Unexpected deeds of familiar proteins: Interplay of Hsp70, PGRP S / Tag7, and S100A4 / Mts1 in host vs. cancer combat

Dukhanina, E. A.; Yashin, Denis V.; Galkin, Andrey; Sashchenko, Lidia P.

doi:10.4161/cc.9.4.10782

Cited by 15 publications

(17 citation statements)

References 28 publications

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“…Several of S100 proteins are up-regulated or differentially expressed in human tumors and exhibit tumor-promoting activities [14,[19][20][21]. While elevated S100A4 expression level has been reported in several types of human cancers and exhibit metastasis-promoting activities [19,[22][23][24][25][26], detailed mechanisms underlying S100A4's role in regulating proliferation and metastasis of tumor cells remain to be fully elucidated. Thus, a further investigation into the role of S100A4 in OS is warranted.…”

Section: Introductionmentioning

confidence: 99%

The E-F Hand Calcium-Binding Protein S100A4 Regulates the Proliferation, Survival and Differentiation Potential of Human Osteosarcoma Cells

Chen

Luther

Zhang

et al. 2013

Cell Physiol Biochem

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This is an Open Access article licensed under the terms of the Creative Commons AttributionNonCommercial 3.0 Unported license (CC BY-NC) (www.karger.com/OA-license), applicable to the online version of the article only. Distribution permitted for non-commercial purposes only. Abstract Background/Aims: Osteosarcoma (OS) is the most common primary bone malignancy in children and young adults. Molecular mechanisms underlying the pathogenesis of OS remain to be fully understood. Several members of the E-F hand calcium-binding S100 protein family are differentially expressed in human cancers. We previously showed that S100A6 is highly expressed in OS tumors. In this study, we investigated the role of S100A4 in regulating OS proliferation and osteogenic differentiation. Methods/Results: Endogenous S100 expression was examined by semi-quantitative PCR in human OS lines. Adenoviral vector-mediated overexpression and RNAi knockdown of S100A4 were used to assess S100A4's effects on cell proliferation, migration and invasion and osteogenic differentiation. Apoptosis was assessed by using anti-caspase-3 immunostaining and flow cytometry with annexin V staining. Early osteogenic marker alkaline phosphatase (ALP) and late markers osteocalcin (OCN) and osteopontin (OPN) were assessed to determine the status of osteogenic differentiation. We found that S100A4 was elevated in metastatic MG63.2 cells. S100A4 knockdown inhibited cell proliferation, prolonged cell doubling time, and induced significant apoptosis. Silencing S100A4 expression in OS cells delayed cell wounding closure and diminished the numbers of migrated OS cells in transwell invasion assay. Furthermore, silencing S100A4 expression stimulated ALP

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Section: Introductionmentioning

confidence: 99%

The E-F Hand Calcium-Binding Protein S100A4 Regulates the Proliferation, Survival and Differentiation Potential of Human Osteosarcoma Cells

Chen

Luther

Zhang

et al. 2013

Cell Physiol Biochem

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“…9, 17 Moreover, we have found 2 additional proteins that can interact with Tag7: the Ca 2C -binding protein S100A4 (Mts1), encoded by the gene that is highly expressed in metastatic tumors and cells of the immune system, and the cochaperone HspBP1, which inhibits the ATPase activity of Hsp70. [18][19][20][21] Their interaction with Tag7 results in the suppression of cytotoxicity of the Tag-Hsp70 complex.…”

Section: Introductionmentioning

confidence: 99%

A new role for PGRP-S (Tag7) in immune defense: lymphocyte migration is induced by a chemoattractant complex of Tag7 with Mts1

et al. 2015

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“…In addition to the aforementioned recognition and lysis of Hsp70+ K562 cells, Tag7 in complex with the Mts1 protein can attract NK cells and lymphocytes to the focus of infection [16] . Moreover, it interacts with Hsp70 to form the cytotoxic Tag7-Hsp70 complex capable of killing tumor cells [17] , which binds to the known TNFR1 death receptor expressed on their surface [18] .…”

Section: Introductionmentioning

confidence: 99%

Innate Immunity Protein Tag7 Induces 3 Distinct Populations of Cytotoxic Cells That Use Different Mechanisms to Exhibit Their Antitumor Activity on Human Leukocyte Antigen-Deficient Cancer Cells

et al. 2017

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The search for new immune response mechanisms capable of controlling immune-evasive tumor cells devoid of the MHC antigen is a challenging task for immunologists. In this study, we found that the treatment of human peripheral blood lymphocytes with the innate immunity protein Tag7 (PGRP-S, PGLYRP1) induces differentiation of the populations of NK (natural killer) cells and CD8+ and CD4+ T lymphocytes that are cytotoxic for human leukocyte antigen-negative tumor cells. These populations employ different mechanisms of tumor cell lysis (based on the release of granzymes in the case of NK cells and on the FasL-Fas interaction in the case of CD8+ and CD4+ T lymphocytes) and induce different death pathways (apoptosis or necroptosis) in tumor cells. An analysis of genes activated in leukocyte populations after Tag7 treatment and experiments with specific inhibitors have shown that the TREM-1 receptor expressed on the monocyte cell surface is essential for activation of cytotoxic activity. Overall, the results of this study provide evidence for a novel role of the Tag7 protein in the immune response.

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Unexpected deeds of familiar proteins: Interplay of Hsp70, PGRP S / Tag7, and S100A4 / Mts1 in host vs. cancer combat

Cited by 15 publications

References 28 publications

The E-F Hand Calcium-Binding Protein S100A4 Regulates the Proliferation, Survival and Differentiation Potential of Human Osteosarcoma Cells

The E-F Hand Calcium-Binding Protein S100A4 Regulates the Proliferation, Survival and Differentiation Potential of Human Osteosarcoma Cells

A new role for PGRP-S (Tag7) in immune defense: lymphocyte migration is induced by a chemoattractant complex of Tag7 with Mts1

Innate Immunity Protein Tag7 Induces 3 Distinct Populations of Cytotoxic Cells That Use Different Mechanisms to Exhibit Their Antitumor Activity on Human Leukocyte Antigen-Deficient Cancer Cells

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