Lingjun Li

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Academic Career Length

24Years (2003-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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20 November 2017 in Analytical Chemistry

Journal Article

Mass Spectrometry Imaging: A Review of Emerging Advancements and Future Insights

Amanda Rae Buchberger

Kellen DeLaney

Jillian Johnson

Lingjun Li

23 October 2017 in Nature Cell Biology

Journal Article

PKM2 methylation by CARM1 activates aerobic glycolysis to promote tumorigenesis

Fabao Liu

Fengfei Ma

Yuyuan Wang

Ling Hao

Hao Zeng

Wei Xu

Metabolic reprogramming is a hallmark of cancer. Herein we discover that the key glycolytic enzyme pyruvate kinase M2 isoform (PKM2), but not the related isoform PKM1, is methylated by co-activator-associated arginine methyltransferase 1 (CARM1). PKM2 methylation reversibly shifts the balance of metabolism from oxidative phosphorylation to aerobic glycolysis in breast cancer cells. Oxidative phosphorylation depends on mitochondrial calcium concentration, which becomes critical for cancer cell survival when PKM2 methylation is blocked. By interacting with and suppressing the expression of inositol-1,4,5-trisphosphate receptors (InsP₃Rs), methylated PKM2 inhibits the influx of calcium from the endoplasmic reticulum to mitochondria. Inhibiting PKM2 methylation with a competitive peptide delivered by nanoparticles perturbs the metabolic energy balance in cancer cells, leading to a decrease in cell proliferation, migration and metastasis. Collectively, the CARM1–PKM2 axis serves as a metabolic reprogramming mechanism in tumorigenesis, and inhibiting PKM2 methylation generates metabolic vulnerability to InsP₃R-dependent mitochondrial functions.

11 July 2018 in Scientific Reports

Journal Article

Extracellular matrix scaffold and hydrogel derived from decellularized and delipidized human pancreas

Sara Dutton Sackett

Daniel M. Tremmel

Fengfei Ma

Austin K. Feeney

Rachel M. Maguire

Jon S. Odorico

Extracellular matrix (ECM) plays an important developmental role by regulating cell behaviour through structural and biochemical stimulation. Tissue-specific ECM, attained through decellularization, has been proposed in several strategies for tissue and organ replacement. Decellularization of animal pancreata has been reported, but the same methods applied to human pancreas are less effective due to higher lipid content. Moreover, ECM-derived hydrogels can be obtained from many decellularized tissues, but methods have not been reported to obtain human pancreas-derived hydrogel. Using novel decellularization methods with human pancreas we produced an acellular, 3D biological scaffold (hP-ECM) and hydrogel (hP-HG) amenable to tissue culture, transplantation and proteomic applications. The inclusion of a homogenization step in the decellularization protocol significantly improved lipid removal and gelation capability of the resulting ECM, which was capable of gelation at 37 °C in vitro and in vivo, and is cytocompatible with a variety of cell types and islet-like tissues in vitro. Overall, this study demonstrates the characterisation of a novel protocol for the decellularization and delipidization of human pancreatic tissue for the production of acellular ECM and ECM hydrogel suitable for cell culture and transplantation applications. We also report a list of 120 proteins present within the human pancreatic matrisome.

19 July 2024 in Nature Chemical Biology

Journal Article

Lysine l-lactylation is the dominant lactylation isomer induced by glycolysis

Di Zhang

Jinjun Gao

Zhijun Zhu

Qianying Mao

Zhiqiang Xu

Yingming Zhao

+11

Lysine l-lactylation (K_l-la) is a novel protein posttranslational modification (PTM) driven by l-lactate. This PTM has three isomers: K_l-la, N-ε-(carboxyethyl)-lysine (K_ce) and d-lactyl-lysine (K_d-la), which are often confused in the context of the Warburg effect and nuclear presence. Here we introduce two methods to differentiate these isomers: a chemical derivatization and high-performance liquid chromatography analysis for efficient separation, and isomer-specific antibodies for high-selectivity identification. We demonstrated that K_l-la is the primary lactylation isomer on histones and dynamically regulated by glycolysis, not K_d-la or K_ce, which are observed when the glyoxalase system was incomplete. The study also reveals that lactyl-coenzyme A, a precursor in l-lactylation, correlates positively with K_l_-la levels. This work not only provides a methodology for distinguishing other PTM isomers, but also highlights K_l-la as the primary responder to glycolysis and the Warburg effect.

10 July 2017 in Journal of the American Society for Mass Spectrometry

Journal Article

Electron-Transfer/Higher-Energy Collision Dissociation (EThcD)-Enabled Intact Glycopeptide/Glycoproteome Characterization

Qing Yu

Bowen Wang

Zhengwei Chen

Go Urabe

Matthew S. Glover

Lingjun Li

17 July 2024 in npj Imaging

Journal Article

Mass spectrometry imaging for spatially resolved multi-omics molecular mapping

Hua Zhang

Kelly H. Lu

Malik Ebbini

Penghsuan Huang

Haiyan Lu

Lingjun Li

The recent upswing in the integration of spatial multi-omics for conducting multidimensional information measurements is opening a new chapter in biological research. Mapping the landscape of various biomolecules including metabolites, proteins, nucleic acids, etc., and even deciphering their functional interactions and pathways is believed to provide a more holistic and nuanced exploration of the molecular intricacies within living systems. Mass spectrometry imaging (MSI) stands as a forefront technique for spatially mapping the metabolome, lipidome, and proteome within diverse tissue and cell samples. In this review, we offer a systematic survey delineating different MSI techniques for spatially resolved multi-omics analysis, elucidating their principles, capabilities, and limitations. Particularly, we focus on the advancements in methodologies aimed at augmenting the molecular sensitivity and specificity of MSI; and depict the burgeoning integration of MSI-based spatial metabolomics, lipidomics, and proteomics, encompassing the synergy with other imaging modalities. Furthermore, we offer speculative insights into the potential trajectory of MSI technology in the future.

About Me

Lingjun Li received her BE degree in Environmental Analytical Chemistry from Beijing Polytechnic University and a PhD degree in Analytical Chemistry/Biomolecular Chemistry from the University of Illinois at Urbana-Champaign in 2000. She conducted three-way postdoctoral research at the Pacific Northwest National Laboratory, Brandeis University, and the University of Illinois before starting her faculty position at the University of Wisconsin-Madison in 2002. She currently holds joint appointments in the School of Pharmacy and Department of Chemistry, as well as being named Charles Melbourne Johnson Distinguished Chair in Pharmaceutical Sciences and Vilas Distinguished Achievement Professor of Pharmaceutical Sciences and Chemistry. Her research interests are in analytical neurochemistry, neuroproteomics, and biological mass spectrometry. She has been recognized with numerous awards, including the ASMS Research Award, NSF CAREER Award, Sloan Fellowship, PittCon Achievement Award, and ASMS Biemann Medal, and was named on the Analytical Scientist Power List four times. She was named one of the Top 50 most influential women in the analytical sciences and was recognized as one of the Top 20 Human Health Heroes worldwide for their impact through analytical science. She is currently serving as an Associate Editor for the Journal of the American Society for Mass Spectrometry (JASMS) and is on the Advisory Board for Analytical and Bioanalytical Chemistry and Mass Spectrometry Reviews.

Lingjun Li

Lingjun Li

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