TAILIEUCHUNG - Báo cáo khoa học: Identification of a 250 kDa putative microtubuleassociated protein as bovine ferritin Evidence for a ferritin–microtubule interaction

We reported previously on the purification and partial characterization of a putative microtubule-associated protein (MAP) from bovine adrenal cor-tex with an approximate molecular mass of 250 kDa. The protein was expressed ubiquitously in mammalian tissues, and bound to microtubules in vitro and in vivo, but failed to promote tubulin polymerization into microtubules. In the present study, partial amino acid sequencing revealed that the protein shares an identical primary structure with the widely distri-buted iron storage protein, ferritin | iFEBS Journal Identification of a 250 kDa putative microtubule-associated protein as bovine ferritin Evidence for a ferritin-microtubule interaction Mohammad R. Hasan1 Daisuke Morishima1 Kyoko Tomita1 Miho Katsuki1 and Susumu Kotani1 2 1 Department of Bioscience and Bioinformatics Kyushu Institute of Technology lizuka Fukuoka Japan 2 Department of BiologicalSciences Faculty of Science Kanagawa University Hiratsuka Kanagawa Japan Keywords ferritin ferritin-microtubule interaction microtubule microtubule-associated protein Correspondence M. R. Hasan Department of Bioscience and Bioinformatics Faculty of Computer Science and Systems Engineering Kyushu Institute of Technology lizuka Fukuoka 820-8502 Japan Fax 81 948 29 7801 Tel 81 948 29 7840 E-mail c791009m@ Received 22 October 2004 revised 6 December 2004 accepted 8 December 2004 doi We reported previously on the purification and partial characterization of a putative microtubule-associated protein MAP from bovine adrenal cortex with an approximate molecular mass of 250 kDa. The protein was expressed ubiquitously in mammalian tissues and bound to microtubules in vitro and in vivo but failed to promote tubulin polymerization into microtubules. In the present study partial amino acid sequencing revealed that the protein shares an identical primary structure with the widely distributed iron storage protein ferritin. We also found that the putative MAP and ferritin are indistinguishable from each other by electrophoretic mobility immunological properties and morphological appearance. Moreover the putative MAP conserves the iron storage and incorporation properties of ferritin confirming that the two are structurally and functionally the same protein. This fact led us to investigate the interaction of ferritin with microtubules by direct electron microscopic observations. Ferritin was bound to microtubules either singly or in the form of large intermolecular aggregates. We

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