Abstract
Skeletal muscle contains slow and fast twitch fibers. These skeletal muscle fibers express type I and type II myosin, respectively, and these myosin isoenzymes have different ATPase activity. The aim of this study was to investigate protein profiles of bovine skeletal muscles by proteomic analysis. Fifty seven spots of distinct proteins were excised and characterized. The expression of sixteen spots was differed in longissimus dorsi muscle with a minimal 2-fold change compared to biceps femoris muscle. The majority of differentially expressed proteins belonged to metabolic regulation-related proteins such as glyceraldehyde 3-phosphate dehydrogenase, triosephosphate isomerase and carbonic anhydrase 3. The real time-PCR assay confirmed an increase or induction of specific genes: RGS12TS isoform, GAPDH, triosephosphate isomerase and carbonic anhydrase. These results suggest that the expression of metabolic proteins is under a specific control system in different bovine skeletal muscle. These observations could have significant implications for understanding the physiological regulation of bovine skeletal muscles.
Highlights
Skeletal muscles are composed of various fibers to fulfill functional needs
Proteomics is a novel area of research that involves the global analysis of cellular proteins using diverse technologies, such as 2-D gel electrophoresis, mass spectrometry and bioinformatics
We detected 286±12 and 293±14 protein spots in gels prepared from bovine longissimus dorsi muscle and biceps femoris muscle, respectively
Summary
Skeletal muscles are composed of various fibers to fulfill functional needs. This diversity is caused by specific myofibrillar protein isoforms that result in different fiber types (Barany, 1967). Two-dimensional gel electrophoresis (2-DE) with its recent development has been seen as an ideal tool for proteome analysis. It has shortcomings, for example, poor ability to separate. To understand the molecular basis of physiological regulations in bovine skeletal muscle, we undertook to compare protein patterns of the longissimus dorsi and biceps femoris muscles in cattle by using proteomic analysis
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