PMID: 6990412Mar 1, 1980Paper

The 68,000-dalton neurofilament-associated polypeptide is a component of nonneuronal cells and of skeletal myofibrils

Proceedings of the National Academy of Sciences of the United States of America
C WangE Lazarides

Abstract

Purified preparations of 10-nm neurofilaments from rat spinal cord and bovine or porcine brain contain a predominant 68,000-dalton polypeptide. This polypeptide is also a major component of the neurofilaments that copurify with brain tubulin isolated by cycles of polymerization and depolymerization. A protein that has the same isoelectric point and molecular weight as the neurofilament-associated polypeptide has also been identified as a cytoskeletal protein in a variety of avian and mammalian cell types, including baby hamster kidney (BHK-21) mouse 3T3, Novikoff rat hepatoma, chicken fibroblast, and chicken muscle cells. This protein is also a component of isolated chicken skeletal myofibrils. One-dimensional peptide maps of the 68,000-dalton proteins purified by two-dimensional isoelectric focusing/NaDodSO(4)/polyacrylamide gel electrophoresis from myofibrils, cycled tubulin, purified neurofilaments, and various cultured cell types were identical. In immunofluorescence this protein was associated with cytoplasmic intermediate filaments and myofibril Z discs. These results indicate that the neurofilament-associated polypeptide is a conserved protein that is present in many different cell types in addition to neuronal cells. Be...Continue Reading

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Sep 30, 1986·Biochemical and Biophysical Research Communications·B D Clark, I R Brown
Jun 1, 1981·Proceedings of the National Academy of Sciences of the United States of America·C WangE Lazarides
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