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Thrombosis Research Section Faculty
Full-Time Faculty (Primary Appointment)
Research Interests:
My research focuses on the role of specialized membrane microdomains,
known as lipid rafts, in platelet activation. Lipid rafts are dynamic
assemblies of cholesterol and sphingolipids that are more ordered
in structure than the rest of the plasma membrane. They are believed
to act as "platforms" for signal transduction, by selectively attracting
certain molecules while excluding others. We have recently demonstrated
a critical role for lipid rafts in platelet adhesion and post adhesion
signaling via the platelet glycoprotein (GP) Ib-IX-V complex, the
receptor that mediates the initial interactions of platelets with
the blood vessel wall. The investigation of the contribution of lipid
rafts to platelet physiology may provide further insights into the
role of platelets in thrombosis.
Selected References:
1. Shrimpton, CN., Wolfson, AJ., Smith, AI. and Lew RA. Regulators
of the neuropeptide-degrading enzyme EC 3.4.24.15 (thimet oligopeptidase),
in cerebrospinal fluid. J. Neurosci. Res. (In Press).
2. Baglia, FA., Shrimpton, CN., Lopez, JA. and Walsh PN (2003). The
glycoprotein Ib-IX-V complex mediates localization of factor XI to
lipid rafts on the platelet membrane. J. Biol. Chem. (In Press).
3. Dong JF, Moake JL, Nolasco L, Bernardo A, Arceneaux W, Shrimpton
CN, Schade AJ, McIntire LV, Fujikawa K, Lopez JA. (2002) ADAMTS-13
rapidly cleaves newly secreted ultralarge von Willebrand factor multimers
on the endothelial surface under flowing conditions. Blood
100:4033-9.
4. Shrimpton, CN., Borthakur G., Larrucea, S., Cruz, MA., Dong, JF.
and Lopez, JA. (2002) Localization of the adhesion receptor glycoprotein
Ib-IX-V complex to lipid rafts is required for platelet adhesion and
activation. J Exp Med. 196:1057-66
5. Tullai JW, Cummins PM, Pabon A, Roberts JL, Lopingco MC, Shrimpton
CN, Smith AI, Martignetti JA, Ferro ES, Glucksman MJ. (2000) The neuropeptide
processing enzyme EC 3.4.24.15 is modulated by protein kinase A phosphorylation.
J Biol Chem 275:36514-22
6. Smith, AI., Shrimpton CN., Norman, IJ., Clarke, IJ., Wolfson,
AJ. and Lew RA. (2000) Neuropeptidases regulating gonadal function.
Biochem. Soc. Trans. 28:430-4.
7. Shrimpton, CN., Abbenante., Lew RA. and Smith. (2000) Development
and characterization of novel potent and stable inhibitors of endopeptidase
EC 3.4.24.15. Biochem. J. 345, 351-356.
8. Smith, AI., Lew. RA., Shrimpton, CN., Evans, RG. And Abbenante,
G. (2000) A novel stable inhibitor of endopeptidase EC 3.4.24.15 and
endopeptidase EC3.4.24.16 potentiates bradykinin-induced hypotension.
Hypertension 35, 626-630.
9. Shrimpton, C.N., Glucksman, M.J., Lew, R.A., Tullai, J.W., Marguiles,
E.H., Roberts, J.L. and Smith, A.I. (1997) Thiol Activation of Endopeptidase
EC 3.4.24.15: A Novel Mechanism for the Regulation of Catalytic Activity.
J. Biol. Chem. 272(28), 17395-17399
10. Wolfson, A.J., Shrimpton, C.N., Lew, R.A. and Smith, A.I. (1996)
Differential Activation of Endopeptidase EC 3.4.24.15 towards Natural
and Synthetic Substrates by Metal Ions. Biochem. Biophys. Res.
Commun. 229, 341-348
Book Chapters:
1. Corie N. Shrimpton, Karine Gousset, Fern Tablin and Jose A. Lopez.
Preparation and analysis of platelet lipid rafts. In: Platelets and
Megakaryocytes. Methods in Molecular Biology. (In Press)
2. Corie N. Shrimpton, Robert K. Andrews, Jose A. Lopez and Michael
C. Berndt. Qualitative platelet disorders: Congenital disorders of
platelets. In: Thrombosis and Hemorrhage. Third Edition. J.
Loscalzo and AI. Schafer (eds.) Williams and Wilkins. 2002.
 ©1995-2003
Baylor College of Medicine
Email: medicine@bcm.tmc.edu
URL: http://public.bcm.tmc.edu/medicine/shrimpton.htm (Modified: June 3, 2003)
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