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1

Heparine - new perspectives of antiinflammatory therapy

100%
Krasnowska M., Kwasniewski A.
|
|
vol. 49
|
issue 5
661-669
EN
Heparine is used as a therapeutic anticoagulant.Research carried out in the last years showed in both in vivo and in vitro experiments (also in men), that this is a pleiotropic substance with many diverse activities.Immunoregulatory properties of heparine, including immunosupressive and most of all anto-proliferative lead to create the theory of its possible use in sevral chronic inflamatory processes.First experiments seem to justify this opinion.
2

Heparin and atherosclerosis

75%
Stajszczak M., Gminski J.
Postępy Higieny i Medycyny Doświadczalnej
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1994
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vol. 48
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issue 3
275-290
EN
Heparin is a highly sulfated glycosaminoglycan with many functions such as antilipemic and antithrombotic.In spite os these activities heparin is able to inhibit vacsular smooth muscle cells proliferation and mmigration what seems to be very important event in the pathogenesis of atherosclerosos.The molecular mechanism of the action of heparin on smooth muscle cells is not yet understood.Heparin inhibits growth factors binding to their receptors,oncogenes expressionand has influence on the extracellular matrix protein deposition in the artery wall.
3

Functions of human complement inhibitor C4b-binding protein in relation to its structure

75%
Blom A. M., Villoutreix B. O., Dahlback B.
Archivum Immunologiae et Therapiae Experimentalis
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2004
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vol. 52
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issue 2
83-95
EN
Considering the destructive potential of the complement cascade, it is no surprise that there are several complement inhibitors present in blood and expressed on virtually all cells of the body to protect self tissue. C4b-binding protein (C4BP) is a potent soluble inhibitor of the classical and lectin pathways of complement. This large (500 kDa) plasma glycoprotein consists of seven identical 75 kDa alpha-chains and a unique 40 kDa alpha-chain that are held together by disulphide bridges. Both types of subunit are almost exclusively composed of complement control protein (CCP) domains. In recent years, detailed studies of structure-function relationships have yielded new understanding of the interactions between C4BP and the activated complement factors C4b and C3b, heparin, and vitamin K-dependent anticoagulant protein S. This review describes the localization of binding sites for a number of C4BP ligands in relation to well-established and novel functions of C4BP such as complement inhibition, protection of apoptotic cells from complement, CD40-dependent stimulation of B cells, and the contribution of a number of human pathogens to pathogenesis.
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