays either a minor or no role in the causation of tissue damage in experimental acute Liver Amebiasis.