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 |