Hornerin, an S100 family protein, is functional in breast cells and aberrantly expressed in breast cancer
<p<Abstract</p< <p<Background</p< <p<Recent evidence suggests an emerging role for S100 protein in breast cancer and tumor progression. These ubiquitous proteins are involved in numerous normal and pathological cell functions including inflammatory and immune responses,...
Ausführliche Beschreibung
Autor*in: |
Fleming Jodie M [verfasserIn] Ginsburg Erika [verfasserIn] Oliver Shannon D [verfasserIn] Goldsmith Paul [verfasserIn] Vonderhaar Barbara K [verfasserIn] |
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E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2012 |
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Übergeordnetes Werk: |
In: BMC Cancer - BMC, 2003, 12(2012), 1, p 266 |
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Übergeordnetes Werk: |
volume:12 ; year:2012 ; number:1, p 266 |
Links: |
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DOI / URN: |
10.1186/1471-2407-12-266 |
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Katalog-ID: |
DOAJ077097297 |
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520 | |a <p<Abstract</p< <p<Background</p< <p<Recent evidence suggests an emerging role for S100 protein in breast cancer and tumor progression. These ubiquitous proteins are involved in numerous normal and pathological cell functions including inflammatory and immune responses, Ca<sup<2+</sup< homeostasis, the dynamics of cytoskeleton constituents, as well as cell proliferation, differentiation, and death. Our previous proteomic analysis demonstrated the presence of hornerin, an S100 family member, in breast tissue and extracellular matrix. Hornerin has been reported in healthy skin as well as psoriatic and regenerating skin after wound healing, suggesting a role in inflammatory/immune response or proliferation. In the present study we investigated hornerin’s potential role in normal breast cells and breast cancer.</p< <p<Methods</p< <p<The expression levels and localization of hornerin in human breast tissue, breast tumor biopsies, primary breast cells and breast cancer cell lines, as well as murine mammary tissue were measured via immunohistochemistry, western blot analysis and PCR. Antibodies were developed against the N- and C-terminus of the protein for detection of proteolytic fragments and their specific subcellular localization via fluorescent immunocytochemisty. Lastly, cells were treated with H<sub<2</sub<O<sub<2</sub< to detect changes in hornerin expression during induction of apoptosis/necrosis.</p< <p<Results</p< <p<Breast epithelial cells and stromal fibroblasts and macrophages express hornerin and show unique regulation of expression during distinct phases of mammary development. Furthermore, hornerin expression is decreased in invasive ductal carcinomas compared to invasive lobular carcinomas and less aggressive breast carcinoma phenotypes, and cellular expression of hornerin is altered during induction of apoptosis. Finally, we demonstrate the presence of post-translational fragments that display differential subcellular localization.</p< <p<Conclusions</p< <p<Our data opens new possibilities for hornerin and its proteolytic fragments in the control of mammary cell function and breast cancer.</p< | ||
650 | 4 | |a Hornerin | |
650 | 4 | |a S100 protein | |
650 | 4 | |a Mammary gland | |
650 | 4 | |a Breast cancer | |
650 | 4 | |a Apoptosis | |
650 | 4 | |a Protein fragmentation | |
653 | 0 | |a Neoplasms. Tumors. Oncology. Including cancer and carcinogens | |
700 | 0 | |a Ginsburg Erika |e verfasserin |4 aut | |
700 | 0 | |a Oliver Shannon D |e verfasserin |4 aut | |
700 | 0 | |a Goldsmith Paul |e verfasserin |4 aut | |
700 | 0 | |a Vonderhaar Barbara K |e verfasserin |4 aut | |
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773 | 1 | 8 | |g volume:12 |g year:2012 |g number:1, p 266 |
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10.1186/1471-2407-12-266 doi (DE-627)DOAJ077097297 (DE-599)DOAJ24f9f937ef9047b7b0457b698941dcf4 DE-627 ger DE-627 rakwb eng RC254-282 Fleming Jodie M verfasserin aut Hornerin, an S100 family protein, is functional in breast cells and aberrantly expressed in breast cancer 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier <p<Abstract</p< <p<Background</p< <p<Recent evidence suggests an emerging role for S100 protein in breast cancer and tumor progression. These ubiquitous proteins are involved in numerous normal and pathological cell functions including inflammatory and immune responses, Ca<sup<2+</sup< homeostasis, the dynamics of cytoskeleton constituents, as well as cell proliferation, differentiation, and death. Our previous proteomic analysis demonstrated the presence of hornerin, an S100 family member, in breast tissue and extracellular matrix. Hornerin has been reported in healthy skin as well as psoriatic and regenerating skin after wound healing, suggesting a role in inflammatory/immune response or proliferation. In the present study we investigated hornerin’s potential role in normal breast cells and breast cancer.</p< <p<Methods</p< <p<The expression levels and localization of hornerin in human breast tissue, breast tumor biopsies, primary breast cells and breast cancer cell lines, as well as murine mammary tissue were measured via immunohistochemistry, western blot analysis and PCR. Antibodies were developed against the N- and C-terminus of the protein for detection of proteolytic fragments and their specific subcellular localization via fluorescent immunocytochemisty. Lastly, cells were treated with H<sub<2</sub<O<sub<2</sub< to detect changes in hornerin expression during induction of apoptosis/necrosis.</p< <p<Results</p< <p<Breast epithelial cells and stromal fibroblasts and macrophages express hornerin and show unique regulation of expression during distinct phases of mammary development. Furthermore, hornerin expression is decreased in invasive ductal carcinomas compared to invasive lobular carcinomas and less aggressive breast carcinoma phenotypes, and cellular expression of hornerin is altered during induction of apoptosis. Finally, we demonstrate the presence of post-translational fragments that display differential subcellular localization.</p< <p<Conclusions</p< <p<Our data opens new possibilities for hornerin and its proteolytic fragments in the control of mammary cell function and breast cancer.</p< Hornerin S100 protein Mammary gland Breast cancer Apoptosis Protein fragmentation Neoplasms. Tumors. Oncology. Including cancer and carcinogens Ginsburg Erika verfasserin aut Oliver Shannon D verfasserin aut Goldsmith Paul verfasserin aut Vonderhaar Barbara K verfasserin aut In BMC Cancer BMC, 2003 12(2012), 1, p 266 (DE-627)326643710 (DE-600)2041352-X 14712407 nnns volume:12 year:2012 number:1, p 266 https://doi.org/10.1186/1471-2407-12-266 kostenfrei https://doaj.org/article/24f9f937ef9047b7b0457b698941dcf4 kostenfrei http://www.biomedcentral.com/1471-2407/12/266 kostenfrei https://doaj.org/toc/1471-2407 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2012 1, p 266 |
spelling |
10.1186/1471-2407-12-266 doi (DE-627)DOAJ077097297 (DE-599)DOAJ24f9f937ef9047b7b0457b698941dcf4 DE-627 ger DE-627 rakwb eng RC254-282 Fleming Jodie M verfasserin aut Hornerin, an S100 family protein, is functional in breast cells and aberrantly expressed in breast cancer 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier <p<Abstract</p< <p<Background</p< <p<Recent evidence suggests an emerging role for S100 protein in breast cancer and tumor progression. These ubiquitous proteins are involved in numerous normal and pathological cell functions including inflammatory and immune responses, Ca<sup<2+</sup< homeostasis, the dynamics of cytoskeleton constituents, as well as cell proliferation, differentiation, and death. Our previous proteomic analysis demonstrated the presence of hornerin, an S100 family member, in breast tissue and extracellular matrix. Hornerin has been reported in healthy skin as well as psoriatic and regenerating skin after wound healing, suggesting a role in inflammatory/immune response or proliferation. In the present study we investigated hornerin’s potential role in normal breast cells and breast cancer.</p< <p<Methods</p< <p<The expression levels and localization of hornerin in human breast tissue, breast tumor biopsies, primary breast cells and breast cancer cell lines, as well as murine mammary tissue were measured via immunohistochemistry, western blot analysis and PCR. Antibodies were developed against the N- and C-terminus of the protein for detection of proteolytic fragments and their specific subcellular localization via fluorescent immunocytochemisty. Lastly, cells were treated with H<sub<2</sub<O<sub<2</sub< to detect changes in hornerin expression during induction of apoptosis/necrosis.</p< <p<Results</p< <p<Breast epithelial cells and stromal fibroblasts and macrophages express hornerin and show unique regulation of expression during distinct phases of mammary development. Furthermore, hornerin expression is decreased in invasive ductal carcinomas compared to invasive lobular carcinomas and less aggressive breast carcinoma phenotypes, and cellular expression of hornerin is altered during induction of apoptosis. Finally, we demonstrate the presence of post-translational fragments that display differential subcellular localization.</p< <p<Conclusions</p< <p<Our data opens new possibilities for hornerin and its proteolytic fragments in the control of mammary cell function and breast cancer.</p< Hornerin S100 protein Mammary gland Breast cancer Apoptosis Protein fragmentation Neoplasms. Tumors. Oncology. Including cancer and carcinogens Ginsburg Erika verfasserin aut Oliver Shannon D verfasserin aut Goldsmith Paul verfasserin aut Vonderhaar Barbara K verfasserin aut In BMC Cancer BMC, 2003 12(2012), 1, p 266 (DE-627)326643710 (DE-600)2041352-X 14712407 nnns volume:12 year:2012 number:1, p 266 https://doi.org/10.1186/1471-2407-12-266 kostenfrei https://doaj.org/article/24f9f937ef9047b7b0457b698941dcf4 kostenfrei http://www.biomedcentral.com/1471-2407/12/266 kostenfrei https://doaj.org/toc/1471-2407 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2012 1, p 266 |
allfields_unstemmed |
10.1186/1471-2407-12-266 doi (DE-627)DOAJ077097297 (DE-599)DOAJ24f9f937ef9047b7b0457b698941dcf4 DE-627 ger DE-627 rakwb eng RC254-282 Fleming Jodie M verfasserin aut Hornerin, an S100 family protein, is functional in breast cells and aberrantly expressed in breast cancer 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier <p<Abstract</p< <p<Background</p< <p<Recent evidence suggests an emerging role for S100 protein in breast cancer and tumor progression. These ubiquitous proteins are involved in numerous normal and pathological cell functions including inflammatory and immune responses, Ca<sup<2+</sup< homeostasis, the dynamics of cytoskeleton constituents, as well as cell proliferation, differentiation, and death. Our previous proteomic analysis demonstrated the presence of hornerin, an S100 family member, in breast tissue and extracellular matrix. Hornerin has been reported in healthy skin as well as psoriatic and regenerating skin after wound healing, suggesting a role in inflammatory/immune response or proliferation. In the present study we investigated hornerin’s potential role in normal breast cells and breast cancer.</p< <p<Methods</p< <p<The expression levels and localization of hornerin in human breast tissue, breast tumor biopsies, primary breast cells and breast cancer cell lines, as well as murine mammary tissue were measured via immunohistochemistry, western blot analysis and PCR. Antibodies were developed against the N- and C-terminus of the protein for detection of proteolytic fragments and their specific subcellular localization via fluorescent immunocytochemisty. Lastly, cells were treated with H<sub<2</sub<O<sub<2</sub< to detect changes in hornerin expression during induction of apoptosis/necrosis.</p< <p<Results</p< <p<Breast epithelial cells and stromal fibroblasts and macrophages express hornerin and show unique regulation of expression during distinct phases of mammary development. Furthermore, hornerin expression is decreased in invasive ductal carcinomas compared to invasive lobular carcinomas and less aggressive breast carcinoma phenotypes, and cellular expression of hornerin is altered during induction of apoptosis. Finally, we demonstrate the presence of post-translational fragments that display differential subcellular localization.</p< <p<Conclusions</p< <p<Our data opens new possibilities for hornerin and its proteolytic fragments in the control of mammary cell function and breast cancer.</p< Hornerin S100 protein Mammary gland Breast cancer Apoptosis Protein fragmentation Neoplasms. Tumors. Oncology. Including cancer and carcinogens Ginsburg Erika verfasserin aut Oliver Shannon D verfasserin aut Goldsmith Paul verfasserin aut Vonderhaar Barbara K verfasserin aut In BMC Cancer BMC, 2003 12(2012), 1, p 266 (DE-627)326643710 (DE-600)2041352-X 14712407 nnns volume:12 year:2012 number:1, p 266 https://doi.org/10.1186/1471-2407-12-266 kostenfrei https://doaj.org/article/24f9f937ef9047b7b0457b698941dcf4 kostenfrei http://www.biomedcentral.com/1471-2407/12/266 kostenfrei https://doaj.org/toc/1471-2407 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2012 1, p 266 |
allfieldsGer |
10.1186/1471-2407-12-266 doi (DE-627)DOAJ077097297 (DE-599)DOAJ24f9f937ef9047b7b0457b698941dcf4 DE-627 ger DE-627 rakwb eng RC254-282 Fleming Jodie M verfasserin aut Hornerin, an S100 family protein, is functional in breast cells and aberrantly expressed in breast cancer 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier <p<Abstract</p< <p<Background</p< <p<Recent evidence suggests an emerging role for S100 protein in breast cancer and tumor progression. These ubiquitous proteins are involved in numerous normal and pathological cell functions including inflammatory and immune responses, Ca<sup<2+</sup< homeostasis, the dynamics of cytoskeleton constituents, as well as cell proliferation, differentiation, and death. Our previous proteomic analysis demonstrated the presence of hornerin, an S100 family member, in breast tissue and extracellular matrix. Hornerin has been reported in healthy skin as well as psoriatic and regenerating skin after wound healing, suggesting a role in inflammatory/immune response or proliferation. In the present study we investigated hornerin’s potential role in normal breast cells and breast cancer.</p< <p<Methods</p< <p<The expression levels and localization of hornerin in human breast tissue, breast tumor biopsies, primary breast cells and breast cancer cell lines, as well as murine mammary tissue were measured via immunohistochemistry, western blot analysis and PCR. Antibodies were developed against the N- and C-terminus of the protein for detection of proteolytic fragments and their specific subcellular localization via fluorescent immunocytochemisty. Lastly, cells were treated with H<sub<2</sub<O<sub<2</sub< to detect changes in hornerin expression during induction of apoptosis/necrosis.</p< <p<Results</p< <p<Breast epithelial cells and stromal fibroblasts and macrophages express hornerin and show unique regulation of expression during distinct phases of mammary development. Furthermore, hornerin expression is decreased in invasive ductal carcinomas compared to invasive lobular carcinomas and less aggressive breast carcinoma phenotypes, and cellular expression of hornerin is altered during induction of apoptosis. Finally, we demonstrate the presence of post-translational fragments that display differential subcellular localization.</p< <p<Conclusions</p< <p<Our data opens new possibilities for hornerin and its proteolytic fragments in the control of mammary cell function and breast cancer.</p< Hornerin S100 protein Mammary gland Breast cancer Apoptosis Protein fragmentation Neoplasms. Tumors. Oncology. Including cancer and carcinogens Ginsburg Erika verfasserin aut Oliver Shannon D verfasserin aut Goldsmith Paul verfasserin aut Vonderhaar Barbara K verfasserin aut In BMC Cancer BMC, 2003 12(2012), 1, p 266 (DE-627)326643710 (DE-600)2041352-X 14712407 nnns volume:12 year:2012 number:1, p 266 https://doi.org/10.1186/1471-2407-12-266 kostenfrei https://doaj.org/article/24f9f937ef9047b7b0457b698941dcf4 kostenfrei http://www.biomedcentral.com/1471-2407/12/266 kostenfrei https://doaj.org/toc/1471-2407 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2012 1, p 266 |
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10.1186/1471-2407-12-266 doi (DE-627)DOAJ077097297 (DE-599)DOAJ24f9f937ef9047b7b0457b698941dcf4 DE-627 ger DE-627 rakwb eng RC254-282 Fleming Jodie M verfasserin aut Hornerin, an S100 family protein, is functional in breast cells and aberrantly expressed in breast cancer 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier <p<Abstract</p< <p<Background</p< <p<Recent evidence suggests an emerging role for S100 protein in breast cancer and tumor progression. These ubiquitous proteins are involved in numerous normal and pathological cell functions including inflammatory and immune responses, Ca<sup<2+</sup< homeostasis, the dynamics of cytoskeleton constituents, as well as cell proliferation, differentiation, and death. Our previous proteomic analysis demonstrated the presence of hornerin, an S100 family member, in breast tissue and extracellular matrix. Hornerin has been reported in healthy skin as well as psoriatic and regenerating skin after wound healing, suggesting a role in inflammatory/immune response or proliferation. In the present study we investigated hornerin’s potential role in normal breast cells and breast cancer.</p< <p<Methods</p< <p<The expression levels and localization of hornerin in human breast tissue, breast tumor biopsies, primary breast cells and breast cancer cell lines, as well as murine mammary tissue were measured via immunohistochemistry, western blot analysis and PCR. Antibodies were developed against the N- and C-terminus of the protein for detection of proteolytic fragments and their specific subcellular localization via fluorescent immunocytochemisty. Lastly, cells were treated with H<sub<2</sub<O<sub<2</sub< to detect changes in hornerin expression during induction of apoptosis/necrosis.</p< <p<Results</p< <p<Breast epithelial cells and stromal fibroblasts and macrophages express hornerin and show unique regulation of expression during distinct phases of mammary development. Furthermore, hornerin expression is decreased in invasive ductal carcinomas compared to invasive lobular carcinomas and less aggressive breast carcinoma phenotypes, and cellular expression of hornerin is altered during induction of apoptosis. Finally, we demonstrate the presence of post-translational fragments that display differential subcellular localization.</p< <p<Conclusions</p< <p<Our data opens new possibilities for hornerin and its proteolytic fragments in the control of mammary cell function and breast cancer.</p< Hornerin S100 protein Mammary gland Breast cancer Apoptosis Protein fragmentation Neoplasms. Tumors. Oncology. Including cancer and carcinogens Ginsburg Erika verfasserin aut Oliver Shannon D verfasserin aut Goldsmith Paul verfasserin aut Vonderhaar Barbara K verfasserin aut In BMC Cancer BMC, 2003 12(2012), 1, p 266 (DE-627)326643710 (DE-600)2041352-X 14712407 nnns volume:12 year:2012 number:1, p 266 https://doi.org/10.1186/1471-2407-12-266 kostenfrei https://doaj.org/article/24f9f937ef9047b7b0457b698941dcf4 kostenfrei http://www.biomedcentral.com/1471-2407/12/266 kostenfrei https://doaj.org/toc/1471-2407 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2012 1, p 266 |
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Hornerin, an S100 family protein, is functional in breast cells and aberrantly expressed in breast cancer |
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Hornerin, an S100 family protein, is functional in breast cells and aberrantly expressed in breast cancer |
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Fleming Jodie M |
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Fleming Jodie M Ginsburg Erika Oliver Shannon D Goldsmith Paul Vonderhaar Barbara K |
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hornerin, an s100 family protein, is functional in breast cells and aberrantly expressed in breast cancer |
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Hornerin, an S100 family protein, is functional in breast cells and aberrantly expressed in breast cancer |
abstract |
<p<Abstract</p< <p<Background</p< <p<Recent evidence suggests an emerging role for S100 protein in breast cancer and tumor progression. These ubiquitous proteins are involved in numerous normal and pathological cell functions including inflammatory and immune responses, Ca<sup<2+</sup< homeostasis, the dynamics of cytoskeleton constituents, as well as cell proliferation, differentiation, and death. Our previous proteomic analysis demonstrated the presence of hornerin, an S100 family member, in breast tissue and extracellular matrix. Hornerin has been reported in healthy skin as well as psoriatic and regenerating skin after wound healing, suggesting a role in inflammatory/immune response or proliferation. In the present study we investigated hornerin’s potential role in normal breast cells and breast cancer.</p< <p<Methods</p< <p<The expression levels and localization of hornerin in human breast tissue, breast tumor biopsies, primary breast cells and breast cancer cell lines, as well as murine mammary tissue were measured via immunohistochemistry, western blot analysis and PCR. Antibodies were developed against the N- and C-terminus of the protein for detection of proteolytic fragments and their specific subcellular localization via fluorescent immunocytochemisty. Lastly, cells were treated with H<sub<2</sub<O<sub<2</sub< to detect changes in hornerin expression during induction of apoptosis/necrosis.</p< <p<Results</p< <p<Breast epithelial cells and stromal fibroblasts and macrophages express hornerin and show unique regulation of expression during distinct phases of mammary development. Furthermore, hornerin expression is decreased in invasive ductal carcinomas compared to invasive lobular carcinomas and less aggressive breast carcinoma phenotypes, and cellular expression of hornerin is altered during induction of apoptosis. Finally, we demonstrate the presence of post-translational fragments that display differential subcellular localization.</p< <p<Conclusions</p< <p<Our data opens new possibilities for hornerin and its proteolytic fragments in the control of mammary cell function and breast cancer.</p< |
abstractGer |
<p<Abstract</p< <p<Background</p< <p<Recent evidence suggests an emerging role for S100 protein in breast cancer and tumor progression. These ubiquitous proteins are involved in numerous normal and pathological cell functions including inflammatory and immune responses, Ca<sup<2+</sup< homeostasis, the dynamics of cytoskeleton constituents, as well as cell proliferation, differentiation, and death. Our previous proteomic analysis demonstrated the presence of hornerin, an S100 family member, in breast tissue and extracellular matrix. Hornerin has been reported in healthy skin as well as psoriatic and regenerating skin after wound healing, suggesting a role in inflammatory/immune response or proliferation. In the present study we investigated hornerin’s potential role in normal breast cells and breast cancer.</p< <p<Methods</p< <p<The expression levels and localization of hornerin in human breast tissue, breast tumor biopsies, primary breast cells and breast cancer cell lines, as well as murine mammary tissue were measured via immunohistochemistry, western blot analysis and PCR. Antibodies were developed against the N- and C-terminus of the protein for detection of proteolytic fragments and their specific subcellular localization via fluorescent immunocytochemisty. Lastly, cells were treated with H<sub<2</sub<O<sub<2</sub< to detect changes in hornerin expression during induction of apoptosis/necrosis.</p< <p<Results</p< <p<Breast epithelial cells and stromal fibroblasts and macrophages express hornerin and show unique regulation of expression during distinct phases of mammary development. Furthermore, hornerin expression is decreased in invasive ductal carcinomas compared to invasive lobular carcinomas and less aggressive breast carcinoma phenotypes, and cellular expression of hornerin is altered during induction of apoptosis. Finally, we demonstrate the presence of post-translational fragments that display differential subcellular localization.</p< <p<Conclusions</p< <p<Our data opens new possibilities for hornerin and its proteolytic fragments in the control of mammary cell function and breast cancer.</p< |
abstract_unstemmed |
<p<Abstract</p< <p<Background</p< <p<Recent evidence suggests an emerging role for S100 protein in breast cancer and tumor progression. These ubiquitous proteins are involved in numerous normal and pathological cell functions including inflammatory and immune responses, Ca<sup<2+</sup< homeostasis, the dynamics of cytoskeleton constituents, as well as cell proliferation, differentiation, and death. Our previous proteomic analysis demonstrated the presence of hornerin, an S100 family member, in breast tissue and extracellular matrix. Hornerin has been reported in healthy skin as well as psoriatic and regenerating skin after wound healing, suggesting a role in inflammatory/immune response or proliferation. In the present study we investigated hornerin’s potential role in normal breast cells and breast cancer.</p< <p<Methods</p< <p<The expression levels and localization of hornerin in human breast tissue, breast tumor biopsies, primary breast cells and breast cancer cell lines, as well as murine mammary tissue were measured via immunohistochemistry, western blot analysis and PCR. Antibodies were developed against the N- and C-terminus of the protein for detection of proteolytic fragments and their specific subcellular localization via fluorescent immunocytochemisty. Lastly, cells were treated with H<sub<2</sub<O<sub<2</sub< to detect changes in hornerin expression during induction of apoptosis/necrosis.</p< <p<Results</p< <p<Breast epithelial cells and stromal fibroblasts and macrophages express hornerin and show unique regulation of expression during distinct phases of mammary development. Furthermore, hornerin expression is decreased in invasive ductal carcinomas compared to invasive lobular carcinomas and less aggressive breast carcinoma phenotypes, and cellular expression of hornerin is altered during induction of apoptosis. Finally, we demonstrate the presence of post-translational fragments that display differential subcellular localization.</p< <p<Conclusions</p< <p<Our data opens new possibilities for hornerin and its proteolytic fragments in the control of mammary cell function and breast cancer.</p< |
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