Differential subcellular localization renders HAI-2 a matriptase inhibitor in breast cancer cells but not in mammary epithelial cells
The type 2 transmembrane serine protease matriptase is under tight control primarily by the actions of the integral membrane Kunitz-type serine protease inhibitor HAI-1. Growing evidence indicates that HAI-2 might also be involved in matriptase inhibition in some contexts. Here we showed that matrip...
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| creator | Chang, Hsiang-Hua D Xu, Yuan Lai, Hongyu Yang, Xiaoyu Tseng, Chun-Che Lai, Ying-Jung J Pan, Yu Zhou, Emily Johnson, Michael D Wang, Jehng-Kang Lin, Chen-Yong |
| description | The type 2 transmembrane serine protease matriptase is under tight control primarily by the actions of the integral membrane Kunitz-type serine protease inhibitor HAI-1. Growing evidence indicates that HAI-2 might also be involved in matriptase inhibition in some contexts. Here we showed that matriptase inhibition by HAI-2 depends on the subcellular localizations of HAI-2, and is observed in breast cancer cells but not in mammary epithelial cells. HAI-2 is co-expressed with matriptase in 21 out of 26 human epithelial and carcinoma cells examined. HAI-2 is also a potent matriptase inhibitor in solution, but in spite of this, HAI-2 inhibition of matriptase is not observed in all contexts where HAI-2 is expressed, unlike what is seen for HAI-1. Induction of matriptase zymogen activation in mammary epithelial cells results in the formation of matriptase-HAI-1 complexes, but matriptase-HAI-2 complexes are not observed. In breast cancer cells, however, in addition to the appearance of matriptase-HAI-1 complex, three different matriptase-HAI-2 complexes, are formed following the induction of matriptase activation. Immunofluorescent staining reveals that activated matriptase is focused at the cell-cell junctions upon the induction of matriptase zymogen activation in both mammary epithelial cells and breast cancer cells. HAI-2, in contrast, remains localized in vesicle/granule-like structures during matriptase zymogen activation in human mammary epithelial cells. In breast cancer cells, however, a proportion of the HAI-2 reaches the cell surface where it can gain access to and inhibit active matriptase. Collectively, these data suggest that matriptase inhibition by HAI-2 requires the translocation of HAI-2 to the cell surface, a process which is observed in some breast cancer cells but not in mammary epithelial cells. |
| doi_str_mv | 10.1371/journal.pone.0120489 |
| format | Article |
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Growing evidence indicates that HAI-2 might also be involved in matriptase inhibition in some contexts. Here we showed that matriptase inhibition by HAI-2 depends on the subcellular localizations of HAI-2, and is observed in breast cancer cells but not in mammary epithelial cells. HAI-2 is co-expressed with matriptase in 21 out of 26 human epithelial and carcinoma cells examined. HAI-2 is also a potent matriptase inhibitor in solution, but in spite of this, HAI-2 inhibition of matriptase is not observed in all contexts where HAI-2 is expressed, unlike what is seen for HAI-1. Induction of matriptase zymogen activation in mammary epithelial cells results in the formation of matriptase-HAI-1 complexes, but matriptase-HAI-2 complexes are not observed. In breast cancer cells, however, in addition to the appearance of matriptase-HAI-1 complex, three different matriptase-HAI-2 complexes, are formed following the induction of matriptase activation. Immunofluorescent staining reveals that activated matriptase is focused at the cell-cell junctions upon the induction of matriptase zymogen activation in both mammary epithelial cells and breast cancer cells. HAI-2, in contrast, remains localized in vesicle/granule-like structures during matriptase zymogen activation in human mammary epithelial cells. In breast cancer cells, however, a proportion of the HAI-2 reaches the cell surface where it can gain access to and inhibit active matriptase. Collectively, these data suggest that matriptase inhibition by HAI-2 requires the translocation of HAI-2 to the cell surface, a process which is observed in some breast cancer cells but not in mammary epithelial cells.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0120489</identifier><identifier>PMID: 25786220</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Activation ; Biochemistry ; Breast cancer ; Cancer ; Cancer cells ; Cell junctions ; Cell Line ; Cell Line, Tumor ; Cell surface ; Cytoplasmic Granules - chemistry ; Cytoplasmic Granules - metabolism ; Enzyme Induction ; Enzyme Precursors - genetics ; Enzyme Precursors - metabolism ; Epithelial cells ; Epithelial Cells - enzymology ; Epithelial Cells - pathology ; Gene Expression ; Growth factors ; Humans ; Hydrogen-Ion Concentration ; Inhibition ; Intercellular Junctions - metabolism ; Localization ; Mammary gland ; Mammary Glands, Human - enzymology ; Mammary Glands, Human - pathology ; Membrane Glycoproteins - genetics ; Membrane Glycoproteins - metabolism ; Oncology ; Organ Specificity ; Physiology ; Proenzymes ; Protease ; Protease inhibitors ; Protein Binding ; Protein Transport ; Proteinase inhibitors ; Proteinase Inhibitory Proteins, Secretory - genetics ; Proteinase Inhibitory Proteins, Secretory - metabolism ; Proteins ; Rodents ; Serine ; Serine Endopeptidases - genetics ; Serine Endopeptidases - metabolism ; Serine proteinase ; Signal Transduction ; Thrombin ; Translocation</subject><ispartof>PloS one, 2015-03, Vol.10 (3), p.e0120489-e0120489</ispartof><rights>COPYRIGHT 2015 Public Library of Science</rights><rights>2015 Chang et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2015 Chang et al 2015 Chang et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c692t-6b9a41babd1e6fcab658d4f9504f10b823e774521c16cae52a2d2c8e6b1bef703</citedby><cites>FETCH-LOGICAL-c692t-6b9a41babd1e6fcab658d4f9504f10b823e774521c16cae52a2d2c8e6b1bef703</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4364774/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4364774/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,865,886,2103,2929,23871,27929,27930,53796,53798</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25786220$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Saleem, Mohammad</contributor><creatorcontrib>Chang, Hsiang-Hua D</creatorcontrib><creatorcontrib>Xu, Yuan</creatorcontrib><creatorcontrib>Lai, Hongyu</creatorcontrib><creatorcontrib>Yang, Xiaoyu</creatorcontrib><creatorcontrib>Tseng, Chun-Che</creatorcontrib><creatorcontrib>Lai, Ying-Jung J</creatorcontrib><creatorcontrib>Pan, Yu</creatorcontrib><creatorcontrib>Zhou, Emily</creatorcontrib><creatorcontrib>Johnson, Michael D</creatorcontrib><creatorcontrib>Wang, Jehng-Kang</creatorcontrib><creatorcontrib>Lin, Chen-Yong</creatorcontrib><title>Differential subcellular localization renders HAI-2 a matriptase inhibitor in breast cancer cells but not in mammary epithelial cells</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>The type 2 transmembrane serine protease matriptase is under tight control primarily by the actions of the integral membrane Kunitz-type serine protease inhibitor HAI-1. Growing evidence indicates that HAI-2 might also be involved in matriptase inhibition in some contexts. Here we showed that matriptase inhibition by HAI-2 depends on the subcellular localizations of HAI-2, and is observed in breast cancer cells but not in mammary epithelial cells. HAI-2 is co-expressed with matriptase in 21 out of 26 human epithelial and carcinoma cells examined. HAI-2 is also a potent matriptase inhibitor in solution, but in spite of this, HAI-2 inhibition of matriptase is not observed in all contexts where HAI-2 is expressed, unlike what is seen for HAI-1. Induction of matriptase zymogen activation in mammary epithelial cells results in the formation of matriptase-HAI-1 complexes, but matriptase-HAI-2 complexes are not observed. In breast cancer cells, however, in addition to the appearance of matriptase-HAI-1 complex, three different matriptase-HAI-2 complexes, are formed following the induction of matriptase activation. Immunofluorescent staining reveals that activated matriptase is focused at the cell-cell junctions upon the induction of matriptase zymogen activation in both mammary epithelial cells and breast cancer cells. HAI-2, in contrast, remains localized in vesicle/granule-like structures during matriptase zymogen activation in human mammary epithelial cells. In breast cancer cells, however, a proportion of the HAI-2 reaches the cell surface where it can gain access to and inhibit active matriptase. Collectively, these data suggest that matriptase inhibition by HAI-2 requires the translocation of HAI-2 to the cell surface, a process which is observed in some breast cancer cells but not in mammary epithelial cells.</description><subject>Activation</subject><subject>Biochemistry</subject><subject>Breast cancer</subject><subject>Cancer</subject><subject>Cancer cells</subject><subject>Cell junctions</subject><subject>Cell Line</subject><subject>Cell Line, Tumor</subject><subject>Cell surface</subject><subject>Cytoplasmic Granules - chemistry</subject><subject>Cytoplasmic Granules - metabolism</subject><subject>Enzyme Induction</subject><subject>Enzyme Precursors - genetics</subject><subject>Enzyme Precursors - metabolism</subject><subject>Epithelial cells</subject><subject>Epithelial Cells - enzymology</subject><subject>Epithelial Cells - pathology</subject><subject>Gene Expression</subject><subject>Growth factors</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Inhibition</subject><subject>Intercellular Junctions - metabolism</subject><subject>Localization</subject><subject>Mammary gland</subject><subject>Mammary Glands, Human - enzymology</subject><subject>Mammary Glands, Human - pathology</subject><subject>Membrane Glycoproteins - genetics</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Oncology</subject><subject>Organ Specificity</subject><subject>Physiology</subject><subject>Proenzymes</subject><subject>Protease</subject><subject>Protease inhibitors</subject><subject>Protein Binding</subject><subject>Protein Transport</subject><subject>Proteinase inhibitors</subject><subject>Proteinase Inhibitory Proteins, Secretory - genetics</subject><subject>Proteinase Inhibitory Proteins, Secretory - metabolism</subject><subject>Proteins</subject><subject>Rodents</subject><subject>Serine</subject><subject>Serine Endopeptidases - genetics</subject><subject>Serine Endopeptidases - 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inhibitor in breast cancer cells but not in mammary epithelial cells</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2015-03-18</date><risdate>2015</risdate><volume>10</volume><issue>3</issue><spage>e0120489</spage><epage>e0120489</epage><pages>e0120489-e0120489</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>The type 2 transmembrane serine protease matriptase is under tight control primarily by the actions of the integral membrane Kunitz-type serine protease inhibitor HAI-1. Growing evidence indicates that HAI-2 might also be involved in matriptase inhibition in some contexts. Here we showed that matriptase inhibition by HAI-2 depends on the subcellular localizations of HAI-2, and is observed in breast cancer cells but not in mammary epithelial cells. HAI-2 is co-expressed with matriptase in 21 out of 26 human epithelial and carcinoma cells examined. HAI-2 is also a potent matriptase inhibitor in solution, but in spite of this, HAI-2 inhibition of matriptase is not observed in all contexts where HAI-2 is expressed, unlike what is seen for HAI-1. Induction of matriptase zymogen activation in mammary epithelial cells results in the formation of matriptase-HAI-1 complexes, but matriptase-HAI-2 complexes are not observed. In breast cancer cells, however, in addition to the appearance of matriptase-HAI-1 complex, three different matriptase-HAI-2 complexes, are formed following the induction of matriptase activation. Immunofluorescent staining reveals that activated matriptase is focused at the cell-cell junctions upon the induction of matriptase zymogen activation in both mammary epithelial cells and breast cancer cells. HAI-2, in contrast, remains localized in vesicle/granule-like structures during matriptase zymogen activation in human mammary epithelial cells. In breast cancer cells, however, a proportion of the HAI-2 reaches the cell surface where it can gain access to and inhibit active matriptase. Collectively, these data suggest that matriptase inhibition by HAI-2 requires the translocation of HAI-2 to the cell surface, a process which is observed in some breast cancer cells but not in mammary epithelial cells.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>25786220</pmid><doi>10.1371/journal.pone.0120489</doi><tpages>e0120489</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2015-03, Vol.10 (3), p.e0120489-e0120489 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1664459782 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Public Library of Science (PLoS) Journals Open Access; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Activation Biochemistry Breast cancer Cancer Cancer cells Cell junctions Cell Line Cell Line, Tumor Cell surface Cytoplasmic Granules - chemistry Cytoplasmic Granules - metabolism Enzyme Induction Enzyme Precursors - genetics Enzyme Precursors - metabolism Epithelial cells Epithelial Cells - enzymology Epithelial Cells - pathology Gene Expression Growth factors Humans Hydrogen-Ion Concentration Inhibition Intercellular Junctions - metabolism Localization Mammary gland Mammary Glands, Human - enzymology Mammary Glands, Human - pathology Membrane Glycoproteins - genetics Membrane Glycoproteins - metabolism Oncology Organ Specificity Physiology Proenzymes Protease Protease inhibitors Protein Binding Protein Transport Proteinase inhibitors Proteinase Inhibitory Proteins, Secretory - genetics Proteinase Inhibitory Proteins, Secretory - metabolism Proteins Rodents Serine Serine Endopeptidases - genetics Serine Endopeptidases - metabolism Serine proteinase Signal Transduction Thrombin Translocation |
| title | Differential subcellular localization renders HAI-2 a matriptase inhibitor in breast cancer cells but not in mammary epithelial cells |
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