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The urokinase-plasminogen activator system in ovine macrophages and neutrophils

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dc.contributor.author Politis, I en
dc.contributor.author Bizelis, I en
dc.contributor.author Rogdakis, E en
dc.date.accessioned 2014-06-06T06:45:10Z
dc.date.available 2014-06-06T06:45:10Z
dc.date.issued 2002 en
dc.identifier.issn 09214488 en
dc.identifier.uri http://dx.doi.org/10.1016/S0921-4488(02)00040-8 en
dc.identifier.uri http://62.217.125.90/xmlui/handle/123456789/2284
dc.subject Macrophages en
dc.subject Neutrophils en
dc.subject Sheep en
dc.subject Urokinase-plasminogen activator en
dc.subject.other Ovis en
dc.subject.other Ovis aries en
dc.title The urokinase-plasminogen activator system in ovine macrophages and neutrophils en
heal.type journalArticle en
heal.identifier.primary 10.1016/S0921-4488(02)00040-8 en
heal.publicationDate 2002 en
heal.abstract The urokinase-plasminogen activator (u-PA) system in resting and activated ovine macrophages and neutrophils was examined. Macrophages and neutrophils were isolated from a total of 28 lactating sheep of the Chios breed. Low amounts of u-PA were found intracellularly or membrane-bound in resting macrophages and neutrophils. However, incubation of resting macrophages or neutrophils with purified u-PA (10 IU/ml) revealed extensive binding of u-PA to cell membranes. Excess amino terminal fragment of the u-PA molecule, a proteolytically inactive fragment of u-PA (amino acids 1-135) blocked binding of u-PA to macrophage or neutrophil cell membrane. These results indicate that the binding of u-PA is specific and that resting neutrophils and macrophages have unoccupied u-PA receptors on their cell membrane. Addition of phorbol myristate acetate (PMA) led to an increase (P < 0.01) in total cell-associated and membrane-bound u-PA activity and a decrease (P < 0.01) in free, unoccupied u-PA binding sites of macrophages or neutrophils. No significant effects on total cell-associated or membrane-bound u-PA were found when macrophages or neutrophils were treated with 4-phorbol-12,13-didecanoate, a phorbol ester that does not activate protein kinase C (PKC). Furthermore, the PMA-induced increase in total cell-associated u-PA activity of sheep macrophages or neutrophils was completely ablated by the PKC inhibitor 1-(5-isoquinolinesulfonyl)-2-methylpiperazine dihydrochloride (H-7, 100 μM) but was unaffected by the cyclic nucleotide-dependent protein kinase inhibitor N-(2-quanidinoethyl)-5-isoquinoline sulfonamide hydrochloride (HA-1004, 100 μM). Thus, PKC plays a role in the modulation of u-PA system by PMA in ovine macrophages and neutrophils. © 2002 Elsevier Science B.V. All rights reserved. en
heal.journalName Small Ruminant Research en
dc.identifier.issue 1 en
dc.identifier.volume 44 en
dc.identifier.doi 10.1016/S0921-4488(02)00040-8 en
dc.identifier.spage 17 en
dc.identifier.epage 23 en


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