Polyphosphate and Polyphosphate Derivatives - updated

Overview

• Novel regulator of fibrin function
• Useful tool for studying blood clotting

Background

Dr. Morrissey's lab makes carefully size-fractionated preparations of inorganic polyphosphate that are useful to researchers working to understand the biological functions of this polymer. The lab also makes modified forms of polyphosphate in which organic molecules such as biotin are covalently attached to the terminal phosphates of polyphosphate, typically by phosphoramidate linkages. Many of these polyphosphate preparations are not commercially available.

Additional Details

Request NowP100 (Phosphate, Short chain)P700 (Phosphate, Long chain)Biotinylated  Phosphate (Short chain)Biotinylated  Phosphate (Long chain)

References

[1] Smith, S. A., Choi, S. H., Davis-Harrison, R., Huyck, J.,
Boettcher, J., Rienstra, C. M., and Morrissey, J. H. (2010) Polyphosphate
exerts differential effects on blood clotting, depending on polymer size, Blood 116, 4353-4359.
[2] Choi, S. H., Collins, J. N., Smith, S. A., Davis-Harrison,
R. L., Rienstra, C. M., and Morrissey, J. H. (2010) Phosphoramidate end
labeling of inorganic polyphosphates: facile manipulation of polyphosphate for
investigating and modulating its biological activities, Biochemistry 49,
9935-9941.
[3] Choi, S. H., Smith, S. A., and Morrissey, J. H. (2011)
Polyphosphate is a cofactor for the activation of factor XI by thrombin, Blood 118, 6963-6970.
[4] Smith, S. A., Choi, S. H., Collins, J. N., Travers, R. J.,
Cooley, B. C., and Morrissey, J. H. (2012) Inhibition of polyphosphate as a
novel strategy for preventing thrombosis and inflammation, Blood 120, 5103-5110.
[5] Puy, C., Tucker, E. I., Wong, Z. C., Gailani, D., Smith, S.
A., Choi, S. H., Morrissey, J. H., Gruber, A., and McCarty, O. J. (2013) Factor
XII promotes blood coagulation independent of factor XI in the presence of
long-chain polyphosphates, J Thromb Haemost
11, 1341-1352.
[6] Choi, S. H., Smith, S. A., and Morrissey, J. H. (2014)
Polyphosphate accelerates factor V activation by factor XIa, Thromb Haemost 113.
[7] Wijeyewickrema, L. C., Lameignere, E., Hor, L., Duncan, R.
C., Shiba, T., Travers, R. J., Kapopara, P. R., Lei, V., Smith, S. A., Kim, H.,
Morrissey, J. H., Pike, R. N., and Conway, E. M. (2016) Polyphosphate is a
novel cofactor for regulation of complement by a serpin, C1 inhibitor, Blood 128, 1766-1776.
[8] Zilberman-Rudenko, J., Reitsma, S. E., Puy, C., Rigg, R. A.,
Smith, S. A., Tucker, E. I., Silasi, R., Merkulova, A., McCrae, K. R., Maas,
C., Urbanus, R. T., Gailani, D., Morrissey, J. H., Gruber, A., Lupu, F.,
Schmaier, A. H., and McCarty, O. J. T. (2018) Factor XII Activation Promotes
Platelet Consumption in the Presence of Bacterial-Type Long-Chain Polyphosphate
In Vitro and In Vivo, Arterioscler Thromb
Vasc Biol 38, 1748-1760.
[9] Wang, Y., Ivanov, I., Smith, S. A., Gailani, D., Morrissey,
J. H., Baker, C. J., Smith, S. A., and Morrissey, J. H. (2019) Polyphosphate,
Zn(2+) and high-molecular-weight kininogen modulate individual reactions of the
contact pathway of blood clotting, J
Thromb Haemost 3, 18-25.