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The E1 copper binding domain of full-length amyloid precursor protein promotes epithelial to mesenchymal transition in DU145 cells in isoform-specific manner

Research output: Contribution to Journal/Magazine › Journal article › peer-review

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The E1 copper binding domain of full-length amyloid precursor protein promotes epithelial to mesenchymal transition in DU145 cells in isoform-specific manner. / Gough, Mallory; Delury, Craig; Parkin, Edward.
In: International Journal of Biochemistry Research and Review, Vol. 6, No. 1, 2015, p. 264-273.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Gough, M, Delury, C & Parkin, E 2015, 'The E1 copper binding domain of full-length amyloid precursor protein promotes epithelial to mesenchymal transition in DU145 cells in isoform-specific manner', International Journal of Biochemistry Research and Review, vol. 6, no. 1, pp. 264-273. https://doi.org/10.9734/IJBCRR/2015/14873

APA

Gough, M., Delury, C., & Parkin, E. (2015). The E1 copper binding domain of full-length amyloid precursor protein promotes epithelial to mesenchymal transition in DU145 cells in isoform-specific manner. International Journal of Biochemistry Research and Review, 6(1), 264-273. https://doi.org/10.9734/IJBCRR/2015/14873

Vancouver

Gough M, Delury C, Parkin E. The E1 copper binding domain of full-length amyloid precursor protein promotes epithelial to mesenchymal transition in DU145 cells in isoform-specific manner. International Journal of Biochemistry Research and Review. 2015;6(1):264-273. Epub 2014 Dec 19. doi: 10.9734/IJBCRR/2015/14873

Author

Gough, Mallory ; Delury, Craig ; Parkin, Edward. / The E1 copper binding domain of full-length amyloid precursor protein promotes epithelial to mesenchymal transition in DU145 cells in isoform-specific manner. In: International Journal of Biochemistry Research and Review. 2015 ; Vol. 6, No. 1. pp. 264-273.

Bibtex

@article{65d739bd0266424d88b6c0ddbf5a4974,
title = "The E1 copper binding domain of full-length amyloid precursor protein promotes epithelial to mesenchymal transition in DU145 cells in isoform-specific manner",
abstract = "Epithelial to mesenchymal transition (EMT) confers migratory and dynamic properties on cells and, as such, plays a pivotal role in the development of metastatic, castration resistant prostate cancer. The amyloid precursor protein (APP), although most closely associated with the neurodegenerative condition Alzheimer's disease, has also been linked to the pathogenesis and prognosis of several cancers including prostate cancer. Aims: To investigate whether over-expression of APP could promote EMT in prostate cancer (PCa) DU145 cells and to determine the molecular prerequisites for this effect. Methodology: A range of APP molecular constructs were stably expressed in DU145 cells and their effects on EMT were monitored by morphological analysis and by immunoblotting for the EMT marker proteins, E-cadherin and vimentin. Results: Our results show that the full-length 695 amino acid isoform (APP695), but not APP751 or APP770, promoted EMT via a mechanism requiring an intact extracellular E1 copper binding domain and tyrosine687 within the cytosolic domain of the protein. Conclusion: Targeting the expression of APP695 or the E1 copper binding domain of the protein may, therefore, contribute to therapeutic strategies for the delay or prevention of prostate cancer metastasis.",
keywords = "Prostate cancer, epithelial to mesenchymal transition, metastasis, amyloid precursor protein",
author = "Mallory Gough and Craig Delury and Edward Parkin",
year = "2015",
doi = "10.9734/IJBCRR/2015/14873",
language = "English",
volume = "6",
pages = "264--273",
journal = "International Journal of Biochemistry Research and Review",
issn = "2231-086X",
publisher = "SCIENCEDOMAIN International",
number = "1",

}

RIS

TY - JOUR

T1 - The E1 copper binding domain of full-length amyloid precursor protein promotes epithelial to mesenchymal transition in DU145 cells in isoform-specific manner

AU - Gough, Mallory

AU - Delury, Craig

AU - Parkin, Edward

PY - 2015

Y1 - 2015

N2 - Epithelial to mesenchymal transition (EMT) confers migratory and dynamic properties on cells and, as such, plays a pivotal role in the development of metastatic, castration resistant prostate cancer. The amyloid precursor protein (APP), although most closely associated with the neurodegenerative condition Alzheimer's disease, has also been linked to the pathogenesis and prognosis of several cancers including prostate cancer. Aims: To investigate whether over-expression of APP could promote EMT in prostate cancer (PCa) DU145 cells and to determine the molecular prerequisites for this effect. Methodology: A range of APP molecular constructs were stably expressed in DU145 cells and their effects on EMT were monitored by morphological analysis and by immunoblotting for the EMT marker proteins, E-cadherin and vimentin. Results: Our results show that the full-length 695 amino acid isoform (APP695), but not APP751 or APP770, promoted EMT via a mechanism requiring an intact extracellular E1 copper binding domain and tyrosine687 within the cytosolic domain of the protein. Conclusion: Targeting the expression of APP695 or the E1 copper binding domain of the protein may, therefore, contribute to therapeutic strategies for the delay or prevention of prostate cancer metastasis.

AB - Epithelial to mesenchymal transition (EMT) confers migratory and dynamic properties on cells and, as such, plays a pivotal role in the development of metastatic, castration resistant prostate cancer. The amyloid precursor protein (APP), although most closely associated with the neurodegenerative condition Alzheimer's disease, has also been linked to the pathogenesis and prognosis of several cancers including prostate cancer. Aims: To investigate whether over-expression of APP could promote EMT in prostate cancer (PCa) DU145 cells and to determine the molecular prerequisites for this effect. Methodology: A range of APP molecular constructs were stably expressed in DU145 cells and their effects on EMT were monitored by morphological analysis and by immunoblotting for the EMT marker proteins, E-cadherin and vimentin. Results: Our results show that the full-length 695 amino acid isoform (APP695), but not APP751 or APP770, promoted EMT via a mechanism requiring an intact extracellular E1 copper binding domain and tyrosine687 within the cytosolic domain of the protein. Conclusion: Targeting the expression of APP695 or the E1 copper binding domain of the protein may, therefore, contribute to therapeutic strategies for the delay or prevention of prostate cancer metastasis.

KW - Prostate cancer

KW - epithelial to mesenchymal transition

KW - metastasis

KW - amyloid precursor protein

U2 - 10.9734/IJBCRR/2015/14873

DO - 10.9734/IJBCRR/2015/14873

M3 - Journal article

VL - 6

SP - 264

EP - 273

JO - International Journal of Biochemistry Research and Review

JF - International Journal of Biochemistry Research and Review

SN - 2231-086X

IS - 1

ER -