Transfection of MCF-7 Carcinoma Cells with Human Integrin α7 cDNA Promotes Adhesion to Laminin

Vizirianakis, Ioannis S.; Yao, Chung-Chen Jane; Chen, Yaoqi; Ziober, Barry L.; Tsiftsoglou, Asterios S.; Kramer, Randall H.

doi:10.1006/abbi.2000.2134

Cited by 22 publications

(17 citation statements)

References 36 publications

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“…In fact, overexpression of adhesion molecules, such as integrin and cadherin has been reported to suppress cell proliferation. [38][39][40] Thus, a decreased rate of proliferation was expected by overexpression of DG and it is not surprising for the MCF10F derivatives that also displayed an increased adhesion to a substratum (Table 1 and Fig. 2A).…”

Section: Discussionmentioning

confidence: 77%

Increased expression of dystroglycan inhibits the growth and tumorigenicity of human mammary epithelial cells

Sgambato¹,

Camerini²,

Faraglia³

et al. 2004

Cancer Biology & Therapy

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Dystroglycan (DG) is an adhesion molecule formed by two subunits, α (extracellular) and β (transmembrane) DG, which are codified by a single gene and form a continuous link from the extracellular matrix to the intracellular cytoskeleton. Reduction or loss of expression of DG has been observed in human cancer cell lines and primary tumors and has been suggested to promote tumor development and invasiveness.In this study, the human breast epithelial non-tumorigenic MCF10F and the breast cancer MCF7 cell lines were engineered to stably express an exogenous DG cDNA and the effects on the phenotype of both cell lines were evaluated. The MCF10F transfected cells displayed an increased expression of both DG subunits which was associated with inhibition of the anchorage-dependent growth, accumulation of cells in the G 0 /G 1 phase of the cell cycle and increased adhesion to a substratum. The MCF7 transfected cells were unable to restore α-DG despite an increased expression of the β-DG subunit. Anchoragedependent and independent growth and the in vivo tumorigenicity were reduced in these derivatives that also displayed a reduced adhesion to a substratum and were shown to release α-DG in the culture medium.These findings confirm and extend previous evidence that transformation of mammary epithelial cells is associated with loss of their ability to retain α-DG on the cell membrane. Moreover, they indicate that DG is involved in cell functions other than cell adhesion to the extracellular matrix, and that its loss of function might predispose to tumor progression by compromising regulatory controls over cell growth and proliferation.

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Section: Discussionmentioning

confidence: 77%

Increased expression of dystroglycan inhibits the growth and tumorigenicity of human mammary epithelial cells

Sgambato¹,

Camerini²,

Faraglia³

et al. 2004

Cancer Biology & Therapy

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“…Then the RA-treated cells were plated as adherent cultures and processed for siRNA transfection or treatment with anti-integrin monoclonal antibody (mAb). For siRNA transfection, 2 ϫ 10 5 cells were transfected with 66 pmol of siRNA using the siRNA Reagent System (Santa Cruz Biotechnology, Inc.) for 24 h. For function-blocking antibody treatment, TS2/7 mAb (Abcam) (22,23) was used at 5 g/ml for 1 h. After 1-h incubation, the cells were treated with GS/BMP-4 for 7 days and then were tested for differentiation status.…”

Section: Methodsmentioning

confidence: 99%

Differentiation of Human Skeletal Muscle Stem Cells into Odontoblasts Is Dependent on Induction of α1 Integrin Expression

Ozeki

Mogi

Yamaguchi

et al. 2014

Journal of Biological Chemistry

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Background: Human skeletal muscle stem cells (hSMSCs) can differentiate into bone and fat cells. Results: hSMSCs could also differentiate into odontoblasts but required an extracellular matrix scaffold and changes in their integrin profile. Conclusion:The present results identify an odontoblast differentiation pathway dependent on adhesion receptor expression. Significance: The data provide insight into how hSMSC adhesion receptors interact with the microenvironment to regulate lineage specification.

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“…Mouse anti-␣3 (mAb J143) was from the American Type Culture Collection (American Type Culture Collection, Manassas, VA), rat anti-mouse ␤1 (mAb MB1.2) and mouse anti-human ␤1 (mAb 2000) were from Chemicon International (Temecula, CA), rat anti-mouse ␣7 (mAb CY8), mouse antihuman ␣7 (mAb 9.1), rabbit anti-human ␤1 cytodomain (polyclonal antibody [pAb] 22778), and rabbit anti-mouse ␣7 light chain (pAb 1211) were from our laboratory, as described previously (Yao et al, 1996b(Yao et al, , 1997Vizirianakis et al, 2001). Fluorescein-conjugated secondary antibodies were obtained from Jackson Immunoresearch Laboratories (West Grove, PA).…”

Section: Methodsmentioning

confidence: 99%

“…Full-length human ␣7X2 cDNA (Vizirianakis et al, 2001) was used as a template for the generation of full-length human ␣7X1. The X2 exon was replaced with the X1 exon by uracil DNA glycosylase excision to generate cohesive ends on the PCR product of the X1 exon.…”

Section: Cloning Of Human ␣7x1mentioning

confidence: 99%

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The β1 Cytoplasmic Domain Regulates the Laminin-binding Specificity of the α7X1 Integrin

Yeh

Ziober

Liu

et al. 2003

MBoC

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During muscle development, the laminin-specific ␣7 integrin is alternatively spliced in the putative ligand-binding domain to yield either the ␣7X1 or the ␣7X2 variant. The relative level of ␣7X1 and ␣7X2 is developmentally regulated. Similarly, the partner ␤1 integrin cytoplasmic domain is converted from the ␤1A to the ␤1D splice variant. To determine whether ␤1D modulates the activity of the ␣7 receptor, cells were transfected with ␣7X1 and ␤1D cDNA. ␣7X1 coupled with ␤1A failed to adhere to laminin-1, whereas cotransfectants expressing ␣7X1 and ␤1D showed strong adhesion. Interestingly, ␣7X1 complexed with ␤1A and ␤1D displayed the same level of poor adhesion to laminin-2/4 or strong adhesion to laminin-10/11. These findings indicate that ␣7 function is regulated not only by X1/X2 in its extracellular domain but also by ␤1 cytoplasmic splice variants. It is likely that expression of ␤1D alters ␣7X1 binding to laminin isoforms by a process related to ligand affinity modulation. Functional regulation of ␣7␤1 by developmentally regulated splicing events may be important during myogenic differentiation and repair because the integrin mediates adhesion, motility, and cell survival.

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Transfection of MCF-7 Carcinoma Cells with Human Integrin α7 cDNA Promotes Adhesion to Laminin

Cited by 22 publications

References 36 publications

Increased expression of dystroglycan inhibits the growth and tumorigenicity of human mammary epithelial cells

Increased expression of dystroglycan inhibits the growth and tumorigenicity of human mammary epithelial cells

Differentiation of Human Skeletal Muscle Stem Cells into Odontoblasts Is Dependent on Induction of α1 Integrin Expression

The β1 Cytoplasmic Domain Regulates the Laminin-binding Specificity of the α7X1 Integrin

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