Author Correction: Soft fibrin gels promote selection and growth of tumorigenic cells

SummaryThis study was performed to quantitate the impact of several glycosaminoglycans (GAG) on fibrin assembly and structure. Gel formation was monitored as the increase in optical density at 633 nm subsequent to thrombin (2 NIH u/ml) or atroxin (0.10 mg/ml) addition to solutions of buffered fibrinogen (1 mg/ml) or plasma. Gel absorbance was measured as a function of wavelength (400 to 800 nm) and gel fiber diameter and mass/length ratio (μ) were calculated. Chondroitin sulfate A (CSA)shortened the lag phase, enhanced the maximal rate of turbidity increase, and increased the final gel turbidity of fibrin gels formed by thrombin or atroxin. CSA (16 mg/ml) increased fiber μ from 1.3 to 3.1 × 1013 dalton/cm and fiber radius from 6.0 to 8.6 × 10-6 cm in thrombin-induced gels. μ increased from 0.7 to 2.7 × 1013 dalton/cm and fiber radius from 4 to 7.8 × 10-6 cm for atroxin-induced gels. Above 16 mg/ml, CSA caused fibrinogen precipitation in purified solutions but not in plasma. CSA inhibited thrombin-induced plasma clotting of plasma but effects in atroxin-mediated plasma gels paralleled those seen in purified solutions. Chondroitin sulfate B (CSB)-induced changes in fibrin were similar but slightly less dramatic than those seen with CSA. μ increased from 0.9 to 2.0 × 1013 dalton/cm for thrombin-induced fibrin gels and from 0.8 to 2.3 × 1013 dalton/cm for atroxininduced gels. Low molecular weight heparin (Mr = 5100) slowed fibrin assembly and reduced fiber size by 50% in thrombininduced gels. Changes in μ of atroxin-induced gels were much less pronounced (<20%). This study documents pronounced GAGinduced changes in fibrin structure which vary with GAG species and may mediate significant physiologic functions.

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Faculty Opinions recommendation of Rapid formation of functional muscle in vitro using fibrin gels.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1024121.286739 ◽

2005 ◽

Author(s):

Mark Hargreaves

Keyword(s):

Fibrin Gels ◽

Rapid Formation

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Peppers: A “Hot” Natural Source for Antitumor Compounds

Molecules ◽

10.3390/molecules26061521 ◽

2021 ◽

Vol 26 (6) ◽

pp. 1521

Author(s):

Micael Rodrigues Cunha ◽

Maurício Temotheo Tavares ◽

Thais Batista Fernandes ◽

Roberto Parise-Filho

Keyword(s):

Cell Death ◽

Cellular Responses ◽

Biological Applications ◽

Traditional Use ◽

Cytotoxic Effects ◽

Antiproliferative Effects ◽

Naturally Occurring ◽

Antitumor Compounds ◽

Tumorigenic Cells ◽

Ancient Civilizations

Piper, Capsicum, and Pimenta are the main genera of peppers consumed worldwide. The traditional use of peppers by either ancient civilizations or modern societies has raised interest in their biological applications, including cytotoxic and antiproliferative effects. Cellular responses upon treatment with isolated pepper-derived compounds involve mechanisms of cell death, especially through proapoptotic stimuli in tumorigenic cells. In this review, we highlight naturally occurring secondary metabolites of peppers with cytotoxic effects on cancer cell lines. Available mechanisms of cell death, as well as the development of analogues, are also discussed.

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Soft materials to treat central nervous system injuries: Evaluation of the suitability of non-mammalian fibrin gels

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research ◽

10.1016/j.bbamcr.2009.01.007 ◽

2009 ◽

Vol 1793 (5) ◽

pp. 924-930 ◽

Cited By ~ 32

Author(s):

Raivo Uibo ◽

Ivo Laidmäe ◽

Evelyn S. Sawyer ◽

Lisa A. Flanagan ◽

Penelope C. Georges ◽

...

Keyword(s):

Central Nervous System ◽

Nervous System ◽

Soft Materials ◽

Fibrin Gels

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Soft gels select tumorigenic cells

Nature Materials ◽

10.1038/nmat3388 ◽

2012 ◽

Vol 11 (8) ◽

pp. 662-663 ◽

Cited By ~ 8

Author(s):

Jae-Won Shin ◽

Dennis E. Discher

Keyword(s):

Tumorigenic Cells ◽

Soft Gels

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Immobilization of Aprotinin to Fibrinogen as a Novel Method for Controlling Degradation of Fibrin Gels

Bioconjugate Chemistry ◽

10.1021/bc060265o ◽

2007 ◽

Vol 18 (3) ◽

pp. 695-701 ◽

Cited By ~ 24

Author(s):

Jason D. Smith ◽

Andrew Chen ◽

Lauren A. Ernst ◽

Alan S. Waggoner ◽

Phil G. Campbell

Keyword(s):

Fibrin Gels ◽

Novel Method

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Role of fibrinopeptide B release: comparison of fibrins produced by thrombin and Ancrod

AJP Heart and Circulatory Physiology ◽

10.1152/ajpheart.1977.232.6.h629 ◽

1977 ◽

Vol 232 (6) ◽

pp. H629-H633 ◽

Cited By ~ 2

Author(s):

L. L. Shen ◽

J. Hermans ◽

J. McDonagh ◽

R. P. McDonagh

Keyword(s):

Elastic Moduli ◽

Slow Release ◽

Control Mechanism ◽

Gelation Time ◽

Fibrin Gels ◽

Lateral Association ◽

Complete Digestion ◽

Low Ionic Strength

The gelation time, opacity, light scattering, and elastic moduli of human fibrin gels clotted in the presence of thrombin, Ancrod, and Reptilase have been compared. At low ionic strength lateral association to thick fibers is observed in all cases. At all ionic strengths thrombin fibrin forms thicker fibers than does Ancrod fibrin. We have demonstrated that an increase in the extent of lateral association is linked to an increase in its velocity and to a decrease in the gelation time. One may consider the removal of fibrinopeptide B to act as a switch: after it is removed fibrin assembles rapidly to thick fibers and gelation is fast; but when this peptide is still attached, there is a slow assembly of thin fibers, and gelation, especially of dilute fibrin, is delayed. We believe that this delay is critical for the complete digestion by plasmin of fibrin formed during in vivo defibrination with Ancrod and of fibrin produced by very small amounts of thrombin (which would still contain fibrinopeptide B), and that slow release of fibrinopeptide B is part of a control mechanism for the regulation of fibrin formation and the prevention of intravascular coagulation.

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