eISSN: 1644-4124
ISSN: 1426-3912
Central European Journal of Immunology
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1/2008
vol. 33
 
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abstract:

Experimental immunology
The role of proteinase-activated receptor 3 (PAR3) in mouse hybridoma studied with monoclonal antibody generated against thrombin cleavage site

Yuliya I. Petrova
,
Olena V. Kameneva
,
Anastasiya I. Zhukova
,
Lesley Scudder
,
Dmitriy V. Gnatenko
,
Wadie F. Bahou
,
Sergiy V. KOMomisarenko
,
Maryna V. Skok

(Centr Eur J Immunol 2008; 33 (1): 14-18)
Online publish date: 2008/03/25
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Thrombin produced upon tissue damage provides a link between inflammation/blood coagulation and immune reactions through proteinase-activated receptor (PAR) types 1, 3 and 4. In contrast to PAR1 and PAR4, functions of PAR3 in cells other than platelets are poorly understood. We generated mAb 8E8 against fragment 31-47, which includes the thrombin cleavage site of human PAR3. MAb 8E8 bound mouse platelets and delayed their aggregation induced by thrombin. This antibody also specifically stained B-lymphocyte-derived hybridoma in flow cytometry. Thrombin dose-dependently inhibited hybridoma cell proliferation and so did mAb 8E8 and PAR3 31-47 fragment, but not the PAR4 activating peptide. It is concluded that mAb 8E8 recognizes PAR3 expressed in hybridoma and mimics the inhibitory effect of thrombin on hybridoma proliferation mediated by PAR3. The data obtained also suggest that, unlike in platelets, targeting PAR3 in mouse B lymphocyte-derived cells doesn’t involve PAR4.
keywords:

proteinase-activated receptor, thrombin, monoclonal antibody, hybridoma, proliferation

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