Bio
In 1999, Dr. Rinku Majumder received her Doctorate in Biochemistry from the Bose Institute
in India. Subsequently, from 1999-2003 she performed postdoctoral studies in the
Department of Biochemistry & Biophysics at the University of North Carolina at Chapel
Hill. In 2003, Dr. Majumder was promoted to the position of Research Assistant Professor,
and in 2010 she was further promoted to Research Associate Professor at the University
of North Carolina. In 2015, Dr. Majumder was appointed Associate Professor in the
Department of Biochemistry & Molecular Biology at LSUHSC in New Orleans. Dr. Majumder
currently serves as a permanent member of the American Heart Association Study Section
Review Committee for basic thrombosis research and she serves on the National Institutes
of Health VA merit award study section.
Education
PhD Biochemistry
Research Interests
From the beginning of her postdoctoral studies, Dr. Majumder has investigated numerous
questions regarding the regulation of blood clotting and diseases arising from deficiencies
in the presence of various clotting factors and in regulation of their activities.
Notably, Dr. Majumder was a key contributor to work that overturned the prevailing
paradigm regarding the role of platelet membranes in regulating thrombin generation.
Previously, it was accepted that the membrane itself triggers prothrombin activation
to thrombin. Dr. Majumder and co-workers demonstrated that soluble phosphatidylserine
mimics recapitulated all of the properties of the membrane, thus proving that phosphatidylserine,
and not the membrane surface, regulates thrombin formation. The technology employed
in these studies is now patented, and it has spawned a biotechnology company that
is developing soluble phospholipid mimics for use in clinical coagulation assays.
More recently, Dr. Majumder's research has focused on development of new, more effective
therapeutics for thrombotic diseases and hemophilia. Her group was the first to discover
a previously unknown function for Protein S, an anticoagulant that, despite 30 years
of research by others, remained poorly characterized. Dr. Majumder's group discovered
that Protein S inhibits activated Factor IX, which, in turn, inhibits thrombin formation.
This newly recognized function of Protein S is the basis for creating new hemostasis
therapies, as described under current research.
NIH Biosketch
