Angiotensin II induces the exocytosis of galectin-3 via integrin αv/AKT/NF-κB signaling pathway.

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Summary of "Angiotensin II induces the exocytosis of galectin-3 via integrin αv/AKT/NF-κB signaling pathway."

The article "Angiotensin II induces the exocytosis of galectin-3 via integrin αv/AKT/NF-κB signaling pathway" by L. Tian, D. Coletti, Z.-L. Li, published in Eur Rev Med Pharmacol Sci 2019; 23(13): 5949-5957 has been retracted with the unanimous agreements of all the authors and the Editors-in-Chief, since the corresponding author submitted the manuscript for review without informing and obtaining the agreement of the senior co-authors.


Journal Details

This article was published in the following journal.

Name: European review for medical and pharmacological sciences
ISSN: 2284-0729
Pages: 7183


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Medical and Biotech [MESH] Definitions

Integrin beta chains combine with integrin alpha chains to form heterodimeric cell surface receptors. Integrins have traditionally been classified into functional groups based on the identity of one of three beta chains present in the heterodimer. The beta chain is necessary and sufficient for integrin-dependent signaling. Its short cytoplasmic tail contains sequences critical for inside-out signaling.

A complex signaling pathway whose name is derived from the DROSOPHILA Wg gene, which when mutated results in the wingless phenotype, and the vertebrate INT gene, which is located near integration sites of MOUSE MAMMARY TUMOR VIRUS. The signaling pathway is initiated by the binding of WNT PROTEINS to cells surface WNT RECEPTORS which interact with the AXIN SIGNALING COMPLEX and an array of second messengers that influence the actions of BETA CATENIN.

An integrin alpha subunit that primarily associates with INTEGRIN BETA1 or INTEGRIN BETA4 to form laminin-binding heterodimers. Integrin alpha6 has two alternatively spliced isoforms: integrin alpha6A and integrin alpha6B, which differ in their cytoplasmic domains and are regulated in a tissue-specific and developmental stage-specific manner.

An integrin beta subunit of approximately 85-kDa in size which has been found in INTEGRIN ALPHAIIB-containing and INTEGRIN ALPHAV-containing heterodimers. Integrin beta3 occurs as three alternatively spliced isoforms, designated beta3A-C.

A galectin found preferentially expressed in the gastrointestinal tract. The protein occurs as a homodimer with two 14-kDa subunits.

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