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Research article summary (published 30 Jul 2003):
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Reelin promotes peripheral synapse elimination and maturation.

Full Abstract

Reelin is an extracellular protein that is crucial for layer formation in the embryonic brain. Here, we demonstrate that Reelin functions postnatally to regulate the development of the neuromuscular junction. Reelin is required for motor end-plate maturation and proper nerve-muscle connectivity, and it directly promotes synapse elimination. Unlike layer formation, neuromuscular junction development requires a function of Reelin that is not mediated by Disabled1 or very-low-density lipoprotein receptors and apolipoprotein E receptor 2 receptors but by a distinct mechanism involving its protease activity.

 

Author information

Author/s: Quattrocchi, Carlo C (CC); Huang, Cheng (C); Niu, Sanyong (S); Sheldon, Michael (M); Benhayon, David (D); Cartwright, Joiner (J); Mosier, Dennis R (DR); Keller, Flavio (F); D'Arcangelo, Gabriella (G);

Affiliation: The Cain Foundation Laboratories, Houston, TX 77030, USA.

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.; Retracted Publication

Journal: Science (New York, N.Y.) (Science), published in United States. (Language: eng)

Reference: 2003-Aug; vol 301 (issue 5633) : pp 649-53

Dates: Created 2003/08/01; Completed 2003/08/13; Revised 2007/03/19;

PMID: 12893944, status: MEDLINE (last retrieval date: 2/18/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

Comments and Corrections

CommentIn: Science. 2004 Mar 26;303(5666):1977; author reply 1977. (PMID: 15044788)

ErratumIn: Science. 2003 Sep;301(5641):1849.

RetractionIn: Quattrocchi CC, Huang C, Niu S, Sheldon M, Benhayon D, Cartwright J Jr, Mosier DR, Keller F, D'Arcangelo G. Science. 2004 Mar 26;303(5666):1974. (PMID: 15044784)

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Associated Chemicals: Cell Adhesion Molecules, Neuronal (0) ; Culture Media, Conditioned (0) ; Dab1 protein, mouse (0) ; Extracellular Matrix Proteins (0) ; Nerve Tissue Proteins (0) ; Receptors, LDL (0) ; Receptors, Lipoprotein (0) ; Serine Proteinase Inhibitors (0) ; Sulfones (0) ; VLDL receptor (0) ; apolipoprotein E receptor 2 (0) ; 4-(2-aminoethyl)benzenesulfonylfluoride (34284-75-8) ; Serine Endopeptidases (EC 3.4.21.-) ; reelin protein (EC 3.4.21.-)

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