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

Identification of a 250 kDa putative microtubule-associated protein as bovine ferritin

Authors:

Mohammad R. Hasan, Daisuke Morishima, Kyoko Tomita, Miho Katsuki, Susumu Kotani

Field:

Bioscience and Bioinformatics, Biological Sciences

Document Content:

This study investigates a protein previously identified as a putative microtubule-associated protein (MAP) with a molecular mass of 250 kDa from bovine adrenal cortex. Through detailed analysis, including partial amino acid sequencing, immunological properties, molecular mass, and iron storage capabilities, the protein is identified as bovine ferritin. The research presents evidence for a ferritin-microtubule interaction, demonstrating that ferritin binds to microtubules in vitro. This interaction is observed to occur both with single ferritin molecules and in the form of intermolecular aggregates. The study suggests that ferritin’s association with microtubules may play a role in regulating its intracellular concentration and release, potentially influencing cellular iron metabolism and stability.

Detailed Table of Contents:

• Keywords
• Correspondence
• Abstract
• Introduction
• Results
• Determination of the primary structure of the 250 kDa protein
• Comparison of the apparent molecular masses of ferritin and the 250 kDa protein
• Immunocrossreactivity of ferritin and the 250 kDa protein
• Detection of iron in the 250 kDa protein
• Iron uptake assay
• Morphological appearances of ferritin and the 250 kDa protein by electron microscopy
• Interaction of ferritin with microtubules
• Discussion
• Experimental procedures
• Chemicals and protein preparations
• Amino acid sequence analysis
• Immunoblotting
• Detection of iron in the 250 kDa protein
• Iron uptake assay
• Microtubule-binding assay
• Electron microscopy
• Miscellaneous
• Acknowledgements
• References