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  • 1
    Online Resource
    Online Resource
    The fibrinogenolytic activity of purified tryptase from human lung mast cells.
    The American Association of Immunologists ; 1985
    In:  The Journal of Immunology Vol. 135, No. 4 ( 1985-10-01), p. 2762-2767
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 135, No. 4 ( 1985-10-01), p. 2762-2767
    Abstract: The capacity of purified tryptase from human lung mast cells to metabolize human fibrinogen, fibrin, and plasminogen was evaluated. Tryptase (5 micrograms/ml) inactivated the thrombin-induced clotting activity of fibrinogen (100 micrograms/ml) with essentially similar t 1/2 values of 4.6 min in the absence of heparin and 5.8 min in the presence of heparin (20 micrograms/ml) that were not appreciably different than with lysine-Sepharose-purified plasmin (5 micrograms/ml). Fibrinogen treated with tryptase together with heparin lost all detectable clotting activity by 4 hr at 37 degrees C, whereas fibrinogen treated with tryptase alone resulted in destruction of only 80% of fibrinogen clotting equivalents after 16 hr. Tryptase alone was observed to cleave only the alpha-chains of fibrinogen by electrophoresis of tryptase-treated, denatured, and reduced fibrinogen in polyacrylamide gradient gels. Tryptase together with heparin cleaved first the alpha-chain and then the beta-chain, the latter cleavage corresponding to complete loss of fibrinogen clotting activity by 4 hr. No fibrinogen fragments with anticoagulant activity were generated by tryptase. In contrast, plasmin left no residual clotting activity after 4 hr of incubation and generated fibrinogen fragments with anticoagulant activity. Plasmin sequentially cleaved the alpha, beta, and gamma subunits of fibrinogen. Tryptase alone (6 micrograms/ml) or together with heparin (20 micrograms/ml) failed to activate plasminogen (0.6 mg/ml) after a 60-min incubation at 37 degrees C. Addition of urokinase to tryptase-treated or untreated plasminogen resulted in essentially identical plasmin activities (0.32 and 0.34 U/ml, respectively), indicating that tryptase neither activates nor destroys plasminogen. Tryptase (700 ng) also failed to substantially solubilize cross-linked fibrin (2.6 micrograms) or the corresponding amount of fibrinogen bound to plastic microtiter plates with or without heparin. The failure to solubilize fibrinogen and, possibly, fibrin is consistent with the observation that the apparent m.w. by SDS polyacrylamide gel electrophoresis of unreduced fibrinogen is not appreciably altered by prior treatment with tryptase, even though cleavage of alpha-and beta-chains is revealed after reduction. Fibrinogenolysis by tryptase complements other mast cell mediators with anticoagulant properties such as heparin and suggests a significant prevention of coagulation by activated mast cells.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.135.4.2762
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 1985
    detail.hit.zdb_id: 1475085-5
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  • 2
    Online Resource
    Online Resource
    Inhibition of catalase-dependent ethanol metabolism in alcohol dehydrogenase-deficient deermice by fructose
    Portland Press Ltd. ; 1987
    In:  Biochemical Journal Vol. 248, No. 2 ( 1987-12-01), p. 415-421
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 248, No. 2 ( 1987-12-01), p. 415-421
    Abstract: Hepatic microsomal fractions from ADH (alcohol dehydrogenase)-negative deermice incubated with an NADPH-generating system metabolized butanol and ethanol at rates around 10 nmol/min per mg. In contrast, cytosolic catalase from ADH-negative deermouse liver oxidized ethanol, but not butanol, when incubated with an H2O2-generating system. Thus butanol is oxidized by cytochrome P-450 in microsomal fractions, but not by cytosolic catalase, in tissues from ADH-negative deermice. In perfused livers from ADH-negative deermice, rates of ethanol uptake at low concentrations of ethanol (1.5 mM) were about 60 mumol/h per g, yet butanol (1.5 mM) uptake was undetectable (less than 4 mumol/h per g). At higher concentrations of alcohol (25-30 mM), rates of ethanol uptake were about 80 mumol/h per g, whereas rates of butanol uptake were only about 9 mumol/h per g. Because rates of butanol metabolism via cytochrome P-450 in deermice were more than an order of magnitude lower than rates of ethanol uptake in livers from ADH-negative deermice, it is concluded that ethanol uptake by perfused livers from ADH-negative deermice is catalysed predominantly via catalase-H2O2. In support of this conclusion, rates of H2O2 generation, which are rate-limiting for the peroxidation of ethanol by catalase, were about 65 mumol/h per g in livers from ADH-negative deermice, values similar to rates of ethanol uptake of about 60 mumol/h per g measured under identical conditions. Rates of ethanol uptake by perfused livers from ADH-positive, but not from ADH-negative, deermice were increased by about 50% by infusion of fructose. Thus it is concluded that the stimulation of hepatic ethanol uptake by fructose is dependent on the presence of ADH. Unexpectedly, fructose decreased rates of ethanol metabolism and H2O2 generation by about 60% in perfused livers from ADH-negative deermice, probably by decreasing activation of fatty acids and thus diminishing rates of peroxisomal beta-oxidation.
    Type of Medium: Online Resource
    ISSN: 0264-6021 , 1470-8728
    URL: Article
    DOI: 10.1042/bj2480415
    RVK:
    WA 15000
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 1987
    detail.hit.zdb_id: 1473095-9
    SSG: 12
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  • 3
    Online Resource
    Online Resource
    INCREASED LIVER INJURY IN FEMALE RATS IS DUE TO HYPOXIA-REOXYGENATION TRIGGERED BY ENDOTOXIN AND KUPFFER CELLS
    Wiley ; 1998
    In:  Alcoholism: Clinical and Experimental Research Vol. 22, No. 3 ( 1998-05), p. 766-768
    Details
    In: Alcoholism: Clinical and Experimental Research, Wiley, Vol. 22, No. 3 ( 1998-05), p. 766-768
    Type of Medium: Online Resource
    ISSN: 0145-6008 , 1530-0277
    URL: Issue
    URL: Article
    DOI: 10.1111/acer.1998.22.issue-3
    DOI: 10.1111/j.1530-0277.1998.tb04341.x
    Language: English
    Publisher: Wiley
    Publication Date: 1998
    detail.hit.zdb_id: 2046886-6
    detail.hit.zdb_id: 3167872-5
    SSG: 15,3
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  • 4
    Online Resource
    Online Resource
    Human mast cell carboxypeptidase. Selective localization to MCTC cells.
    The American Association of Immunologists ; 1991
    In:  The Journal of Immunology Vol. 147, No. 1 ( 1991-07-01), p. 247-253
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 147, No. 1 ( 1991-07-01), p. 247-253
    Abstract: Two murine mAb were prepared against human mast cell carboxypeptidase (HMC-CP) purified from human skin, and were termed CP1 and CP2, respectively. Double immunohistochemical labeling of Carnoy's-fixed sections of human skin, lung, and gastrointestinal tissue with CP1 and CP2, respectively, and with a murine monoclonal antitryptase antibody demonstrated that HMC-CP was selectively present in a subset of human mast cells. Double labeling experiments with CP1 and CP2, respectively, and a murine anti-chymase mAb demonstrated the presence of HMC-CP in the tryptase-positive, chymase-positive mast cell type (MCTC) only. Immunohistochemical labeling of peripheral blood leukocytes resulted in staining of monocytes with CP2 but not with CP1. In addition to chymase and a cathepsin-G like proteinase, HMC-CP is another neutral protease that is selectively present in the MCTC tryptase-positive, chymase-positive mast cells type of mast cell, thus extending the biochemical definition of human mast cell heterogeneity.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.147.1.247
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 1991
    detail.hit.zdb_id: 1475085-5
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  • 5
    Online Resource
    Online Resource
    LIPOPOLYSACCHARIDE-BINDING PROTEIN MODULATES HEPATIC DAMAGE AND INFLAMMATORY RESPONSE AFTER HEMORRHAGIC SHOCK AND RESUSCITATION. : 81
    Ovid Technologies (Wolters Kluwer Health) ; 2003
    In:  Shock Vol. 19, No. Supplement ( 2003-06), p. 28-
    Details
    In: Shock, Ovid Technologies (Wolters Kluwer Health), Vol. 19, No. Supplement ( 2003-06), p. 28-
    Type of Medium: Online Resource
    ISSN: 1073-2322
    URL: Article
    DOI: 10.1097/00024382-200306001-00081
    Language: English
    Publisher: Ovid Technologies (Wolters Kluwer Health)
    Publication Date: 2003
    detail.hit.zdb_id: 2011863-6
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  • 6
    Online Resource
    Online Resource
    Role of Kupffer cells in the pathogenesis of hepatic reperfusion injury
    American Physiological Society ; 1994
    In:  American Journal of Physiology-Gastrointestinal and Liver Physiology Vol. 267, No. 4 ( 1994-10-01), p. G630-G636
    Details
    In: American Journal of Physiology-Gastrointestinal and Liver Physiology, American Physiological Society, Vol. 267, No. 4 ( 1994-10-01), p. G630-G636
    Abstract: The purpose of this study was to evaluate the role of Kupffer cell activation in the pathogenesis of reperfusion injury. In a blood-free liver perfusion model, pericentral hypoxia and reperfusion injury occurred. Lactate dehydrogenase (LDH) and malondialdehyde (MDA) release, oxygen uptake, and trypan blue staining were assessed. Within the first 10 min of reflow, LDH and MDA release reached maximal values of 44 U.g-1.h-1 and 115 nmol.g-1.h-1, respectively. Trypan blue cell staining was confined to pericentral regions of the liver lobule. When Kupffer cells were inactivated with GdCl3, release of enzymes and MDA was reduced significantly by 〉 50%, and hepatic cell death was almost completely absent. Since increases in MDA suggested involvement of free radicals, livers were perfused with phenyl N-t-butylnitrone (5 mM), a spin-trapping agent. Analysis of liver tissue by electron paramagnetic resonance spectroscopy revealed a typical six-line spectrum, providing direct evidence that carbon-centered radicals were generated on reflow. GdCl3 treatment decreased radical adduct formation by approximately 50%. Collectively, these results strongly support the hypothesis that activation of Kupffer cells plays an important role in the pathogenesis of hepatic reperfusion injury.
    Type of Medium: Online Resource
    ISSN: 0193-1857 , 1522-1547
    URL: Article
    DOI: 10.1152/ajpgi.1994.267.4.G630
    Language: English
    Publisher: American Physiological Society
    Publication Date: 1994
    detail.hit.zdb_id: 1477329-6
    SSG: 12
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  • 7
    Online Resource
    Online Resource
    Nimodipine, a dihydropyridine-type calcium channel blocker, prevents alcoholic hepatitis caused by chronic intragastric ethanol exposure in the rat
    Ovid Technologies (Wolters Kluwer Health) ; 1996
    In:  Hepatology Vol. 24, No. 2 ( 1996-08), p. 391-397
    Details
    In: Hepatology, Ovid Technologies (Wolters Kluwer Health), Vol. 24, No. 2 ( 1996-08), p. 391-397
    Type of Medium: Online Resource
    ISSN: 0270-9139 , 1527-3350
    URL: Issue
    URL: Journal
    URL: Article
    DOI: 10.1002/hep.v24:2
    DOI: 10.1002/(ISSN)1527-3350
    DOI: 10.1002/hep.510240217
    Language: English
    Publisher: Ovid Technologies (Wolters Kluwer Health)
    Publication Date: 1996
    detail.hit.zdb_id: 1472120-X
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  • 8
    Online Resource
    Online Resource
    How Is the Liver Primed or Sensitized for Alcoholic Liver Disease?
    Wiley ; 2001
    In:  Alcoholism: Clinical and Experimental Research Vol. 25, No. s1 ( 2001-05)
    Details
    In: Alcoholism: Clinical and Experimental Research, Wiley, Vol. 25, No. s1 ( 2001-05)
    Abstract: This article represents the proceedings of a symposium at the 2000 ISBRA Meeting in Yokohama, Japan. The chairs were Hidekazu Tsukamoto and Yoshiyuki Takei. The presentations were (1) Tribute to Professor Rajendar K. Chawla, by Craig J. McClain; (2) Dysregulated TNF signaling in alcoholic liver disease, by Craig J. McClain, S. Joshi‐Barve, D. Hill, J Schmidt, I. Deaciuc, and S. Barve; (3) The role of mitochondria in ethanol‐mediated sensitization of the liver, by Anna Colell, Carmen Garcia‐Ruiz, Neil Kaplowitz, and Jose C. Fernandez‐Checa; (4) A peroxisome proliferator (bezafibrate) can prevent superoxide anion release into hepatic sinusoid after acute ethanol administration, by Hirokazu Yokoyama, Yukishige Okamura, Yuji Nakamura, and Hiromasa Ishii; (5) S‐adenosylmethionine affects tumor necrosis factor‐α gene expression in macrophages, by Rajendar K. Chawla, S. Barve, S. Joshi‐Barve, W. Watson, W. Nelson, and C. McClain; (6) Iron, retinoic acid and hepatic macrophage TNFα gene expression in ALD, by Hidekazu Tsukamoto, Min Lin, Mitsuru Ohata, and Kenta Motomura; and (7) Role of Kupffer cells and gut‐derived endotoxin in alcoholic liver injury, by N. Enomoto, K. Ikejima, T. Kitamura, H. Oide, Y. Takei, M. Hirose, B. U. Bradford, C. A. Rivera, H. Kono, S. Peter, S. Yamashina, A. Konno, M. Ishikawa, H. Shimizu, N. Sato, and R. Thurman.
    Type of Medium: Online Resource
    ISSN: 0145-6008 , 1530-0277
    URL: Issue
    URL: Article
    DOI: 10.1111/acer.2001.25.issue-s1
    DOI: 10.1111/j.1530-0277.2001.tb02393.x
    Language: English
    Publisher: Wiley
    Publication Date: 2001
    detail.hit.zdb_id: 2046886-6
    detail.hit.zdb_id: 3167872-5
    SSG: 15,3
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  • 9
    Online Resource
    Online Resource
    Acute alcohol produces hypoxia directly in rat liver tissue in vivo: role of Kupffer cells
    American Physiological Society ; 1996
    In:  American Journal of Physiology-Gastrointestinal and Liver Physiology Vol. 271, No. 3 ( 1996-09-01), p. G494-G500
    Details
    In: American Journal of Physiology-Gastrointestinal and Liver Physiology, American Physiological Society, Vol. 271, No. 3 ( 1996-09-01), p. G494-G500
    Abstract: Previous studies using liver slices and isolated perfused rat liver have suggested that ethanol causes hypoxia by increasing oxygen consumption. However, ethanol also increases blood flow to the liver, a phenomenon that may counteract the effects of hypermetabolism by increasing oxygen delivery. Thus whether ethanol causes hypoxia in vivo remains unclear. To clarify this important point, female Sprague-Dawley rats (100-125 g) simultaneously received pimonidazole (120 mg/kg ip), a 2-nitroimidazole hypoxia marker, and one large dose of ethanol (5 g/kg ig), which increase hepatic oxygen uptake dramatically and elevate ethanol metabolism (swift increase in alcohol metabolism) in 2-3 h. After 2 h, ethanol significantly increased the accumulation of bound pimonidazole in pericentral regions of the liver lobule. Treatment of animals with the Kupffer cell-specific toxicant, GdCl3 (10 mg/kg iv, 24 h before experiment), blocked ethanol-induced increases in pimonidazole binding. It is concluded that one large dose of ethanol causes pericentral hypoxia in rat liver tissue in vivo and that Kupffer cells are involved.
    Type of Medium: Online Resource
    ISSN: 0193-1857 , 1522-1547
    URL: Article
    DOI: 10.1152/ajpgi.1996.271.3.G494
    Language: English
    Publisher: American Physiological Society
    Publication Date: 1996
    detail.hit.zdb_id: 1477329-6
    SSG: 12
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  • 10
    Online Resource
    Online Resource
    Female rats exhibit greater susceptibility to early alcohol-induced liver injury than males
    American Physiological Society ; 1997
    In:  American Journal of Physiology-Gastrointestinal and Liver Physiology Vol. 272, No. 5 ( 1997-05-01), p. G1186-G1194
    Details
    In: American Journal of Physiology-Gastrointestinal and Liver Physiology, American Physiological Society, Vol. 272, No. 5 ( 1997-05-01), p. G1186-G1194
    Abstract: It is known that women develop hepatic injury more rapidly and with exposure to less ethanol than men; however, mechanisms remain unclear. The purpose of this study was to determine if an enteral alcohol delivery model could be used to study susceptibility of females to alcohol-induced liver injury. Male and female Wistar rats (age- or weight-matched) were given ethanol (11-12 g.kg-1.day-1) continuously for up to 4 wk via intragastric feeding, and control rats received a high-fat diet without ethanol. There were no significant differences in body weight among the groups studied. Furthermore, mean ethanol concentrations, their cyclic pattern in urine, and rates of ethanol elimination were also not different between the genders under these conditions. Ethanol treatment elevated serum aspartate aminotransferase levels in male rats to 126 +/- 10 IU/l after 4 wk. In females, however, values increased more rapidly and reached significantly higher values at 4 wk (168 +/- 18 IU/l). Steatosis, inflammation, and necrosis assessed histologically also developed more rapidly and were more severe in females than males. Steatosis due to ethanol exposure, which was localized in centrilobular areas in males, was panlobular in the female. Moreover, endotoxin in plasma, intercellular adhesion molecule 1 expression in hepatic sinusoidal-lining cells, and the number of infiltrating inflammatory cells in the liver were 2-2.5-fold greater in females than males. These changes possibly account for increased hepatic injury due to ethanol in the female.
    Type of Medium: Online Resource
    ISSN: 0193-1857 , 1522-1547
    URL: Article
    DOI: 10.1152/ajpgi.1997.272.5.G1186
    Language: English
    Publisher: American Physiological Society
    Publication Date: 1997
    detail.hit.zdb_id: 1477329-6
    SSG: 12
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