Study on the interaction between Fe3+and fibrinogen and its influence on the polymerization behavior of fibrin networks

Lei Wang; Rui Li; Lianzhi Li; Huaisheng Wang; Jifeng Liu

doi:10.1039/c6ra17661e

Study on the interaction between Fe3+and fibrinogen and its influence on the polymerization behavior of fibrin networks

RSC Advances ◽

10.1039/c6ra17661e ◽

2016 ◽

Vol 6 (79) ◽

pp. 75207-75214

Author(s):

Lei Wang ◽

Rui Li ◽

Lianzhi Li ◽

Huaisheng Wang ◽

Jifeng Liu

Keyword(s):

Fibrin Networks ◽

Polymerization Behavior ◽

Amorphous Aggregation ◽

Fibrinogen Molecule

The interactions between fibrinogen molecule and Fe3+were studied and applied to explicate the polymerization behavior of fibrinogen mediated with Fe3+. Overloading Fe3+in the fibrinogen solution will accelerate the amorphous aggregation of fibrin.

Download Full-text

Properties of Fibrinogen Cleaved by Jararhagin, a Metalloproteinase from the Venom of Bothrops jararaca

Thrombosis and Haemostasis ◽

10.1055/s-0038-1648847 ◽

1994 ◽

Vol 72 (02) ◽

pp. 244-249 ◽

Cited By ~ 48

Author(s):

Aura S Kamiguti ◽

Joseph R Slupsky ◽

Mirko Zuzel ◽

Charles R M Hay

Keyword(s):

Platelet Aggregation ◽

Platelet Function ◽

Fibrin Clot ◽

Clot Formation ◽

Human Fibrinogen ◽

Activated Platelets ◽

Bothrops Jararaca ◽

Platelet Binding ◽

Fibrin Monomers ◽

Fibrinogen Molecule

SummaryHaemorrhagic metalloproteinases from Bothrops jararaca and other venoms degrade vessel-wall and plasma proteins involved in platelet plug and fibrin clot formation. These enzymes also cause proteolytic digestion of fibrinogen which has been suggested to cause defective platelet function. Fibrinogen degradation by jararhagin, a metalloproteinase from B. jararaca, and the effect of jararhagin fibrinogenolysis on both platelet aggregation and fibrin clot formation were investigated. Jararhagin was found to cleave human fibrinogen in the C-terminal region of the Aα-chain giving rise to a 285-290 kDa fibrinogen molecule lacking the Aα-chain RGD 572-574 platelet-binding site. Platelet binding and aggregation of ADP-activated platelets is unaffected by this modification. This indicates that the lost site is not essential for platelet aggregation, and that the remaining platelet binding sites located in the N-terminal portion of Aα chains (RGD 95-97) and the C-terminal of γ chains (dodecapeptide 400-411) are unaffected by jararhagin-digestion of fibrinogen. Fibrin clot formation with thrombin of this remnant fibrinogen molecule was defective, with poor polymerization of fibrin monomers but normal release of FPA. The abnormal polymerization could be explained by the loss of one of the two complementary polymerization sites required for side-by-side association of fibrin protofibrils. Jararhagin-induced inhibition of platelet function, an important cause of haemorrhage in envenomed patients, is not caused by proteolysis of fibrinogen, as had been thought, and the mechanism remains to be elucidated.

Download Full-text

Common Antigenic Sites in Human, Bovine and Porcine Fibrinogens

Thrombosis and Haemostasis ◽

10.1055/s-0038-1650157 ◽

1981 ◽

Vol 45 (02) ◽

pp. 169-172 ◽

Cited By ~ 2

Author(s):

Czeslaw S Cierniewski

Keyword(s):

Antigenic Determinants ◽

Antigenic Sites ◽

Specific Antisera ◽

Antigenic Homology ◽

Polypeptide Chains ◽

Fibrinogen Molecule

SummarySpecific antisera to the Aα, Bβ and γ chains of porcine fibrinogen were used to characterize an antigenic homology of human, bovine, and porcine fibrinogens. Antigenic determinants shared by these fibrinogens were mostly formed by the Aα chain. However, in the case of bovine and porcine fibrinogens they were also found in the Bβ and γ polypeptide chains. The results reported here show that the Aα chain determinants exposed on the intact fibrinogen molecule are conserved to a considerably larger extent than those of the Bβ and γ chains.

Download Full-text

Functional Relationship of Polymerization Sites of Vertebrate Fibrinogens

10.1055/s-0038-1665661 ◽

1979 ◽

Author(s):

C Cierniewski ◽

T Krajewski ◽

E Janiak

Keyword(s):

Gel Electrophoresis ◽

Functional Relationship ◽

Polyacrylamide Gel Electrophoresis ◽

Polyacrylamide Gel ◽

Functional Similarity ◽

Fractionation Method ◽

Relationship Of ◽

Fibrin Monomers ◽

Fibrinogen Molecule ◽

Cold Ethanol Fractionation

Various studies on the interaction of immobilized mammalian fibrinogen and fibrin monomers with some fibrinogen derivatives demonstrated the presence of two sets of polymerization sites in the mammalian fibrinogen molecule. We obtained the same results while investigating the fibrinogen molecules of other classes of vertebrates /Pisces. Amphibia. Aves/. Despite significant differences among their subunit structures, all of them contain polymerization sites homologous to mammalian counterparts. Moreover, due to great functional similarity, fibrinogen or fibrin monomers of the analyzed species of Pisces. Amphibia. Aves and Mammalia interacted in a specific way with immobilized pig fibrin monomers or fibrinogen, respectively. Using these pig affinity adsorbents, fibrinogen and fibrin monomers of different vertebrates were isolated directly from plasma and analyzed by SDS polyacrylamide gel electrophoresis. Polypeptide compositions of eluted proteins were identical to those obtained for corresponding fibrinogen preparations isolated by cold-ethanol fractionation method. It appears to indicate that the nature of polymerization sites in vertebrate fibrinogens is alike.

Download Full-text

The Effect of Sibutramine, a Serotonin-Norepinephrine Reuptake Inhibitor, on Platelets and Fibrin Networks of Male Sprague-Dawley Rats: A Descriptive Study

Ultrastructural Pathology ◽

10.3109/01913123.2014.946635 ◽

2014 ◽

Vol 38 (6) ◽

pp. 399-405 ◽

Cited By ~ 2

Author(s):

Ciska van der Schoor ◽

Hester Magdalena Oberholzer ◽

Megan Jean Bester ◽

Mia-Jeanne van Rooy

Keyword(s):

Reuptake Inhibitor ◽

Descriptive Study ◽

Sprague Dawley ◽

Fibrin Networks ◽

Sprague Dawley Rats ◽

Norepinephrine Reuptake Inhibitor ◽

Serotonin Norepinephrine Reuptake Inhibitor ◽

Norepinephrine Reuptake

Download Full-text

The Budapest Amyloid Predictor and Its Applications

Biomolecules ◽

10.3390/biom11040500 ◽

2021 ◽

Vol 11 (4) ◽

pp. 500

Author(s):

László Keresztes ◽

Evelin Szögi ◽

Bálint Varga ◽

Viktor Farkas ◽

András Perczel ◽

...

Keyword(s):

Neural Network ◽

Neural Networks ◽

Artificial Neural Networks ◽

Support Vector ◽

User Needs ◽

Computational Technique ◽

Linear Support Vector Machine ◽

Β Sheets ◽

Artificial Neural ◽

Amorphous Aggregation

The amyloid state of proteins is widely studied with relevance to neurology, biochemistry, and biotechnology. In contrast with nearly amorphous aggregation, the amyloid state has a well-defined structure, consisting of parallel and antiparallel β-sheets in a periodically repeated formation. The understanding of the amyloid state is growing with the development of novel molecular imaging tools, like cryogenic electron microscopy. Sequence-based amyloid predictors were developed, mainly using artificial neural networks (ANNs) as the underlying computational technique. From a good neural-network-based predictor, it is a very difficult task to identify the attributes of the input amino acid sequence, which imply the decision of the network. Here, we present a linear Support Vector Machine (SVM)-based predictor for hexapeptides with correctness higher than 84%, i.e., it is at least as good as the best published ANN-based tools. Unlike artificial neural networks, the decisions of the linear SVMs are much easier to analyze and, from a good predictor, we can infer rich biochemical knowledge. In the Budapest Amyloid Predictor webserver the user needs to input a hexapeptide, and the server outputs a prediction for the input plus the 6 × 19 = 114 distance-1 neighbors of the input hexapeptide.

Download Full-text

Non-coding RNA suppresses FUS aggregation caused by mechanistic shear stress on pipetting in a sequence-dependent manner

Scientific Reports ◽

10.1038/s41598-021-89075-w ◽

2021 ◽

Vol 11 (1) ◽

Author(s):

Nesreen Hamad ◽

Ryoma Yoneda ◽

Masatomo So ◽

Riki Kurokawa ◽

Takashi Nagata ◽

...

Keyword(s):

Shear Stress ◽

Neurodegenerative Diseases ◽

Suppressive Effect ◽

Dependent Manner ◽

Aggregation State ◽

Fused In Sarcoma ◽

Sequence Dependent ◽

Non Coding Rna ◽

Aggregation Inhibitors ◽

Amorphous Aggregation

AbstractFused in sarcoma/translocated in liposarcoma (FUS/TLS) is a multitasking RNA/DNA binding protein. FUS aggregation is implicated in various neurodegenerative diseases. RNA was suggested to modulate phase transition of FUS. Here, we found that FUS transforms into the amorphous aggregation state as an instant response to the shear stress caused by usual pipetting even at a low FUS concentration, 100 nM. It was revealed that non-coding RNA can suppress the transformation of FUS into aggregates. The suppressive effect of RNA on FUS aggregation is sequence-dependent. These results suggested that the non-coding RNA could be a prospective suppressor of FUS aggregation caused by mechanistic stress in cells. Our finding might pave the way for more research on the role of RNAs as aggregation inhibitors, which could facilitate the development of therapies for neurodegenerative diseases.

Download Full-text

Grignard coupling-based synthesis of vinyl-substituted hydridopolycarbosilane: effect of starting material and polymerization behavior

RSC Advances ◽

10.1039/d1ra00244a ◽

2021 ◽

Vol 11 (19) ◽

pp. 11771-11778

Author(s):

Minji Jeong ◽

Moon-Gun Choi ◽

Yoonjoo Lee

Keyword(s):

Coupling Reaction ◽

Starting Material ◽

Polymerization Behavior

Polymerization of VHPCS by the Grignard coupling reaction depended on the type of starting material. In the case of Cl3SiCH2Cl starting material, a stepwise growth manner was shown, due to a coupling between –CH2Cl and the Si–Cl sites.

Download Full-text