Jun Yoshioka
CUNY City College, NY·Physiology
Diabetes damages the heart even without blocked arteries, a condition called diabetic cardiomyopathy. Its cause is still unclear.
- Fields
Physiology
Medicine & Clinical Research
Biochemistry
- Topics
diabetic cardiomyopathy
diabetes mellitus
type 1 diabetes
- Grants
- 1 known grant, through Dec 2027
What they work on
- Test whether Arrdc4, an adaptor protein switched on by high glucose, is controlled by the cell's glucose-sensing gene machinery, linking high blood sugar to ER stress in cardiomyocytes.
- Determine whether Arrdc4 makes heart muscle cells vulnerable to ER stress by blocking the glucose transporter GLUT1 and causing an energy shortage, or through mechanisms beyond GLUT1.
- Characterize heart metabolism in a type 2 diabetic mouse model and test whether Arrdc4-knockout hearts are protected from cell death caused by misfolded proteins.
- Use inducible, tissue-specific Arrdc4-knockout mice to test whether protection comes from the heart itself or from skeletal muscle blood sugar control, focusing on exercise intolerance.
More about the research
One clue is ER stress. This is a stress response that switches on when the endoplasmic reticulum (ER), the cell's protein-folding compartment, stops working properly. ER stress has been linked to heart cell death in diabetes. Still, how high blood sugar sets off this stress in heart muscle cells has not been worked out.
Why it matters
Heart disease is a major complication of diabetes, yet its underlying cause is poorly understood. By defining how the Arrdc4–GLUT1 pathway links high blood sugar to heart cell stress and death, this work could reveal new ways to protect heart muscle in people with type 1 or type 2 diabetes. It may also help address exercise intolerance, which predicts poor prognosis in diabetes.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Federica Brandizzi
Michigan State University, MI·Biology
Determine how IRE1, the most conserved UPR sensor and both a protein kinase and an RNA-cutting enzyme, drives protein phosphorylation changes that support growth and relieve ER stress in Arabidopsis.
Smriti Sangwan
Northwestern University, IL·Biochemistry·Early-career
Determine how IRE1, an ER stress sensor, physically connects to the protein-making translational machinery, using single-particle cryo-electron microscopy to resolve the 3D structures involved.
Malavika Raman
Tufts University, MA·Biochemistry
Identify how UBXN1 represses translation (protein synthesis at the ribosome), testing whether it binds specific ribosomal proteins in a ubiquitin-dependent way.
The school
CUNY City College: 9 labs on PI Pages, $72M a year on research, 31 research doctorates a year.
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