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  • American Physiological Society  (3)
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  • American Physiological Society  (3)
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  • 1
    Online Resource
    Online Resource
    Isoproterenol antagonizes endothelial permeability induced by thrombin and thrombin receptor peptide
    American Physiological Society ; 1993
    In:  Journal of Applied Physiology Vol. 75, No. 3 ( 1993-09-01), p. 1171-1179
    Details
    In: Journal of Applied Physiology, American Physiological Society, Vol. 75, No. 3 ( 1993-09-01), p. 1171-1179
    Abstract: We determined whether 1) amino-terminal peptides of the thrombin receptor increase endothelial permeability to a comparable extent as alpha-thrombin does, 2) isoproterenol attenuates the thrombin-induced increase in endothelial permeability by an antagonistic action to that of thrombin or by lowering baseline permeability, and 3) isoproterenol decreases permeability via stimulation of the beta 2-adrenergic receptor. Permeability across monolayers of bovine pulmonary artery endothelial cells (CCL 209) was assessed by the clearance of 125I-labeled albumin. Thrombin receptor peptides increased permeability at 1 microM but required a dose of between 10 and 100 microM to equal the permeability response of 1 microM alpha-thrombin. Dose-response experiments demonstrated that isoproterenol antagonized the action of alpha-thrombin and a thrombin receptor peptide on endothelial permeability and that it lowered baseline permeability. This permeability-decreasing action of isoproterenol occurred via stimulation of the beta 2-adrenergic receptor. Terbutaline, a partial beta 2-agonist, prevented the thrombin-induced permeability, but dobutamine, a partial beta 1-agonist, did not. The active stereoisomer of terbutaline and the racemic form mimicked the action of isoproterenol, but the inactive stereoisomer had no effect. ICI-118,551, a specific beta 2-receptor antagonist, prevented the permeability-decreasing action of isoproterenol, whereas ICI-89,406, a specific beta 1-receptor antagonist, did not. Competitive binding studies of 125I-pindolol with ICI-118,551 or ICI-89,406 demonstrated the presence of beta-adrenergic receptors, predominantly beta 2-receptors, on cell membrane homogenates.(ABSTRACT TRUNCATED AT 250 WORDS)
    Type of Medium: Online Resource
    ISSN: 8750-7587 , 1522-1601
    URL: Article
    DOI: 10.1152/jappl.1993.75.3.1171
    RVK:
    WA 15000
    RVK:
    XA 52094
    Language: English
    Publisher: American Physiological Society
    Publication Date: 1993
    detail.hit.zdb_id: 1404365-8
    SSG: 12
    SSG: 31
    Location Call Number Limitation Availability
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    Online Resource
  • 2
    Online Resource
    Online Resource
    Thrombin's enzymatic activity increases permeability of endothelial cell monolayers
    American Physiological Society ; 1990
    In:  Journal of Applied Physiology Vol. 69, No. 5 ( 1990-11-01), p. 1599-1606
    Details
    In: Journal of Applied Physiology, American Physiological Society, Vol. 69, No. 5 ( 1990-11-01), p. 1599-1606
    Abstract: Human alpha-thrombin increases the permeability of bovine pulmonary artery endothelial cell (CCL-209) monolayers. To determine if this increase is via an enzymatic or receptor-mediated mechanism, enzymatically active forms of alpha-thrombin and enzymatically inactive forms with cell binding activity were incubated with the monolayers. Enzymatic forms included alpha-thrombin and two digestion products, zeta-thrombin (chymotryptic product with 89% clotting activity) and gamma-thrombin (tryptic product). Enzymatically inactive forms included D-Phe-Pro-Arg-chloromethylketone-(PPACK) alpha-thrombin and diisopropylphosphorofluoridate-(DIP) alpha-thrombin. Cell binding activity of alpha- and PPACK-alpha-thrombin was demonstrated to be similar to each other and comparable to that cited in the literature for DIP-alpha-thrombin. gamma-Thrombin, on the other hand, did not compete for binding of 125I-labeled alpha-thrombin. All enzymatic forms of alpha-thrombin increased endothelial permeability as assessed by the clearance of 125I-albumin across the monolayers. Coincubation of PPACK, an enzymatic site inhibitor, with alpha- or gamma-thrombin prevented the increase in permeability, further indicating that alpha-thrombin increased permeability by its enzymatic activity. Both enzymatically inactive forms of alpha-thrombin with high-affinity binding activity had no effect on permeability. To further examine whether cell binding activity of alpha-thrombin contributed to the increased permeability, a sulfated COOH-terminal fragment of hirudin (hirugen) that binds to the anion-binding site of alpha-thrombin but, unlike hirudin, does not interact with the catalytic site was coincubated with alpha-thrombin.(ABSTRACT TRUNCATED AT 250 WORDS)
    Type of Medium: Online Resource
    ISSN: 8750-7587 , 1522-1601
    URL: Article
    DOI: 10.1152/jappl.1990.69.5.1599
    RVK:
    WA 15000
    RVK:
    XA 52094
    Language: English
    Publisher: American Physiological Society
    Publication Date: 1990
    detail.hit.zdb_id: 1404365-8
    SSG: 12
    SSG: 31
    Location Call Number Limitation Availability
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    Online Resource
  • 3
    Online Resource
    Online Resource
    Isoproterenol reduces thrombin-induced pulmonary endothelial permeability in vitro
    American Physiological Society ; 1989
    In:  American Journal of Physiology-Heart and Circulatory Physiology Vol. 257, No. 5 ( 1989-11-01), p. H1613-H1623
    Details
    In: American Journal of Physiology-Heart and Circulatory Physiology, American Physiological Society, Vol. 257, No. 5 ( 1989-11-01), p. H1613-H1623
    Abstract: The ability of the beta-adrenergic agonist, isoproterenol, to attenuate the thrombin-induced increase in endothelial permeability was examined by measuring 125I-labeled albumin clearance across endothelial cell monolayers. Bovine pulmonary artery endothelial cells (CCL-209) were grown to confluence on gelatinized, polycarbonate micropore filters and mounted on modified Boyden chambers with Dulbecco's modified Eagle's medium (DMEM) and 0.5% bovine serum albumin. alpha-Thrombin at 0.2 nM to 2 microM produced a dose-related increase (P less than 0.01) in 125I-labeled albumin clearance from the DMEM control value. Light and electron microscopy revealed that the thrombin-induced increase in permeability correlated with changes in cell shape and rearrangement of filamentous actin. Coincubation of 2 microM isoproterenol with 2 microM alpha-thrombin reduced (P less than 0.01) the thrombin-induced increase in albumin clearance and the observed morphological changes. This attenuation was not caused by inhibition of thrombin's enzymatically active site, since isoproterenol did not impair thrombin's fibrinogen clotting activity nor its amidolytic cleavage of an artificial substrate (Spectrozyme-TH). Coincubation of 20 microM propranolol, a beta-adrenergic antagonist, with 2 microM isoproterenol and thrombin blocked the permeability-decreasing effect of isoproterenol. Both 2 microM isoproterenol and 2 pM alpha-thrombin alone decreased (P less than 0.01) albumin clearance below the DMEM control value. These results suggest that isoproterenol can reduce the thrombin-induced increase in endothelial permeability in vitro by directly maintaining actin filaments and the shape of endothelial cells.
    Type of Medium: Online Resource
    ISSN: 0363-6135 , 1522-1539
    URL: Article
    DOI: 10.1152/ajpheart.1989.257.5.H1613
    RVK:
    WA 15000
    Language: English
    Publisher: American Physiological Society
    Publication Date: 1989
    detail.hit.zdb_id: 1477308-9
    SSG: 12
    Location Call Number Limitation Availability
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    Online Resource
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