Knockdown of the α5 laminin chain affects differentiation of colorectal cancer cells and their sensitivity to chemotherapy.

Antimetabolites, Antineoplastic / pharmacology Cell Dedifferentiation Colorectal Neoplasms / drug therapy Fluorouracil / pharmacology Gene Knockdown Techniques HT29 Cells Humans Laminin / genetics
Colorectal cancer Dedifferentiation HT29 Intestinal epithelium stem cell marker LAMA5 Laminin

Journal

Biochimie
ISSN: 1638-6183
Titre abrégé: Biochimie
Pays: France
ID NLM: 1264604

Informations de publication

Date de publication:
Jul 2020
Historique:
received: 26 01 2020
revised: 13 04 2020
accepted: 14 04 2020
pubmed: 26 4 2020
medline: 15 1 2021
entrez: 26 4 2020
Statut: ppublish

Résumé

The interaction of tumor cells with the extracellular matrix (ECM) may affect the rate of cancer progression and metastasis. One of the major components of ECM are laminins, the heterotrimeric glycoproteins consisting of α-, β-, and γ-chains (αβγ). Laminins interact with their cell surface receptors and, thus, regulate multiple cellular processes. In this work, we demonstrate that shRNA-mediated knockdown of the α5 laminin chain results in Wnt- and mTORC1-dependent partial dedifferentiation of colorectal cancer cells. Furthermore, we showed that this dedifferentiation involved activation of ER-stress signaling, pathway promoting the sensitivity of cells to 5-fluorouracil.

Identifiants

DOI: 10.1016/j.biochi.2020.04.016 PMID: 32334043
pubmed: 32334043
pii: S0300-9084(20)30086-9
doi: 10.1016/j.biochi.2020.04.016
pii:
doi:

Substances chimiques

Antimetabolites, Antineoplastic 0
Laminin 0
laminin alpha5 0
Fluorouracil U3P01618RT

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

107-116

Informations de copyright

Copyright © 2020 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors declare that they have no competing interests.

Auteurs

Diana Maltseva (D)

Faculty of Biology and Biotechnology, National Research University Higher School of Economics, Myasnitskaya str. 13/4, 117997, Moscow, Russia; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, 117997, Moscow, Russia; Scientific Research Center Bioclinicum, Ugreshskaya str. 2/85, 115088, Moscow, Russia. Electronic address: d.maltseva@hse.ru.

Maria Raygorodskaya (M)

Scientific Research Center Bioclinicum, Ugreshskaya str. 2/85, 115088, Moscow, Russia.

Evgeny Knyazev (E)

Faculty of Biology and Biotechnology, National Research University Higher School of Economics, Myasnitskaya str. 13/4, 117997, Moscow, Russia; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, 117997, Moscow, Russia.

Victor Zgoda (V)

Institute of Biomedical Chemistry, Pogodinskaya str. 10, 119121, Moscow, Russia.

Olga Tikhonova (O)

Institute of Biomedical Chemistry, Pogodinskaya str. 10, 119121, Moscow, Russia.

Shan Zaidi (S)

School of Systems Biology, George Mason University, Fairfax, VA, 22030, USA.

Sergey Nikulin (S)

Faculty of Biology and Biotechnology, National Research University Higher School of Economics, Myasnitskaya str. 13/4, 117997, Moscow, Russia; Moscow Institute of Physics and Technology, Institutskiy per. 9, 141700, Dolgoprudny, Russia.

Ancha Baranova (A)

School of Systems Biology, George Mason University, Fairfax, VA, 22030, USA; Moscow Institute of Physics and Technology, Institutskiy per. 9, 141700, Dolgoprudny, Russia; Research Center of Medical Genetics, Moskvorechye str. 1, 115522, Moscow, Russia.

Andrey Turchinovich (A)

SciBerg e.Kfm, Birkenauer str. 7, 68309, Mannheim, Germany.

Sergey Rodin (S)

Department of Surgical Sciences, Ångström Laboratory, Uppsala University, 752 37, Uppsala, Sweden.

Alexander Tonevitsky (A)

Faculty of Biology and Biotechnology, National Research University Higher School of Economics, Myasnitskaya str. 13/4, 117997, Moscow, Russia; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, 117997, Moscow, Russia; Scientific Research Center Bioclinicum, Ugreshskaya str. 2/85, 115088, Moscow, Russia. Electronic address: atonevitsky@hse.ru.

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Classifications MeSH

questionsmedicales.fr › Actions chimiques et utilisations › Actions toxiques › Noxas › Antimétabolites › Antimétabolites antinéoplasiques › Knockdown of the α5 laminin chain affects...
questionsmedicales.fr › Phénomènes physiologiques cellulaires › Dédifférenciation cellulaire › Knockdown of the α5 laminin chain affects...
questionsmedicales.fr › Maladies de l'appareil digestif › Maladies gastro-intestinales › Maladies intestinales › Maladies du rectum › Tumeurs colorectales › Knockdown of the α5 laminin chain affects...
questionsmedicales.fr › Composés hétérocycliques › Composés hétéromonocycliques › Pyrimidines › Pyrimidinones › Uracile › Fluorouracil › Knockdown of the α5 laminin chain affects...
questionsmedicales.fr › Techniques d'investigation › Techniques génétiques › Ciblage de gène › Techniques de knock-down de gènes › Knockdown of the α5 laminin chain affects...
questionsmedicales.fr › Cellules › Cellules épithéliales › Cellules HT29 › Knockdown of the α5 laminin chain affects...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Knockdown of the α5 laminin chain affects...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Scléroprotéines › Protéines de la matrice extracellulaire › Laminine › Knockdown of the α5 laminin chain affects...