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University of Colorado Denver

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Kristofer S. Fritz, PhD

Assistant Professor of Toxicology, Department of Pharmaceutical Sciences


Kristofer Fritz PhD
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Mailing address:

University of Colorado
Skaggs School of Pharmacy and Pharmaceutical Sciences
Mail Stop C238
12850 E. Montview Blvd. V20-2131
Aurora, CO 80045

Office Location:

Pharmacy and Pharmaceutical Sciences Building (V20)
2nd Floor
Room 2131

Lab Location:

Pharmacy and Pharmaceutical Sciences Building (V20)
2nd Floor
Room 2450G

Contact:

Affiliation:

  • Faculty Member – School of Medicine, Division of Cardiology
  • Board Member - Colorado Biological Mass Spectrometry Society

Training and Education:

  • BS, La Sierra University, Riverside, CA (Biochemistry)
  • PhD, Loma Linda University, Loma Linda, CA (Biochemistry)
  • Postdoctoral Fellow, University of Colorado

Research Interests:

The long-term goal of our research is to elucidate biochemical mechanisms of cellular dysfunction resulting from altered protein post-translational modifications (PTMs). Specifically, our lab focuses on the downstream effects of protein carbonylation due to lipid peroxidation and protein acylation due to altered liver metabolism. Protein carbonylation is examined in the failing human heart through functional assays, proteomics, mass spectrometry, and bioinformatics approaches. Towards this aim, we investigate the role of oxidative stress induced protein carbonylation and the associated alterations to antioxidant and metabolic processes that contribute to the pathogenesis of cardiomyopathy. Protein carbonylation, like other post-translational modifications, is known to alter the structure and function of cellular proteins. By further understanding the biochemical perturbations stemming from oxidative-stress induced changes in protein modifications, we can leverage these new findings to develop therapeutic interventions for heart failure.

As mentioned above, our lab also focuses on studying the metabolic consequences of lysine acetylation on mitochondrial proteins in models of altered liver metabolism. Here, our main goal is to continue to contribute to the discovery that lysine acylation is a crucial post-translational modification on mitochondrial proteins that is required for the proper regulation of metabolic and antioxidant processes within the liver. This project has enabled the Fritz lab to establish cutting-edge proteomics techniques investigating the role of lysine acylation in liver disease.


Publications​​