Limited tissue distribution of the intestinal brush border myosin I protein.

A myosinlike 105-110-kilodalton calmodulin-binding protein, brush border myosin I, found in the intestinal brush border has been linked to two seemingly disparate but possibly interacting functions of the brush border, namely, microvillar motility and vitamin D regulated calcium transport. If brush border myosin I were to function primarily as a myosinlike molecule powering cellular or microvillar motility, one might expect it to be found in a variety of tissues with microvilli such as the renal brush border and bile canaliculus. On the other hand, a more specialized function such as participation in vitamin D regulated calcium transport might dictate a more restricted tissue distribution for brush border myosin I. To determine the tissue distribution of brush border myosin I, we purified this protein to apparent homogeneity, generated antisera to it, and used the antisera to localize the protein within the intestinal epithelial cell by immunocytochemistry. We then screened a variety of other tissues (brain, lung, heart, liver, spleen, pancreas, kidney, and skeletal muscle) both for calmodulin-binding proteins as well as for brush border myosin I using Western blots and immunofluorescence. Our results indicate that the intestinal brush border myosin I is limited in its distribution to the intestinal brush border.