TAILIEUCHUNG - Báo cáo khoa học: Disruption of structural and functional integrity of a2-macroglobulin by cathepsin E

a2 -Macroglobulin (a2M) is an abundant glycoprotein with the intrinsic capacity for capturing diverse proteins for rapid delivery into cells. After internalization by the receptor-mediated endocytosis,a2M-protein complexes were rapidly degraded in the endolysosome system. Although this is an importantpathway for clearanceofbotha2Mandbiological targets, little is known about the nature ofa2M degradation in the endolysosome system. | Eur. J. Biochem. 270 1189-1198 2003 FEBS 2003 doi Disruption of structural and functional integrity of a2-macroglobulin by cathepsin E Mitsue Shibata1. Hideaki Sakai1. Eiko Sakai1 Kuniaki Okamoto1 Kazuhisa Nishishita1 Yoshivuki Yasuda2 Yuzo Kato1 and Kenji Yamamoto2 1 Department of Pharmacology Nagasaki University School of Dentistry Japan department of Pharmacology Graduate School of Dental Science Kyushu University Fukuoka Japan a2-Macroglobulin a2M is an abundant glycoprotein with the intrinsic capacity for capturing diverse proteins for rapid delivery into cells. After internalization by the receptor-mediated endocytosis a2M-protein complexes were rapidly degraded in the endolysosome system. Although this is an important pathway for clearance of both a2M and biological targets little is known about the nature of a2M degradation in the endolysosome system. To investigate the possible involvement of intracellular aspartic proteinases in the disruption of structural and functional integrity of a2M in the endolysosome system we examined the capacity of a2M for interacting with cathepsin E and cathepsin D under acidic conditions and the nature of its degradation. a2M was efficiently associated with cathepsin E under acidic conditions to form noncovalent complexes and rapidly degraded through the generation of three major proteins with apparent molecular masses of 90 85 and 30 kDa. Parallel with this reaction a2M resulted in the rapid loss of its antiproteolytic activity. Analysis of the N-terminal amino-acid sequences of these proteins revealed that a2M was selectively cleaved at the Phe811-Leu812 bond in about 100mer downstream of the bait region. In contrast little change was observed for a2M treated by cathepsin D under the same conditions. Together the synthetic SPAFLA peptide corresponding to the Ser808-Ala813 sequence of human a2M which contains the cathepsin E-cleavage site was selectively cleaved by cathepsin E but not .

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