Dudley K. Strickland, PhD, University of Maryland, Baltimore
Dr. Strickland's laboratory was one of two laboratories to identify the LDL receptor related protein (LRP1) as an hepatic receptor involved in the removal of protease-inhibitor complexes (a2M-protease or serpin-protease). While identifying LRP1, the Strickland laboratory also discovered the 39 kDa Receptor Associated Protein (RAP), a molecular chaperone for this receptor family. We now know that LRP1 is an efficient endocytic and signaling receptor that is widely expressed in the vasculature, in neurons and in inflammatory cells such as macrophages. Ongoing projects in the Strickland laboratory include investigating the role of LRP1 in regulating thrombosis, cell migration, proliferation and signaling events, ultimately altering the pathology of certain diseases such as vascular remodeling, atherosclerosis, and vessel wall pathology.
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References
- Ruiz J, Kouiavskaia D, Migliorini M, Robinson S, Saenko EL, Gorlatova N, Li D, Lawrence D, Hyman BT, Weisgraber KH, Strickland DK. The apoE isoform binding properties of the VLDL receptor reveal marked differences from LRP and the LDL receptor. J Lipid Res. 2005 Aug;46(8):1721-31. Epub 2005 May 1. PubMed PMID: 15863833.
- Prasad JM, Migliorini M, Galisteo R, Strickland DK. Generation of a Potent Low Density Lipoprotein Receptor-related Protein 1 (LRP1) Antagonist by Engineering a Stable Form of the Receptor-associated Protein (RAP) D3 Domain. J Biol Chem. 2015 Jul 10;290(28):17262-8.
