TAILIEUCHUNG - Báo cáo khoa học: Comprehensive interaction of dicalcin with annexins in frog olfactory and respiratory cilia

Dicalcin (renamed from p26olf) is a dimer form of S100 proteins found in frog olfactory epithelium. S100 proteins form a group of EF-hand Ca 2+ -binding proteins, and are known to interact with many kinds of tar-get protein to modify their activities. To determine the role of dicalcin in the olfactory epithelium, we identified its binding proteins. | ỊFEBS Journal Comprehensive interaction of dicalcin with annexins in frog olfactory and respiratory cilia Tatsuya Uebi1 Naofumi Miwa1 2 and Satoru Kawamura1 2 1 Department of Biology Graduate Schoolof Science Osaka University Japan 2 Graduate Schoolof Frontier Biosciences Osaka University Japan Keywords annexin dicalcin olfactory cilia respiratory cilia S100 Correspondence S. Kawamura Graduate School of Frontier Biosciences Osaka University Yamada-oka 1-3 Suita Osaka 565-0871 Japan Fax 81 6 6879 4614 Tel 81 6 6879 4610 E-mail kawamura@ Present address Department of Physiology Schoolof Medicine Toho University Tokyo Japan Database Amino acid sequences have been submitted to DDBJ under the following accession numbers frog annexin A1 AB286845 frog annexin A2 AB286846 frog annexin A4 AB286848 frog annexin A5 AB286847 Received 8 May 2007 revised 20 July 2007 accepted 24 July 2007 Dicalcin renamed from p26olf is a dimer form of S100 proteins found in frog olfactory epithelium. S100 proteins form a group of EF-hand Ca2 -binding proteins and are known to interact with many kinds of target protein to modify their activities. To determine the role of dicalcin in the olfactory epithelium we identified its binding proteins. Several proteins in frog olfactory epithelium were found to bind to dicalcin in a Ca2 -dependent manner. Among them 38 kDa and 35 kDa proteins were most abundant. Our analysis showed that these were a mixture of annexin A1 annexin A2 and annexin A5. Immunohistochemical analysis showed that dicalcin and all of these three subtypes of annexin colocalize in the olfactory cilia. Dicalcin was found to be present in a quantity almost sufficient to bind all of these annexins. Colocalization of dicalcin and the three subtypes of annexin was also observed in the frog respiratory cilia. Dicalcin facilitated Ca2 -dependent liposome aggregation caused by annexin A1 or annexin A2 and this facilitation was additive when both annexin A1 and annexin A2 .

• Báo cáo khoa học
• Report medicine
• traditional medicine
• scientific reports
• medical knowledge
• cytoplasm
• analysis of cytoplasmic
• medical research
• oxidation
• Crystal structure
• bacteria
• hemoglobin
• medicine
• cell proliferation
• breast cancer
• chemical reaction
• gastric cancer
• hormone medicine
• tumor cells
• biochemical studies
• environmental medicine