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The alpha-smooth muscle actin (aortic type) is one of the six isoforms of mammalian actin. It is difficult to distinguish them immunologically, because the amino acid sequences of the isoforms are well conserved. Here, we detected alpha-smooth muscle actin by means of in situ hybridization using an oligonucleotide probe complimentary to the 3'-untranslated region which does not cross-hybridize with the remaining isoforms. We developed the following non-radiolabeled procedure, where labeled digoxigenin is intensively immunostained by a combination of PAP and ABC methods. In the both thick (100-mu-m) and semi-thin (2-mu-m) sections of rat parotid gland, actin mRNA was positively stained in myoepithelial cells which emitted flat and cytoplasmic processes over the basal surfaces of acini and intercalated ducts. These findings were also confirmed by immunohistochemistry using a monoclonal antibody which is slightly cross-reactive with the other actins. In the immunohistochemical study, however, the myoepithelial processes could be pursued to the distal end. It is probable that this discrepancy between the two methods is due to the different subcellular distribution of the actin protein and its mRNA.

Non-radiolabeled in situ hybridization and immunohistochemistry of .ALPHA.-smooth muscle actin in myoepithelial cells.