On the aggregation of fibrinogen molecules

Gollwitzer, Rotraut; Bode, Wolfram; Karges, H E

doi:10.1016/0049-3848(83)90438-3

Cited by 21 publications

(20 citation statements)

References 14 publications

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“…The needles ranged in size up to 100-pm long and 1-to 5-pm thick. Similar structures, induced by a vapor diffusion technique, have been reported recently by Gollwitzer et al 5 The fibrinogen needles formed in buffers containing 200 m M NaCl accounted for only 10-15% of the total fibrinogen; 85-90% of the fibrinogen remained soluble even a t the high protein concentration. The number of needles formed in 300 m M NaCl was less than in buffer B1 or B2, but the exact amount was not quantitated.…”

Section: Fibrinogen Needlessupporting

confidence: 84%

Concentration of protein in fibrin fibers and fibrinogen polymers determined by refractive index matching

1986

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SynopsisWe have used refractive index matching to determine the concentration of protein in the fibers in fibrin clots and of needlelike crystals of native fibrinogen. Our results are in agreement with those of Carr and Hermans [(1978) Macromolecules 11, 46-50], as determined by light scattering -namely, that protein makes up about 20% of the volume of the fiber. However, we have found that the protein concentration is strongly dependent on ionic strength. An increase in ionic strength caused a substantial drop in the protein concentration. In a buffer containing 100 m M NaCl, the protein concentration was 26.6-29.8 g of protein per 100 cm3 of polymer, and at 200 m M NaCl it was reduced to 22.1-23.1 g/lW cm3.

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Section: Fibrinogen Needlessupporting

confidence: 84%

Concentration of protein in fibrin fibers and fibrinogen polymers determined by refractive index matching

1986

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“…The self-assembly of fibrinogen without thrombin activation is a well known phenomenon that occurs under several experimental conditions (12). Although self-association of fibrinogen is readily induced, suggesting its potential significance, no physiologic role has been ascribed to this process.…”

Section: Discussionmentioning

confidence: 99%

“…It is well established that fibrinogen forms complexes with fibrin (11) and can self-associate without thrombin activation, forming aggregates (12). We have recently identified a new nanoscale fibrinogendependent process, which may contribute to the natural antiadhesive mechanisms operating on the surface of fibrin clots.…”

mentioning

confidence: 99%

“…In addition to these primary strong interactions, other weak interactions may play a role in the assembly of fibrin, including the ␣C-␣C (17), ␥C-␥C, and ␥C-␤C interactions (21) between the neighboring molecules in the fiber. These binding sites do not require thrombin activation and may potentially be involved in self-association of intact fibrinogen in the absence of thrombin activation, a process that occurs under certain experimental conditions (12).…”

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confidence: 99%

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The Assembly of Nonadhesive Fibrinogen Matrices Depends on the αC Regions of the Fibrinogen Molecule

Yermolenko

Gorkun

Fuhrmann

et al. 2012

Journal of Biological Chemistry

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Background: Surface-induced aggregation of fibrinogen results in the assembly of an extensible multilayered matrix, which prevents integrin-mediated cell adhesion. Results: Without the ␣C regions, the fibrinogen molecules assemble a defective, poorly extensible matrix supporting sustained cell adhesion. Conclusion:The assembly of nonadhesive fibrinogen multilayer requires the ␣C regions of the molecule. Significance: The molecular mechanism for the assembly of the fibrinogen multilayer is identified.

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“…Although the ability of soluble fibrinogen to form complexes with fibrin and its capacity to undergo self-association in solution under special conditions is well characterized, 19,27 little is known about the capacity of immobilized fibrinogen to form a complex with soluble fibrinogen. Numerous studies demonstrated that fibrinogen adsorbed on the surfaces or deposited in the extracellular matrix undergoes conformational changes and acquires properties of fibrin manifesting in binding of fibrin-specific mAbs and other molecules.…”

Section: Conformationally Altered Fibrinogen Is Capable Of Binding Somentioning

confidence: 99%

Antiadhesive effect of fibrinogen: a safeguard for thrombus stability

Lishko

Burke

Ugarova

2006

Blood

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The recruitment of phagocytic leukocytes to sites of vessel wall injury plays an important role in thrombus dissolution by proteases elaborated on their adhesion. However, leukocyte adhesion to the fibrin clot can be detrimental at the early stages of wound healing when hemostatic plug integrity is critical for preventing blood loss. Adhesion of circulating leukocytes to the insoluble fibrin(ogen) matrix is mediated by integrins and occurs in the presence of a high concentration of plasma fibrinogen. In this study, the possibility that soluble fibrinogen could protect fibrin from excessive adhesion of leukocytes was examined. Fibrinogen was a potent inhibitor of adhesion of U937 monocytoid cells and neutrophils to fibrin gel and immobilized fibrin(ogen). An investigation of the mechanism by which soluble fibrinogen exerts its influence on leukocyte adhesion indicated that it did not block integrins but rather associated with the fibrin(ogen) substrate. Consequently, leukocytes that engage fibrinogen molecules loosely bound to the surface of fibrin(ogen) matrix are not able to consolidate their grip on the substrate; IntroductionThe recruitment of phagocytic leukocytes to sites of injured vessel wall plays an important role in thrombus remodeling during normal vascular repair and in the pathophysiology of thrombosis. Fibrinogen and fibrin, present in the thrombus, function as potent adhesive substrates for neutrophils and monocytes. They support cellular attachment by binding cell-surface receptors that belong to the ␤ 2 subfamily of integrins, including ␣ M ␤ 2 (Mac-1, CD11b/CD18), ␣ X ␤ 2 (CD11c/CD18), and ␣ D ␤ 2 (CD11d/CD18). 1-3 Furthermore, integrin ␣ 5 ␤ 1 on neutrophils contributes to adhesion to fibrin. 4 Numerous in vitro studies performed under static and flow conditions demonstrated that either stimulated or unstimulated neutrophils and monocytes adhere to the surface-bound fibrinogen and fibrin with alacrity. [5][6][7] Furthermore, stimulated cells are capable of binding soluble plasma fibrinogen, whereas integrins expressed on resting leukocytes do not bind soluble protein. 1,8,9 The prerequisite for its binding is activation of leukocytes with agonists that induce conformational changes in integrins and their transition into a high-affinity state. 10 The ability of surface-bound fibrinogen to support adhesion of resting leukocytes, as well as of other cells such as platelets, is incompletely understood but is believed to derive from its capacity to induce integrin clustering. In addition, the conformational changes in fibrinogen, which occur on its immobilization or transformation into fibrin, and which are associated with unmasking of integrin binding sites, can contribute to adhesion of unstimulated cells. 11 Although fibrin clots and deposits of fibrinogen are highly adhesive for resting leukocytes in vitro, they seem to be much less adhesive in vivo, at least in the first hours after thrombus formation. Several studies using experimental models of thrombosis have shown that few leukocytes adhe...

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On the aggregation of fibrinogen molecules

Cited by 21 publications

References 14 publications

Concentration of protein in fibrin fibers and fibrinogen polymers determined by refractive index matching

Concentration of protein in fibrin fibers and fibrinogen polymers determined by refractive index matching

The Assembly of Nonadhesive Fibrinogen Matrices Depends on the αC Regions of the Fibrinogen Molecule

Antiadhesive effect of fibrinogen: a safeguard for thrombus stability

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