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Article

The Role of the C-Terminal Lysine of S100P in S100P-Induced Cell Migration and Metastasis

1
Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Biosciences Building, Crown Street, Liverpool L69 7ZB, UK
2
College of Health and Life Sciences, Aston University, Aston Triangle, Birmingham B4 7ET, UK
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Academic Editors: Wiesława Leśniak and Anna Filipek
Biomolecules 2021, 11(10), 1471; https://doi.org/10.3390/biom11101471
Received: 12 September 2021 / Revised: 29 September 2021 / Accepted: 2 October 2021 / Published: 6 October 2021
S100P protein is a potent inducer of metastasis in a model system, and its presence in cancer cells of patients is strongly associated with their reduced survival times. A well-established Furth Wistar rat metastasis model system, methods for measuring cell migration, and specific inhibitors were used to study pathways of motility-driven metastasis. Cells expressing C-terminal mutant S100P proteins display markedly-reduced S100P-driven metastasis in vivo and cell migration in vitro. These cells fail to display the low focal adhesion numbers observed in cells expressing wild-type S100P, and the mutant S100P proteins exhibit reduced biochemical interaction with non-muscle myosin heavy chain isoform IIA in vitro. Extracellular inhibitors of the S100P-dependent plasminogen activation pathway reduce, but only in part, wild-type S100P-dependent cell migration; they are without effect on S100P-negative cells or cells expressing C-terminal mutant S100P proteins and have no effect on the numbers of focal adhesions. Recombinant wild-type S100P protein, added extracellularly to S100P-negative cells, stimulates cell migration, which is abolished by these inhibitors. The results identify at least two S100P-dependent pathways of migration, one cell surface and the other intracellularly-linked, and identify its C-terminal lysine as a target for inhibiting multiple migration-promoting activities of S100P protein and S100P-driven metastasis. View Full-Text
Keywords: S100P; membrane; metastasis; cell migration; myosin llA S100P; membrane; metastasis; cell migration; myosin llA
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MDPI and ACS Style

Ismail, T.M.; Gross, S.R.; Lancaster, T.; Rudland, P.S.; Barraclough, R. The Role of the C-Terminal Lysine of S100P in S100P-Induced Cell Migration and Metastasis. Biomolecules 2021, 11, 1471. https://doi.org/10.3390/biom11101471

AMA Style

Ismail TM, Gross SR, Lancaster T, Rudland PS, Barraclough R. The Role of the C-Terminal Lysine of S100P in S100P-Induced Cell Migration and Metastasis. Biomolecules. 2021; 11(10):1471. https://doi.org/10.3390/biom11101471

Chicago/Turabian Style

Ismail, Thamir M., Stephane R. Gross, Tara Lancaster, Philip S. Rudland, and Roger Barraclough. 2021. "The Role of the C-Terminal Lysine of S100P in S100P-Induced Cell Migration and Metastasis" Biomolecules 11, no. 10: 1471. https://doi.org/10.3390/biom11101471

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