Nanoscale probing reveals that reduced stiffness of clots from fibrinogen lacking 42 N-terminal Bbeta-chain residues is due to the formation of abnormal oligomers. Export

@article{citeulike:4209360, abstract = {Removal of Bbetal-42 from fibrinogen by Crotalus atrox venom results in a molecule lacking fibrinopeptide B and part of a thrombin binding site. We investigated the mechanism of polymerization of desBbeta1-42 fibrin. Fibrinogen trinodular structure was clearly observed using high resolution noncontact atomic force microscopy. E-regions were smaller in desBbeta1-42 than normal fibrinogen (1.2 nm +/- 0.3 vs. 1.5 nm +/- 0.2), whereas there were no differences between the D-regions (1.7 nm +/- 0.4 vs. 1.7 nm +/- 0.3). Polymerization rate for desBbeta1-42 was slower than normal, resulting in clots with thinner fibers. Differences in oligomers were found, with predominantly lateral associations for desBbeta1-42 and longitudinal associations for normal fibrin. Clot elasticity as measured by magnetic tweezers showed a G' of approximately 1 Pa for desBbeta1-42 compared with approximately 8 Pa for normal fibrin. Spring constants of early stage desBbeta1-42 single fibers determined by atomic force microscopy were approximately 3 times less than normal fibers of comparable dimensions and development. We conclude that Bbeta1-42 plays an important role in fibrin oligomer formation. Absence of Bbeta1-42 influences oligomer structure, affects the structure and properties of the final clot, and markedly reduces stiffness of the whole clot as well as individual fibrin fibers.}, author = {Abou-Saleh, R. H. and Connell, S. D. and Harrand, R. and Ajjan, R. A. and Mosesson, M. W. and Smith, D. A. and Grant, P. J. and Ari\"{e}ns, R. A.}, citeulike-article-id = {4209360}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.bpj.2008.12.3913}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/19289066}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=19289066}, day = {18}, doi = {10.1016/j.bpj.2008.12.3913}, issn = {1542-0086}, journal = {Biophysical journal}, keywords = {blood, clot, simon}, month = {March}, number = {6}, pages = {2415--2427}, posted-at = {2009-03-23 13:18:18}, priority = {2}, title = {Nanoscale probing reveals that reduced stiffness of clots from fibrinogen lacking 42 N-terminal Bbeta-chain residues is due to the formation of abnormal oligomers.}, url = {http://dx.doi.org/10.1016/j.bpj.2008.12.3913}, volume = {96}, year = {2009} }

TY - JOUR ID - citeulike:4209360 L3 - citeulike-article-id:4209360 N2 - Removal of Bbetal-42 from fibrinogen by Crotalus atrox venom results in a molecule lacking fibrinopeptide B and part of a thrombin binding site. We investigated the mechanism of polymerization of desBbeta1-42 fibrin. Fibrinogen trinodular structure was clearly observed using high resolution noncontact atomic force microscopy. E-regions were smaller in desBbeta1-42 than normal fibrinogen (1.2 nm +/- 0.3 vs. 1.5 nm +/- 0.2), whereas there were no differences between the D-regions (1.7 nm +/- 0.4 vs. 1.7 nm +/- 0.3). Polymerization rate for desBbeta1-42 was slower than normal, resulting in clots with thinner fibers. Differences in oligomers were found, with predominantly lateral associations for desBbeta1-42 and longitudinal associations for normal fibrin. Clot elasticity as measured by magnetic tweezers showed a G' of approximately 1 Pa for desBbeta1-42 compared with approximately 8 Pa for normal fibrin. Spring constants of early stage desBbeta1-42 single fibers determined by atomic force microscopy were approximately 3 times less than normal fibers of comparable dimensions and development. We conclude that Bbeta1-42 plays an important role in fibrin oligomer formation. Absence of Bbeta1-42 influences oligomer structure, affects the structure and properties of the final clot, and markedly reduces stiffness of the whole clot as well as individual fibrin fibers. IS - 6 JF - Biophysical journal SN - 1542-0086 EP - 2427 TI - Nanoscale probing reveals that reduced stiffness of clots from fibrinogen lacking 42 N-terminal Bbeta-chain residues is due to the formation of abnormal oligomers. VL - 96 SP - 2415 KW - blood KW - clot KW - simon AU - Abou-Saleh, RH AU - Connell, SD AU - Harrand, R AU - Ajjan, RA AU - Mosesson, MW AU - Smith, DA AU - Grant, PJ AU - Ariëns, RA PY - 2009/03/18/ UR - http://dx.doi.org/10.1016/j.bpj.2008.12.3913 ER -