A disintegrin and metalloproteinase with thrombospondin motifs 4 (ADAMTS-4) cleaves Reelin in an isoform-dependent manner

作者：Hisanaga Arisa; Morishita Shunsuke; Suzuki Kenta; Sasaki Kazutomo; Koie Mari; Kohno Takao; Hattori Mitsuharu^*

来源：FEBS LETTERS, 2012, 586(19): 3349-3353.

DOI：10.1016/j.febslet.2012.07.017

• Reelin
• Brain
• Protease
• ADAMTS
• Processing

Reel in is a glycoprotein essential for brain development and functions. Reelin is subject to specific proteolysis at two distinct (N-t and C-t) sites, and these cleavages significantly diminish Reelin activity. The decrease of Reelin activity is detrimental for brain function, but the protease that catalyzes specific cleavage of Reelin remains elusive. Here we found that a disintegrin and metalloproteinase with thrombospondin motifs 4 (ADAMTS-4) cleaves Reelin in an isoform-specific manner. Among ADAMTS-4 isoforms, p50 cleaves the N-t site only, while p75 cleaves both sites. This is the first report identifying a protease that can specifically cleave Reelin.

• 出版日期2012-9-21