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Mechanism and significance of specific proteolytic cleavage of Reelin.

Abstract：

:Reelin is a secreted glycoprotein essential for normal brain development and function. In the extracellular milieu, Reelin is subject to specific cleavage at two (N-t and C-t) sites. The N-t cleavage of Reelin is implicated in psychiatric and Alzheimer's diseases, but the molecular mechanism and physiological significance of this cleavage are not completely understood. Particularly, whether the N-t cleavage affects the signaling activity of Reelin remains controversial. Here, we show that the protease in charge of the N-t cleavage of Reelin requires the activity of certain proprotein convertase family for maturation and has strong affinity for heparin. By taking advantage of these observations, we for the first time succeeded in obtaining "Uncleaved" and "Completely Cleaved" Reelin proteins. The N-t cleavage splits Reelin into two distinct fragments and virtually abolishes its signaling activity. These findings provide an important biochemical basis for the function of Reelin proteolysis in brain development and function.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kohno S,Kohno T,Nakano Y,Suzuki K,Ishii M,Tagami H,Baba A,Hattori M

doi

10.1016/j.bbrc.2009.01.039

subject

Has Abstract

pub_date

2009-02-27 00:00:00

pages

93-7

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(09)00077-1

journal_volume

380

pub_type

杂志文章

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