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• W149775114 abstract "Publisher Summary This chapter discusses the structural chemistry and the biological aspects of ADAM10. Originally, ADAM10 was characterized as a myelin-associated metalloproteinase. After cloning the bovine ADAM10 cDNA, the deduced amino acid sequence indicated that the enzyme belonged to the reprolysin subfamily and therefore was named MADM (mammalian disintegrin metalloprotease). The mammalian reprolysin subfamily has been named ADAM (a disintegrin and metalloproteinase) and MADM has been designated ADAM10. The ADAM10 homologs in Drosophila melanogaster and Caenorhabditis elegans are named kuzbanian and sup-17, respectively. The enzymatic activity of isolated ADAM10 can be monitored in vitro either by cleavage of Myelin Basic Protein (MBP) or by processing of peptide substrates derived from Amyloid Precursor Protein (APP) or pro-tumor necrosis factor α (pro-TNFα). Human ADAM10 is localized on chromosome 15 (15q22) and is widely expressed in mammalian organs, including brain. The role of ADAM10 as α-secretase cleaving APP has been confirmed by overexpression in intact cells, which leads to a several-fold increase in the release of secreted APPsα." @default.
• W149775114 created "2016-06-24" @default.
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• W149775114 date "2004-01-01" @default.
• W149775114 modified "2023-10-16" @default.
• W149775114 title "ADAM10, myelin-associated metalloendopeptidase" @default.
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• W149775114 doi "https://doi.org/10.1016/b978-0-12-079611-3.50227-5" @default.
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