Dr. Ping’s current
research program focuses on the understanding of proteome biology in
cardiovascular medicine, with a particular interest on alterations of
subproteomes encoding signaling pathways and cellular organelles during
cardiac pathogenesis. Her research group investigates specific areas in:
in the Heart:
Cardiac mitochondria proteome and phosphoproteome: The
subproteome composition and post-translational modification profiles
define the functional state of the cardiac mitochondria. My group
employs state-of-the-art mass spectrometry expertise to interrogate
their dynamics in health and diseases. Mitochondrial proteome
turnover: The body of mitochondrial proteome is continuously
replaced. Such kinetics varies greatly among distinct proteins and
even for the same protein under different pathophysiological states.
A novel strategy to systematically characterize their perturbations
has been devised in our research group. Mitochondrial
permeability transition (MPT): MPT is caused by the opening
of permeability transition pores in the inner mitochondrial membrane
and may lead to cell death. A multi-disciplinary approach using an
array of omics tools is applied to characterize MPT regulation
(i.e., their interacting partners) in the healthy and diseased
Proteasome Biology in
Proteasome function: Our research group has
established necessary toolboxes for the investigation of
ubiquitin-proteasome-dependent degradation of proteins in the heart.
We combine both biochemical and proteomic technologies to
investigate 20S and 26S proteasome complexes in the normal,
protected, and diseased heart. Proteasome heterogeneity:
A heterogenic population of proteasome complexes exists in the
heart, the composition of which is subject to change upon stress. A
powerful technical platform has been assembled to characterize each
subpopulation individually with its native constituents, which
enables us to pinpoint specific changes. Proteasome regulation
by post-translational modifications: The functional dynamics
of the proteasome complexes are regulated via various forms of
Protein atlas Knowledgebase (COPaKB): We have developed a COPa
knowledgebase, a specialized resource for cardiac proteome biology.
It integrates orthogonal sets of proteome knowledge and biomedical
insights into context, while providing bioinformatics tools and web
portals to efficiently disseminate proteomics proficiencies. It
bridges data-driven proteomic discoveries and hypothesis-driven
investigations, facilitates synergistic research paradigm across the
research community, thereby advancing cardiovascular biology and
1. Deng N, Zhang J,
Zong C, Wang Y, Lu H, Yang P, Wang W, Young GW, Wang Y, Korge P,
Lotz C, Doran P, Liem DA, Apweiler R, Weiss JN, Duan H,
Ping P. Phosphoproteome Analysis Reveals Regulatory Sites in Major
pathways of Cardiac Mitochondria. Mol Cell Proteomics.
2. Ping P. Getting to the Heart of Proteomics. New Eng J Med.
2009; 360: 532-534.
3. Zong C, Gomes AV, Drews O, Li X, Young GW, Berhane B, Qiao X,
French SW, Bardag-Gorce F, Ping P. Regulation of Murine Cardiac
20S Proteasomes: Role of Associating Partners. Circ
4. Gomes AV, Zong C, Edmondson RD, Li X, Stefani E, Zhang J,
Jones RC, Thyparambil S, Ping P. Mapping the murine cardiac 26S
proteasome complexes. Circ Res. 2006; 99:362-371.
5. Weiss JN, Korge P, Honda HM, Ping P. Role of the
mitochondrial permeability transition in myocardial disease.
Circ Res. 2003; 93:292-301.
6. Edmondson RD, Vondriska TM, Biederman KJ, Zhang J, Jones RC,
Pisano MR, Ping P. PKC complexes include metabolic- and
translation-related proteins. Mol Cell Proteomics.
7. Baines CP, Zhang J, Wang GW, Zheng YT, Xiu JX, Cardwell EM,
Bolli R, Ping P. Mitochondrial PKC and MAPK form signaling
modules. Circ Res. 2002;90:390-397.
8. Ping P, Song C, Zhang J, Guo Y, Cao X, Li R, Vondriska TM,
Pass JM, Tang XL, Pierce WM, Bolli R. Formation of PKCε-Lck
signaling modules confers cardioprotection. J Clin Invest.
9. Ping P, Zhang J, Pierce W, Bolli R. Functional proteomic
analysis of PKCε signaling complexes in the normal heart and
during cardioprotection. Circ Res. 2001;88:59-62.
10. Ping P, Takano H, Zhang J, Tang XL, Qiu Y, Li R, Banerjee S,
Dawn B, Bolli R. Isoform-selective activation of PKCε by nitric
oxide in the heart of conscious rabbits. Circ Res.
11. Ping P, Zhang J, Zheng YT, Li R, Dawn B, Takano H,
Balafanova Z, Bolli R. Demonstration of PKCε-dependent
activation of Src and Lck tyrosine kinases in preconditioning.
Circ Res. 1999;85:542-50.
12. Ping P, Qiu Y, Zhang J, Tang XL, Manchikalapudi S, Bolli R.
Direct evidence for an essential role of PKC in the development
of late preconditioning in rabbits. J Clin Invest
13. Ping P, Gao M, Post S, Insel PA, Tang R, Hammond HK.
Increased expression of adenylylcyclase type VI proportionately
increases β-adrenergic receptor-stimulated cAMP in neonatal rat
cardiac myocytes. Proc Natl Acad Sci USA 1998;95:1038-1043.
14. Ping P, Zhang J, Qiu Y, Tang XL, Cao X, Bolli R. Ischemic
preconditioning induces selective translocation of PKC isoform ε
and in the heart of conscious rabbits. Circ Res
15. Giordano F, Ping P, Mckirnan D, Nozaki S, DeMaria A,
Dillmann W, Mathieu-Costello O, Hammond HK. Intracoronary gene
transfer of fibroblast growth factor-5 increases blood flow and
contractile function in an ischemic region of the heart. Nature