Anthony Cammarato
Johns Hopkins University, MD·Physiology
Each heartbeat depends on a tiny molecular machine inside muscle cells. Thin filaments — chains of the protein actin wrapped by regulatory proteins — act as a switch that decides when the muscle can pull and when it must relax.
- Fields
Physiology
Biophysics
Medicine & Clinical Research
- Topics
cardiomyopathy
thin filament
actin
- Grants
- 1 known grant, through Dec 2026
What they work on
- Test whether acetylation of actin residues K326 and K328 — sites previously shown by this group to bind and orient the regulatory protein tropomyosin — shifts tropomyosin away from its contraction-blocking position and enhances cardiac performance, using recombinant human proteins, flies and mice.
- Determine how specific cardiomyopathy mutations in actin and troponin T disrupt distinct contacts with tropomyosin, and how these differences alter myocardial relaxation and force production to produce different cardiac diseases, using new Drosophila models complemented by mouse models.
- Express human actin variants in Drosophila for purification and biophysical analysis, enabling direct structural and mechanical comparison of disease-causing and modified actins.
- Test whether pseudo-acetylation of actin improves dilated cardiomyopathy while aggravating hypertrophic cardiomyopathy in fly and mouse models, using high-speed video of beating hearts, cryo-electron microscopy, computational modeling and mechanical assays.
More about the research
The individual parts must shift against each other in a precise choreography. Inherited mutations at the seams where these parts touch cause cardiomyopathies, diseases in which the heart enlarges, stiffens or weakens. Chemical modifications added to the proteins after they are made can also change how the switch behaves. This work asks how both kinds of change alter the machine's mechanics and tip the heart toward disease.
Why it matters
Inherited mutations in thin filament proteins cause dilated and hypertrophic cardiomyopathy, forms of heart muscle disease that can lead to heart failure and sudden death. Mapping how particular mutations and chemical modifications of actin change contraction and relaxation would connect specific genotypes to specific disease patterns and indicate whether boosting contractility through actin acetylation would help or harm a given patient's form of disease.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
E. Ostap
University of Pennsylvania, PA·Biophysics
Determine the structural basis of myosin force sensing by testing conserved residues that tune tension sensitivity in Myo1b and Myo1c, using engineered motors, microsecond optical trapping and cryo-EM.
Ju Chen
University of California-San Diego, CA·Physiology
Test whether mini-ALPK3, a shortened version of the ALPK3 kinase delivered by the muscle-targeting MyoAAV virus on the first day of life, prevents cardiomyopathy and early death in Alpk3 knockout mice.
Ryan Stowers
University of California-Santa Barbara, CA·Biomedical Engineering
Determine whether cardiomyopathy-driven remodeling of the extracellular matrix alters myocardial viscoelasticity, by mechanically testing human DCM and HCM heart tissue and pig disease-model tissue.
The school
Johns Hopkins University: 100 labs on PI Pages, $4.1B a year on research, 622 research doctorates a year.
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