Dean Burkin Ph.D.

Professor; Director, Cellular and Molecular Pharmacology and Physiology Graduate Program

Cellular and Molecular Pharmacology & Physiology | COBRE in Cell Biology | Department of Pharmacology

Dean Burkin

Translational research identifying novel therapies for children with muscular dystrophy. Role of extracellular matrix and integrin signaling in muscle development and disease.

Contact Dean Burkin Ph.D.

Location

Center for Molecular Medicine (CMM)
Room 303C

1664 North Virginia Street
Center for Molecular Medicine
RenoNV 89557
Dean Burkin

Translational research identifying novel therapies for children with muscular dystrophy. Role of extracellular matrix and integrin signaling in muscle development and disease.

Education

  • B.S., 1985, Victoria University of Well, New Zealand, Zoology
  • B.S., 1986, Victoria University of Well, New Zealand, Developmental Biology
  • Ph.D., 1994, University of Colorado, Biochemistry

Biography

Dr. Dean Burkin received his B.Sc. and B.Sc. (1st class Hons) degrees in Developmental Biology and Genetics from Victoria University of Wellington, New Zealand and Ph.D. in Biochemistry and Genetics from the University of Colorado, USA. Dr. Burkin completed postdoctoral training in Genetics, Cell and Molecular Biology at Cambridge University, England and the University of Illinois at Urbana-Champaign.

Research

Translational research identifying novel therapies for children with muscular dystrophy. Role of extracellular matrix and integrin signaling in muscle development and disease.

The primary goal of my research is to understand the role integrin receptors and the extracellular matrix play in neuromuscular development and disease. Using transgenic and knockout mice we have shown that the α7β1 integrin is a major modifier of disease progression in several muscular dystrophies including Duchenne Muscular Dystrophy (DMD) and Merosin-Deficient Congenital Muscular Dystrophy type 1A (MDC1A). These studies support the idea that the α7β1 integrin is a drug target for the treatment of these and potentially other fatal muscle diseases. Using a novel muscle-based assay and high throughput drug discovery, we have recently identified that laminin-111 protein can increase α7 integrin protein in mouse and human muscle cells. We have demonstrated laminin-111 protein therapy can improve muscle repair after damage and prevent muscle disease progression in mouse models of DMD and MDC1A. In addition, we have identified several integrin-enhancing small molecules that may be useful in the treatment of muscle disease and serve as molecular probes to identify and dissect signaling pathways regulated by the α7β1 integrin in normal and diseased muscle.

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