Dr Matthew A Benson, B. Sc. (hons.), D. Phil. 

Matthew BensonGoogle Scholar h-index 16, i10-index 17

 

Matt received a B.Sc (hons.) in Biotechnology (Applied Molecular Biology) from the University of Leeds in 1996.  Following his undergraduate he spent a year at the University of Exeter modifying the bacteria E. coli to biodegrade Jet Fuel  (Hydrazine).  After moving to Derek Blake’s lab in Oxford in 1997, he began working on the dystrophin-associated glycoprotein complex (DGC).  The DGC is a group of proteins that are fundamental for the normal function of cardiac and skeletal muscle [1] .  Disruption of the DGC, caused by genetic mutations, results in many different forms of neuromuscular diseases including Duchenne Muscular Dystrophy. 

During this period in Prof Blake’s lab he cloned a number of new disease candidate genes including dysbindin [2] (a schizophrenia susceptibility candidate) and FKRP [3, 4] (Congenital muscular dystrophy 1C and Limb Girdle muscular dystrophy 2i).      

The DGC (courtesy of Qiagen)

dysbindin

 

 

 

The dystrophin glycoprotein complex (courtesy of Qiagen) and Dysbindin in normal and dystrophic muscle

 

 

 

 

He extended this work during his D.Phil in the Pharmacology Department of the University of Oxford where he identified the massive (413 kDa) cardiac and skeletal muscle-specific protein, Myospryn (aka CMYA5) [5] .  Recently, a polymorphism within myospryn has been associated with a thickening of the heart walls in hypertensive patients [6].

Upon completing his D.Phil he worked at Imperial College with Dr Stuart Cook examining the role of the protein Osteoglycin in the regulation of left ventricular size [7] .  He is now back in Oxford where he is developing assays to identify novel cardiovascular drug targets.

Osteoglycin in a cardiomyocyte

OGn

 

A list of his publications is found here.

 

 

1.            Ervasti, J.M. and K.J. Sonnemann, Biology of the striated muscle dystrophin-glycoprotein complex. Int Rev Cytol, 2008. 265: p. 191-225.

2.            Benson, M.A., et al., Dysbindin, a novel coiled-coil-containing protein that interacts with the dystrobrevins in muscle and brain. J Biol Chem, 2001. 276(26): p. 24232-41.

3.            Brockington, M., et al., Mutations in the fukutin-related protein gene (FKRP) identify limb girdle muscular dystrophy 2I as a milder allelic variant of congenital muscular dystrophy MDC1C. Hum Mol Genet, 2001. 10(25): p. 2851-9.

4.            Brockington, M., et al., Mutations in the fukutin-related protein gene (FKRP) cause a form of congenital muscular dystrophy with secondary laminin alpha2 deficiency and abnormal glycosylation of alpha-dystroglycan. Am J Hum Genet, 2001. 69(6): p. 1198-209.

5.            Benson, M.A., C.L. Tinsley, and D.J. Blake, Myospryn is a novel binding partner for dysbindin in muscle. J Biol Chem, 2004. 279(11): p. 10450-8.

6.            Nakagami, H., et al., Gene polymorphism of myospryn (cardiomyopathy-associated 5) is associated with left ventricular wall thickness in patients with hypertension. Hypertens Res, 2007. 30(12): p. 1239-46.

7.            Petretto, E., et al., Integrated genomic approaches implicate osteoglycin (Ogn) in the regulation of left ventricular mass. Nat Genet, 2008. 40(5): p. 546-52.