Ph.D., Muscle Biology, University of Wisconsin at Madison, 1981
M.S., Muscle Biology, University of Wisconsin at Madison, 1976
B.S., Biochemistry, University of Wisconsin at Madison, 1974
204 G.M. Trout FSHN Building
Michigan State University
East Lansing, MI 48824-1224
Phone: (517) 355-8474, Ext. 100
Lab: (517) 355-8452, Ext. 211
Fax: (517) 353-8963
E-mail: stragale@msu.edu
My laboratory is focused on molecular mechanisms associated with development of inferior muscle food quality. We hypothesize that intensive breeding of food animals for rapid growth rate and high feed conversion over the past several decades has led to inadvertent selection for traits which have led to meat quality problems such as pale, soft, exudative (PSE) meat. Our laboratory has recently demonstrated the existence of several alternatively spliced isoforms of a skeletal muscle calcium release protein, sometimes referred to as ryanodine receptor. Abnormally high calcium release in the early period post-mortem could stimulate glycolysis, generating heat which could denature muscle proteins with resultant loss of protein functionality. We are currently engaged in studies to determine whether heat stress could alter the splice pattern of ryanodine receptor, which in turn could alter the kinetics of calcium release.
In a related project, we are investigating the molecular basis for the dramatic differences in growth rate between the turkey of the 1960s and the modern commercial turkey. We are using DNA microarray approaches to
identify proteins up-regulated or down-regulated at different developmental stages, including the 18-day embryo,
the 1-day-old neonate and the 16-week
adult in the two lines of turkeys. In
addition, we will be using microarray analysis to determine differences in
gene expression between normal and PSE meat samples. Our long-term goal is to provide strategies to breeders
to reduce the genetic contribution to
development of PSE meat.
Chiang W, Yoon HJ, Linz JE, Airey JA, Strasburg GM. Divergent mechanisms in generating molecular variations of alphaRYR and betaRYR in turkey skeletal muscle. J Muscle Res Cell Motil. 2008 Mar 8; [Epub ahead of print]
Chiang W, Byrem T, Zhang H, Strasburg G. Binding property of avian skeletal muscle ryanodine receptor isoforms with dihydropyridine receptor and calmodulin. J Muscle Res Cell Motil. 28:59-66, 2007.
Chiang W, Allison CP, Linz JE and Strasburg GM. "Identification of two alpha-RYR alleles and characterization of alphaRYR transcript variants in turkey skeletal muscle." Gene. 330:177-84, 2004.
Fruen BR, Bardy JM, Byrem TM, Strasburg GM and Louis CF. " Differential Ca(2+) sensitivity of skeletal and cardiac muscle ryanodine receptors in the presence of calmodulin." Am. J. Physiol. Cell Physiol. 279:C724-33, 2000.
Rodney GG, Williams BY, Strasburg GM, Beckingham K and Hamilton SL. "Regulation of RYR1 activity by Ca(2+) and calmodulin." Biochemistry. 39:7807-12, 2000.
Moore CP, Rodney G, Zhang JZ, Santacruz-Toloza L, Strasburg G and Hamilton SL. "Apocalmodulin and Ca2+ calmodulin bind to the same region on the skeletal muscle Ca2+ release channel." Biochemistry. 38:8532-7, 1999.
Wang LJ, Byrem TM, Zarosley J, Booren AM and Strasburg GM. "Skeletal muscle calcium channel ryanodine binding activity in genetically unimproved and commercial turkey populations." Poult. Sci. 78:792-7, 1999.
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