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  • Open Access

    ABSTRACT

    Autodigestion in Physiological Shock, Organ Dysfunction and Death

    Erik B. Kistler1, Geert W. Schmid-Schönbein2,*

    Molecular & Cellular Biomechanics, Vol.16, Suppl.2, pp. 8-8, 2019, DOI:10.32604/mcb.2019.07256

    Abstract A longstanding question in research on organ failure after physiological shock (such as trauma, burns, sepsis, surgery and medical emergencies) is the underlying mechanism for a progressive loss of cell and tissue functions. Our systematic analysis of this problem has served to identify digestive enzymes as key players [1, 2]. After synthesis and discharge from the pancreas, the digestive enzymes are usually contained inside the lumen of the small intestine where they break down food every day. Escape of the digestive enzymes out of the lumen of the intestine is kept to a minimum by… More >

  • Open Access

    ARTICLE

    Biomechanical Aspects of the Auto-digestion Theory

    Geert W. Schmid-Schönbein*

    Molecular & Cellular Biomechanics, Vol.5, No.2, pp. 83-96, 2008, DOI:10.3970/mcb.2008.005.083

    Abstract Increasing evidence suggests that most cardiovascular diseases, tumors and other ailments are associated with an inflammatory cascade. The inflammation is accompanied by activation of cells in the circulation and fundamental changes in the mechanics of the microcirculation, expression of pro-inflammatory genes and downregulation of anti-inflammatory genes, attachment of leukocytes to the endothelium, elevated permeability of the endothelium, and many other events. The evidence has opened great opportunities for medicine to develop new anti-inflammatory interventions. But it also raises a fundamental question: What is the origin of inflammation? I will discuss a basic series of studies that was… More >

  • Open Access

    ARTICLE

    Cysteine proteinases of Trypanosoma cruzi: from digestive enzymes to programmed cell death mediators

    GREGOR KOSEC, VANINA ALVAREZ**¶, JUAN J. CAZZULO**

    BIOCELL, Vol.30, No.3, pp. 479-490, 2006, DOI:10.32604/biocell.2006.30.479

    Abstract Trypanosoma cruzi, the parasite causing Chagas disease, contains a number of proteolytic enzymes. The recent completion of the genome sequence of the T. cruzi CL Brener clone suggests the presence of 70 cysteine peptidases, 40 serine peptidases (none of them from the chymotrypsin family), about 250 metallopeptidases (most leishmanolysin homologues), 25 threonine peptidases, and only two aspartyl peptidases, none of them from the pepsin family. The cysteine peptidases belong to 7 families of Clan CA, 3 families of Clan CD, and one each of Clans CE and CF. In Clan CA, the C1 family is represented by More >

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