Palladin fulfils a crucial function as a molecular scaffold in organizing and stabilizing the actin cytoskeleton. At least four major palladin isoforms exist due to different promoter usage and alternative splicing: a 200-kDa isoform, a 140-kDa isoform, and two isoforms with a size of 90-92 kDa. Here, we describe their expression during mouse development and in adult tissues. The 200-kDa isoform is predominantly expressed in developing heart and skeletal muscle. The 140-kDa isoform is expressed in various mesenchymal tissues, and also represents the major isoform of the brain. The 90-92-kDa isoforms are almost ubiquitously expressed with the highest levels in smooth muscle-rich tissues. Immunohistochemical and immunofluorecence staining with an anti-200-kDa isoform-specific antiserum localizes the large isoform to the Z-discs of cardiac and skeletal muscle cells. Interestingly, the expression of this isoform is initiated and increasing during in vitro differentiation and fusion of C2C12 myoblasts, suggesting that the 200-kDa palladin isoform may play a scaffolding role during sarcomeric organization.
Copyright (c) 2008 Wiley-Liss, Inc.