Galectin-1 Restricts Vascular Smooth Muscle Cell Motility Via Modulating Adhesion Force and Focal Adhesion Dynamics

Min Shao Tsai, Ming Tsai Chiang, Dong Lin Tsai, Chih Wen Yang, Hsien San Hou, Yi Ru Li, Po Chiao Chang, Heng Huei Lin, Huan Yuan Chen, Ing Shouh Hwang, Pei Kuen Wei, Chiao Po Hsu, Kuo I. Lin, Fu-Tong Liu, Lee Young Chau

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Vascular smooth muscle cell (VSMC) migration play a key role in the development of intimal hyperplasia and atherosclerosis. Galectin-1 (Gal-1) is a redox-sensitive β-galactoside-binding lectin expressed in VSMCs with intracellular and extracellular localizations. Here we show that VSMCs deficient in Gal-1 (Gal-1-KO) exhibited greater motility than wild type (WT) cells. Likewise, Gal-1-KO-VSMC migration was inhibited by a redox-insensitive but activity-preserved Gal-1 (CSGal-1) in a glycan-dependent manner. Gal-1-KO-VSMCs adhered slower than WT cells on fibronectin. Cell spreading and focal adhesion (FA) formation examined by phalloidin and vinculin staining were less in Gal-1-KO-VSMCs. Concomitantly, FA kinase (FAK) phosphorylation was induced to a lower extent in Gal-1-KO cells. Analysis of FA dynamics by nocodazole washout assay demonstrated that FA disassembly, correlated with FAK de-phosphorylation, was faster in Gal-1-KO-VSMCs. Surface plasmon resonance assay demonstrated that CSGal-1 interacted with α5β1integrin and fibronectin in a glycan-dependent manner. Chemical crosslinking experiment and atomic force microscopy further revealed the involvement of extracellular Gal-1 in strengthening VSMC-fibronectin interaction. In vivo experiment showed that carotid ligation-induced neointimal hyperplasia was more severe in Gal-1-KO mice than WT counterparts. Collectively, these data disclose that Gal-1 restricts VSMC migration by modulating cell-matrix interaction and focal adhesion turnover, which limits neointimal formation post vascular injury.

Original languageEnglish (US)
Article number11497
JournalScientific Reports
Volume8
Issue number1
DOIs
StatePublished - Dec 1 2018
Externally publishedYes

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Galectin 1
Focal Adhesions
Vascular Smooth Muscle
Smooth Muscle Myocytes
Cell Movement
Fibronectins
Cell Communication
Oxidation-Reduction
Hyperplasia
Polysaccharides
Phosphorylation
Cell-Matrix Junctions
Tunica Intima
Vinculin
Nocodazole
Phalloidine
Galactosides
Focal Adhesion Protein-Tyrosine Kinases
Surface Plasmon Resonance
Atomic Force Microscopy

ASJC Scopus subject areas

  • General

Cite this

Tsai, M. S., Chiang, M. T., Tsai, D. L., Yang, C. W., Hou, H. S., Li, Y. R., ... Chau, L. Y. (2018). Galectin-1 Restricts Vascular Smooth Muscle Cell Motility Via Modulating Adhesion Force and Focal Adhesion Dynamics. Scientific Reports, 8(1), [11497]. https://doi.org/10.1038/s41598-018-29843-3

Galectin-1 Restricts Vascular Smooth Muscle Cell Motility Via Modulating Adhesion Force and Focal Adhesion Dynamics. / Tsai, Min Shao; Chiang, Ming Tsai; Tsai, Dong Lin; Yang, Chih Wen; Hou, Hsien San; Li, Yi Ru; Chang, Po Chiao; Lin, Heng Huei; Chen, Huan Yuan; Hwang, Ing Shouh; Wei, Pei Kuen; Hsu, Chiao Po; Lin, Kuo I.; Liu, Fu-Tong; Chau, Lee Young.

In: Scientific Reports, Vol. 8, No. 1, 11497, 01.12.2018.

Research output: Contribution to journalArticle

Tsai, MS, Chiang, MT, Tsai, DL, Yang, CW, Hou, HS, Li, YR, Chang, PC, Lin, HH, Chen, HY, Hwang, IS, Wei, PK, Hsu, CP, Lin, KI, Liu, F-T & Chau, LY 2018, 'Galectin-1 Restricts Vascular Smooth Muscle Cell Motility Via Modulating Adhesion Force and Focal Adhesion Dynamics', Scientific Reports, vol. 8, no. 1, 11497. https://doi.org/10.1038/s41598-018-29843-3
Tsai, Min Shao ; Chiang, Ming Tsai ; Tsai, Dong Lin ; Yang, Chih Wen ; Hou, Hsien San ; Li, Yi Ru ; Chang, Po Chiao ; Lin, Heng Huei ; Chen, Huan Yuan ; Hwang, Ing Shouh ; Wei, Pei Kuen ; Hsu, Chiao Po ; Lin, Kuo I. ; Liu, Fu-Tong ; Chau, Lee Young. / Galectin-1 Restricts Vascular Smooth Muscle Cell Motility Via Modulating Adhesion Force and Focal Adhesion Dynamics. In: Scientific Reports. 2018 ; Vol. 8, No. 1.
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abstract = "Vascular smooth muscle cell (VSMC) migration play a key role in the development of intimal hyperplasia and atherosclerosis. Galectin-1 (Gal-1) is a redox-sensitive β-galactoside-binding lectin expressed in VSMCs with intracellular and extracellular localizations. Here we show that VSMCs deficient in Gal-1 (Gal-1-KO) exhibited greater motility than wild type (WT) cells. Likewise, Gal-1-KO-VSMC migration was inhibited by a redox-insensitive but activity-preserved Gal-1 (CSGal-1) in a glycan-dependent manner. Gal-1-KO-VSMCs adhered slower than WT cells on fibronectin. Cell spreading and focal adhesion (FA) formation examined by phalloidin and vinculin staining were less in Gal-1-KO-VSMCs. Concomitantly, FA kinase (FAK) phosphorylation was induced to a lower extent in Gal-1-KO cells. Analysis of FA dynamics by nocodazole washout assay demonstrated that FA disassembly, correlated with FAK de-phosphorylation, was faster in Gal-1-KO-VSMCs. Surface plasmon resonance assay demonstrated that CSGal-1 interacted with α5β1integrin and fibronectin in a glycan-dependent manner. Chemical crosslinking experiment and atomic force microscopy further revealed the involvement of extracellular Gal-1 in strengthening VSMC-fibronectin interaction. In vivo experiment showed that carotid ligation-induced neointimal hyperplasia was more severe in Gal-1-KO mice than WT counterparts. Collectively, these data disclose that Gal-1 restricts VSMC migration by modulating cell-matrix interaction and focal adhesion turnover, which limits neointimal formation post vascular injury.",
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AU - Tsai, Min Shao

AU - Chiang, Ming Tsai

AU - Tsai, Dong Lin

AU - Yang, Chih Wen

AU - Hou, Hsien San

AU - Li, Yi Ru

AU - Chang, Po Chiao

AU - Lin, Heng Huei

AU - Chen, Huan Yuan

AU - Hwang, Ing Shouh

AU - Wei, Pei Kuen

AU - Hsu, Chiao Po

AU - Lin, Kuo I.

AU - Liu, Fu-Tong

AU - Chau, Lee Young

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N2 - Vascular smooth muscle cell (VSMC) migration play a key role in the development of intimal hyperplasia and atherosclerosis. Galectin-1 (Gal-1) is a redox-sensitive β-galactoside-binding lectin expressed in VSMCs with intracellular and extracellular localizations. Here we show that VSMCs deficient in Gal-1 (Gal-1-KO) exhibited greater motility than wild type (WT) cells. Likewise, Gal-1-KO-VSMC migration was inhibited by a redox-insensitive but activity-preserved Gal-1 (CSGal-1) in a glycan-dependent manner. Gal-1-KO-VSMCs adhered slower than WT cells on fibronectin. Cell spreading and focal adhesion (FA) formation examined by phalloidin and vinculin staining were less in Gal-1-KO-VSMCs. Concomitantly, FA kinase (FAK) phosphorylation was induced to a lower extent in Gal-1-KO cells. Analysis of FA dynamics by nocodazole washout assay demonstrated that FA disassembly, correlated with FAK de-phosphorylation, was faster in Gal-1-KO-VSMCs. Surface plasmon resonance assay demonstrated that CSGal-1 interacted with α5β1integrin and fibronectin in a glycan-dependent manner. Chemical crosslinking experiment and atomic force microscopy further revealed the involvement of extracellular Gal-1 in strengthening VSMC-fibronectin interaction. In vivo experiment showed that carotid ligation-induced neointimal hyperplasia was more severe in Gal-1-KO mice than WT counterparts. Collectively, these data disclose that Gal-1 restricts VSMC migration by modulating cell-matrix interaction and focal adhesion turnover, which limits neointimal formation post vascular injury.

AB - Vascular smooth muscle cell (VSMC) migration play a key role in the development of intimal hyperplasia and atherosclerosis. Galectin-1 (Gal-1) is a redox-sensitive β-galactoside-binding lectin expressed in VSMCs with intracellular and extracellular localizations. Here we show that VSMCs deficient in Gal-1 (Gal-1-KO) exhibited greater motility than wild type (WT) cells. Likewise, Gal-1-KO-VSMC migration was inhibited by a redox-insensitive but activity-preserved Gal-1 (CSGal-1) in a glycan-dependent manner. Gal-1-KO-VSMCs adhered slower than WT cells on fibronectin. Cell spreading and focal adhesion (FA) formation examined by phalloidin and vinculin staining were less in Gal-1-KO-VSMCs. Concomitantly, FA kinase (FAK) phosphorylation was induced to a lower extent in Gal-1-KO cells. Analysis of FA dynamics by nocodazole washout assay demonstrated that FA disassembly, correlated with FAK de-phosphorylation, was faster in Gal-1-KO-VSMCs. Surface plasmon resonance assay demonstrated that CSGal-1 interacted with α5β1integrin and fibronectin in a glycan-dependent manner. Chemical crosslinking experiment and atomic force microscopy further revealed the involvement of extracellular Gal-1 in strengthening VSMC-fibronectin interaction. In vivo experiment showed that carotid ligation-induced neointimal hyperplasia was more severe in Gal-1-KO mice than WT counterparts. Collectively, these data disclose that Gal-1 restricts VSMC migration by modulating cell-matrix interaction and focal adhesion turnover, which limits neointimal formation post vascular injury.

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