Muscle protein analysis by two-dimensional gel electrophoresis

Abstract

Two-dimensional electrophoresis was first applied to the analysis of muscle proteins in 1976 when the occurrence of multiple forms of actin was discovered. Since that time the technique has become widely accepted as a new approach to studies of myogenesis, muscle differentiation, and muscle pathology. In addition, two-dimensional electrophoresis now is being used to investigate contractile proteins present in nonmuscle cells. This review will discuss, in general, the technique of two-dimensional electrophoresis in polyacrylamide gels which combines isoelectric focusing and sodium dodecyl sulfate electrophoresis. The application of the technique specifically to muscle protein analysis will be discussed through a review of existing literature on two-dimensional electrophoresis of cultured muscle cells and tissue homogenates. Attention will be given to contractile protein heterogeneities such as alpha, beta, and gamma actin and the embryonic forms of myosin light chains, all discovered through the use of two-dimensional electrophoresis. New information concerning gene expression during muscle differentiation revealed by differences in two-dimensional electrophoresis protein patterns and the use of two-dimensional electrophoresis for studying human muscle pathology through analysis of tissue biopsies will also be discussed.