PL
 |
EN
Nowa wersja platformy, zawierająca wyłącznie zasoby pełnotekstowe, jest już dostępna.
Przejdź na https://bibliotekanauki.pl
Preferencje help
Polish version English version Język
Widoczny [Schowaj] Abstrakt
Liczba wyników

Znaleziono wyników: 11

Liczba wyników na stronie
first rewind previous Strona / 1 next fast forward last
Wyniki wyszukiwania
Wyszukiwano:
w słowach kluczowych:  fibrin
help Sortuj według:

help Ogranicz wyniki do:
first rewind previous Strona / 1 next fast forward last
1
Content available Non-enzymatic activation of prothrombin induced by interaction with fibrin β26-42 region
100%
Chernyshenko V. , Chernyshenko T. , Korolova D. y. , Volynets G. , Kolesnikova I. , Platonova T. , Lugovskoy E.
Acta Biochimica Polonica
|
2015
|
tom 62
|
nr 3
517-522
EN
We have discovered that addition of monomeric desAB fibrin to prothrombin leads to appearance of the thrombin-like activity of prothrombin towards S2238 chromogenic substrate. DesA and desABβ(15-42)2 fibrin forms did not cause any activation of prothrombin. From this observation we could suggested that amino acid residues of the 15-42 fragment of BβN-domain presented in desAB fibrin, cleaved in desABβ(15-42)2 fibrin and protected in desA fibrin, play a crucial role in the non-enzymatic activation of prothrombin. To identify the Bβ amino acid residues involved in the fibrin-prothrombin binding we used monoclonal antibodies 1-5G and 2d2a with epitopes in Bβ26-42 and Bβ12-26 fibrin fragments respectively. The thrombin-like activity in the mixture of prothrombin and desAB fibrin was monitored in the presence of each of these monoclonal antibodies. It was found that anti-Bβ12-26 antibody does not exhibit any inhibitory effect on the thombin-like activity of the mixture. In contrast, adding of Bβ26-42 antibody into the mixture of desAB fibrin with prothrombin diminished the thrombin-like activity by 70%. Recombinant dimeric peptides Bβ(15-44)2 and Bβ(15-66)2 that mimic amino acid residues in fibrin were also tested for their ability to activate prothrombin. It was found that both peptides were able to induce non-enzymatic activation of prothrombin. The activation was more evident in the case of Bβ(15-44)2 peptide. From the data obtained we can conclude that desAB fibrin binds to prothrombin through the Bβ26-42 amino acid residues and the formation of such a complex caused a non-enzymatic activation of prothrombin.
2
Influence of phosphorohydrazone derivatives of benzopyrones on polymerization and viscosity of fibrin
86%
Michalska M. , Pajak W. , Kolodziejska J. , Lazarenkow A. , Nawrot-Modranka J.
Acta Biochimica Polonica
|
2008
|
tom 55
|
nr 3
613-617
EN
The synthesis and antitumour and antibacterial activity of coumarin and chromone phosphorohydrazones have been reported. This study describes influence of phosphorohydrazones derivatives of coumarin and chromone on the polymerization and viscosity of fibrin. The fibrin polymerization assay was performed by the Shen and Lorand method and the clot viscosity was measured on the basis of Shen and Lorand and Marchi and coworkers methods. Among the eight compounds tested, one coumarin derivative and two chromone derivatives showed significant activity
3
Content available remote Influence of phosphorohydrazone derivatives of benzopyrones on polymerization and viscosity of fibrin
86%
Michalska M. , Pająk W. , Kołodziejska J. , Łazarenkow A. , Nawrot-Modranka J.
Acta Biochimica Polonica
|
2008
|
tom 55
|
nr 3
613-617
EN
The synthesis and antitumour and antibacterial activity of coumarin and chromone phosphorohydrazones have been reported. This study describes influence of phosphorohydrazones derivatives of coumarin and chromone on the polymerization and viscosity of fibrin. The fibrin polymerization assay was performed by the Shen and Lorand method and the clot viscosity was measured on the basis of Shen and Lorand and Marchi and coworkers methods. Among the eight compounds tested, one coumarin derivative and two chromone derivatives showed significant activity.
4
Content available remote Plasma fibrin clots of pulmonary embolism patients present increased amounts of factor XIII and alpha2-antiplasmin at 3 months’ anticoagulation since the acute phase
72%
Zabczyk M. , Natorska J. , Bagoly Z. , Sarkady F. , Barath B. , Katona E. , Bryk A. , Zettl K. , Wisniewski J. R. , Undas A.
Journal of Physiology and Pharmacology
|
2020
|
tom 71
|
nr 4
5
Content available remote Angiotensin-[1-9], the product of angiotensin I conversion in platelets, enhances arterial thrombosis in rats
72%
Kramkowski K. , Mogielnicki A. , Leszczynska A. , Buczko W.
Journal of Physiology and Pharmacology
|
2010
|
tom 61
|
nr 3
317-324
EN
Angiotensin (Ang) (1-9) is the renin-angiotensin-system peptide found in the plasma of healthy volunteers and after angiotensin-converting-enzyme inhibitors therapy. In vitro experiments proved that Ang-(1-9) may be produced from Ang I. In our study, we tried to expand the poor data about the in vivo properties of Ang-(1-9). We revealed that Ang-(1-9) enhanced electrically stimulated arterial thrombosis in the carotid artery of Wistar rats. Losartan, a selective blocker of AT1 receptor for Ang II, abolished the prothrombotic activity of Ang-(1-9). This peptide increased plasma level of fibrinogen, augments fibrin generation, and similarly to Ang II, potentiated collagen induced platelet aggregation. Using HPLC, we found that after incubation of Ang-(1-9) with platelet homogenates or after intravenous administration this peptide is converted to Ang II. We concluded that Ang-(1-9) exerts an Ang II-like prothrombotic effect due to the conversion to Ang II in the circulatory system of rats and that platelets are involved in this process.
6
Content available Endothelial cells on pet vascular prostheses impregnated with polyester-based copolymers and coated with cell-adhesive protein assemblies
58%
Chlupac J. , Filova E. , Riedel T. , Brynda E. , Pamuła E. , Lisa V. , Bacakova L.
Engineering of Biomaterials
|
2008
|
tom Vol. 11, no. 81-84
108--111
EN
Arterial bypass surgery with synthetic vascular prostheses achieves poor patency rates compared to autogenous natural materials, and this is a challenge for tissue engineering research concerning small caliber vascular grafts. Modifications of the prosthetic surface followed by endothelial cell seeding may reduce thrombogenicity and intimal hyperplasia. Planar polyethylene terephthalate (PET) vascular prosthetic samples were impregnated with the copolymer poly(glycolide-L-lactide) (PGL) or with the terpolymer poly(glycolide-L-lactide-(e)caprolactone) (PGLCap) in order to lower the permeability of the knitted fabrics and ensure a less adhesive background. Subsequent modification with adhesive protein assemblies composed of collagen type I (Co) in conjunction with laminin (LM), fibronectin (FN) or fibrin (Fb) gel was performed to enhance cell adhesion. Bovine pulmonary artery endothelial cells (EC) of the CPAE line were seeded on to the coatings and subjected to static tissue culture conditions for 7 days. Impregnation of the PET prostheses decreased the initial adhesion and proliferation of the EC. After coating with the protein assemblies, the impregnated PET provided better substrates for cell culture than the protein-coated PET, on which the EC population started decreasing after 4 days of culture. The cells proliferated better on the CoFN, CoFb and CoFbFN coatings than on the Co and CoLM coatings. Impregnation type and adhesive matrix protein deposition may play an important role in successful endothelialization, healing and clinical performance of vascular grafts.
7
Content available Human endothelium on vascular prostheses modified by extracellular matrix proteins in a flow experiment
58%
Chlupac J. , Filova E. , Riedel T. , Brynda E. , Remy-Zolghadri M. , Bareille R. , Fernandez P. , Daculsi R. , Bordenave L. , Bacakova L.
Inżynieria Biomateriałów
|
2006
|
tom R. 9, nr 58-60
10-13
EN
Artificial vascular prostheses are used for bypass surgery. Thrombogenicity often cause graft occlusion. Targeted surface alterations including cell seeding may improve the haemocompatibility. Knitted commercial tubular PET (polyethylene terephtalate) vascular prostheses with collagen impregnation were modified by adsorption of laminin (LM) or coating with fibrin network (FB) on the luminal surface. Human endothelial cells were harvested, cultured and seeded at the density of 150x10\3 cells/cm square on all grafts. The cell lining was continuously visualized and quantified. The retention was 21%, 37% and only 2% of the seeding density on the unmodified (UM), LM- and FB-coated grafts, respectively. These seeded prostheses were exposed to a laminar shear stress (SS) 15 dynes/cm square for 40 minutes (UM, LM, FB) and 120 min (UM, LM) in a chamber simulating blood circulation. The SS was excluded in static (ST) control grafts. After 40 min-SS the cell numbers were78%, 27% and 72% for the UM, LM and FB prosthesis compared to the ST. The cell densities were 61% and 57% on the UM and LM after 120 min-SS. To conclude, the endothelium formed a confluent layer whereas laminin immobilization improved endothelial adhesion but not the flow resistance. Reverse effect was observed on fibrin coating.
8
Content available remote Niskocząsteczkowe inhibitory plazminy
58%
Midura-Nowaczek K.
Wiadomości Chemiczne
|
1998
|
tom [Z] 52, 11-12
871--887
EN
Plasmin, serine protease with trypsin specifity, plays a key role in the process of fibrinolysis. Analogs of lysine like e-aminocaproic acid and trans-4-aminomethylclohexanecarboxylic acid are employed clinically as plasmin inhibitors and exhibit an inhibitory effect by blocking lysine binding sites of the enzyme. Their inhibitory activity on plasmin with the respect to fibrinogen and other proteins is much weaker than towards fibrin. Because of this reason investigations on the synthesis of an active centre directed inhibitors of plasmin were also undertaken. A great number of compounds was obtained including derivatives of w-aminoacids or lysine. Next important group were short peptides with C-terminal lysine or arginine derivatives such as aldehydes, chloromethylketones, fluoromethylketone, methylketones, amides or esters. This paper presents literature data on structure-activity relationship for low molecular inhibitors of plasmin with a structure of aminoacids or peptides derivatives.
9
Inhibition of fibrin formation and plasmin activity by formaldehyde: studies in vitro
58%
Jasielczuk J. , Dabrowski L.
|
|
tom 11
|
nr 1
10
Wlasciwosci pepsyny jako biaka polianionowego. Cz. VIII. Interakcje pepsyny z fibrynogenem, monomerami fibryny i fibryna
51%
Jasielczuk J.
Bromatologia i Chemia Toksykologiczna
|
2003
|
tom 36
|
nr 3
247-254
11
Wplyw skladnikow suplementow diety - wapnia i magnezu na lepkosc fibryny nieusieciowanej
44%
Michalska M. , Kolodziejska J.
Bromatologia i Chemia Toksykologiczna
|
2006
|
tom 39
|
nr 2
173-178
first rewind previous Strona / 1 next fast forward last
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.