{"id":13510,"date":"2020-08-04T19:57:34","date_gmt":"2020-08-04T23:57:34","guid":{"rendered":"https:\/\/dev.inrs.ca\/professeurs\/professors\/yves-st-pierre\/"},"modified":"2021-07-23T09:23:40","modified_gmt":"2021-07-23T13:23:40","slug":"yves-st-pierre","status":"publish","type":"professor","link":"https:\/\/dev.inrs.ca\/en\/research\/professors\/yves-st-pierre\/","title":{"rendered":"Yves St-Pierre"},"author":1,"featured_media":55638,"parent":13241,"template":"","sectors":[678,679,729],"expertise":[855,857,905,906,858],"taxo_thematic":[1186,1189],"professor_program":[825,1196],"professor_education_offer":[1205],"expertise_groups":[1653,1652,1655,1660,1663,1685,1701,1683,1648],"class_list":["post-13510","professor","type-professor","status-publish","has-post-thumbnail","hentry","sectors-biotechnologie-en","sectors-sante-en","sectors-environnement-en","expertise-breast-cancer","expertise-cancer-and-metastases","expertise-galectin-mmp","expertise-galectins","expertise-haematological-cancers","taxo_thematic-infection-and-immunity","taxo_thematic-novel-therapeutic-and-preventive-agents","professor_program-biology","professor_program-experimental-health-sciences","professor_education_offer-for-students","expertise_groups-biochemistry-of-proteins-and-peptides","expertise_groups-biogeochemistry","expertise_groups-biomarkers","expertise_groups-cancer-en","expertise_groups-climate-change","expertise_groups-genetics-and-epigenetics","expertise_groups-immunology","expertise_groups-pregnancy-fertility-and-toxicology","expertise_groups-therapeutic-agents"],"acf":[],"yoast_head":"<!-- This site is optimized with the Yoast SEO Premium plugin v24.6 (Yoast SEO v24.6) - https:\/\/yoast.com\/wordpress\/plugins\/seo\/ -->\n<title>Yves St-Pierre | INRS<\/title>\n<meta name=\"description\" content=\"Research Interest\u00a0The roles of galectins in cancer.\u00a0Our research focuses on the role of galectins in cancer. Galectins represent a family of evolutionarily conserved animal lectins that are widely distributed from lower invertebrates to higher vertebrates. They were initially described in 1975 in the electric eel, Electrophorus electricus, as low molecular weight, \u03b2-galactoside binding proteins. Since then, galectins have been numbered according to the order of their discovery. The 15 family members are now classified according to their structure and number of carbohydrate recognition domains (CRDs). The prototype subfamily of galectins (galectin-1, -2, -5, -7, -10, -11, -13, -14, and -15) consists of a single CRD with a short N-terminal sequence. In this subfamily, the CRD exists as a monomer that noncovalently dimerizes in solution. The tandem-repeat type subfamily members (galectin-4, -6, -8, -9, and -12) are constitutively bivalent since their gene encodes one single protein displaying two non-identical CRDs joined by a short linker peptide sequence. There is also a chimeric form of galectin (galectin-3) that contains one CRD connected to a non-lectin domain, which helps in the formation of multimers that form disorganized heterogeneous cross-linked complexes. Sequencing of galectins isolated from amphibians, birds, fish, and mammals has revealed extensive sequence similarity. In addition to the presence of a CRD, all galectins harbour a highly conserved three-dimensional structure characterized by a jelly-roll topology composed of an 11- or 12-strand anti-parallel b-sandwich of approximately 135-140 amino acid residues. The main structural differences among galectins are located in the loop regions, which contain the main flexible areas of galectins. These structural differences between galectins are believed to be responsible for variations in their carbohydrate ligand specificity and their divergent function.\u00a0It is now well established that galectins are expressed at abnormally high levels in both tumour cells and peritumoral cells. Once released in the extracellular space, galectins binds to repeating units of high density O-glycans on the peptide backbone of membrane receptors, facilitating the packing of glycosylated receptors into an ordered cross-linked lattice at the cell surface. Such cross-linking of glycosylated receptors triggers cell death or activation of other signals that regulate cell fate. On immune cells, this cascade of events has been shown to regulate both innate and acquired immune responses by killing immune cells, helping tumors escape the anti-tumoral immune response. Overexpression of galectins by cancer cells thus contributes to local and systemic immunosuppression in cancer patients. Another means by which prototypic galectins contribute to cancer is via their binding to cell surface glycoreceptors expressed on cancer cells, protecting them from negative regulation via constitutive endocytosis. By doing so, sensitivity of tumour cells to growth factors is increased, promoting growth of cancer cells. Binding of galectins on cancer cells will also promote their invasive behavior by increasing cell motility and\/or by metastatic genes, such as mmp-9. \u00a0Most studies on galectins have focused on galectin-1 and -3. Our lab got interested on galectin-7 many years ago while comparing the transcriptome of highly metastatic and non-metastatic cancer cells. We were among the first research group to show that galectin-7 plays a central role in promoting cancer progression, at least for certain types of cancer, such as lymphoma, triple-negative breast cancer and high grade serous ovarian carcinoma. We are now exploring novel means by which we could inhibit the protumorigenic activity of galecitn-7. We are also exploring the relevance of less well known galectins in cancer, such as galectin-8, galectin-14 and others. We use in vitro cell models combined to genetic engineering to understand how they work. We are also using tissue microarrays constructed from tumour samples of patients with aggressive forms of cancer, most notably patients with high fatality cancers for which there is no effective treatments.\u00a0\u00a0The development of biomarkers for monitoring climate change. In recent years, our team has used its expertise in molecular immunology and in the development of biomarkers in humans to develop new molecular biomarkers to monitor the medium and long-term impacts of climate change and pollution on aquatic environments. For this purpose, we study cells of the immune system (hemocytes) of the blue mussel, an ideal sentinel species for studying the quality of marine environments. Our team is also interested in studying the role of galectins found in invertebrates (such as the blue mussels) to better understand how the functions of these proteins have developed through evolution. These activities are taking place in collaboration with Dr. St\u00e9phane Betoulle (University of Reims) and the Institut Polaire Paul-\u00c9mile Victor (IPEV).\u00a0\u00a0BiographyDr. Yves St-Pierre obtained his B.Sc in Biology from the Universit\u00e9 of Qu\u00e9bec at Montr\u00e9al in 1985, and his M.Sc. in Virology from the Institut Armand-Frappier in 1987.\u00a0 He obtained his Ph.D. in Immunology from the University of Toronto, in 1991. He has completed his postdoctoral training in the Department of Pathology at Harvard University. He is currently Professor at INRS-Institut Armand-Frappier.\u00a0Dr. St-Pierre is interested in the role of the galectins and extracellular proteases in cancer and inflammatory disorders.\u00a0\" \/>\n<meta name=\"robots\" content=\"noindex, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Yves St-Pierre | INRS\" \/>\n<meta property=\"og:description\" content=\"Research Interest\u00a0The roles of galectins in cancer.\u00a0Our research focuses on the role of galectins in cancer. Galectins represent a family of evolutionarily conserved animal lectins that are widely distributed from lower invertebrates to higher vertebrates. They were initially described in 1975 in the electric eel, Electrophorus electricus, as low molecular weight, \u03b2-galactoside binding proteins. Since then, galectins have been numbered according to the order of their discovery. The 15 family members are now classified according to their structure and number of carbohydrate recognition domains (CRDs). The prototype subfamily of galectins (galectin-1, -2, -5, -7, -10, -11, -13, -14, and -15) consists of a single CRD with a short N-terminal sequence. In this subfamily, the CRD exists as a monomer that noncovalently dimerizes in solution. The tandem-repeat type subfamily members (galectin-4, -6, -8, -9, and -12) are constitutively bivalent since their gene encodes one single protein displaying two non-identical CRDs joined by a short linker peptide sequence. There is also a chimeric form of galectin (galectin-3) that contains one CRD connected to a non-lectin domain, which helps in the formation of multimers that form disorganized heterogeneous cross-linked complexes. Sequencing of galectins isolated from amphibians, birds, fish, and mammals has revealed extensive sequence similarity. In addition to the presence of a CRD, all galectins harbour a highly conserved three-dimensional structure characterized by a jelly-roll topology composed of an 11- or 12-strand anti-parallel b-sandwich of approximately 135-140 amino acid residues. The main structural differences among galectins are located in the loop regions, which contain the main flexible areas of galectins. These structural differences between galectins are believed to be responsible for variations in their carbohydrate ligand specificity and their divergent function.\u00a0It is now well established that galectins are expressed at abnormally high levels in both tumour cells and peritumoral cells. Once released in the extracellular space, galectins binds to repeating units of high density O-glycans on the peptide backbone of membrane receptors, facilitating the packing of glycosylated receptors into an ordered cross-linked lattice at the cell surface. Such cross-linking of glycosylated receptors triggers cell death or activation of other signals that regulate cell fate. On immune cells, this cascade of events has been shown to regulate both innate and acquired immune responses by killing immune cells, helping tumors escape the anti-tumoral immune response. Overexpression of galectins by cancer cells thus contributes to local and systemic immunosuppression in cancer patients. Another means by which prototypic galectins contribute to cancer is via their binding to cell surface glycoreceptors expressed on cancer cells, protecting them from negative regulation via constitutive endocytosis. By doing so, sensitivity of tumour cells to growth factors is increased, promoting growth of cancer cells. Binding of galectins on cancer cells will also promote their invasive behavior by increasing cell motility and\/or by metastatic genes, such as mmp-9. \u00a0Most studies on galectins have focused on galectin-1 and -3. Our lab got interested on galectin-7 many years ago while comparing the transcriptome of highly metastatic and non-metastatic cancer cells. We were among the first research group to show that galectin-7 plays a central role in promoting cancer progression, at least for certain types of cancer, such as lymphoma, triple-negative breast cancer and high grade serous ovarian carcinoma. We are now exploring novel means by which we could inhibit the protumorigenic activity of galecitn-7. We are also exploring the relevance of less well known galectins in cancer, such as galectin-8, galectin-14 and others. We use in vitro cell models combined to genetic engineering to understand how they work. We are also using tissue microarrays constructed from tumour samples of patients with aggressive forms of cancer, most notably patients with high fatality cancers for which there is no effective treatments.\u00a0\u00a0The development of biomarkers for monitoring climate change. In recent years, our team has used its expertise in molecular immunology and in the development of biomarkers in humans to develop new molecular biomarkers to monitor the medium and long-term impacts of climate change and pollution on aquatic environments. For this purpose, we study cells of the immune system (hemocytes) of the blue mussel, an ideal sentinel species for studying the quality of marine environments. Our team is also interested in studying the role of galectins found in invertebrates (such as the blue mussels) to better understand how the functions of these proteins have developed through evolution. These activities are taking place in collaboration with Dr. St\u00e9phane Betoulle (University of Reims) and the Institut Polaire Paul-\u00c9mile Victor (IPEV).\u00a0\u00a0BiographyDr. Yves St-Pierre obtained his B.Sc in Biology from the Universit\u00e9 of Qu\u00e9bec at Montr\u00e9al in 1985, and his M.Sc. in Virology from the Institut Armand-Frappier in 1987.\u00a0 He obtained his Ph.D. in Immunology from the University of Toronto, in 1991. He has completed his postdoctoral training in the Department of Pathology at Harvard University. He is currently Professor at INRS-Institut Armand-Frappier.\u00a0Dr. St-Pierre is interested in the role of the galectins and extracellular proteases in cancer and inflammatory disorders.\u00a0\" \/>\n<meta property=\"og:url\" content=\"https:\/\/dev.inrs.ca\/en\/research\/professors\/yves-st-pierre\/\" \/>\n<meta property=\"og:site_name\" content=\"INRS\" \/>\n<meta property=\"article:publisher\" content=\"https:\/\/www.facebook.com\/inrsciences\/\" \/>\n<meta property=\"article:modified_time\" content=\"2021-07-23T13:23:40+00:00\" \/>\n<meta property=\"og:image\" content=\"https:\/\/dev.inrs.ca\/wp-content\/uploads\/yves-st-pierre-inrs-professor-professeur-scaled-e1625776520371.jpg\" \/>\n\t<meta property=\"og:image:width\" content=\"1943\" \/>\n\t<meta property=\"og:image:height\" content=\"2560\" \/>\n\t<meta property=\"og:image:type\" content=\"image\/jpeg\" \/>\n<meta name=\"twitter:card\" content=\"summary_large_image\" \/>\n<meta name=\"twitter:site\" content=\"@inrsciences\" \/>\n<script type=\"application\/ld+json\" class=\"yoast-schema-graph\">{\"@context\":\"https:\/\/schema.org\",\"@graph\":[{\"@type\":\"WebPage\",\"@id\":\"https:\/\/dev.inrs.ca\/en\/research\/professors\/yves-st-pierre\/\",\"url\":\"https:\/\/dev.inrs.ca\/en\/research\/professors\/yves-st-pierre\/\",\"name\":\"Yves St-Pierre | INRS\",\"isPartOf\":{\"@id\":\"https:\/\/dev.inrs.ca\/en\/#website\"},\"primaryImageOfPage\":{\"@id\":\"https:\/\/dev.inrs.ca\/en\/research\/professors\/yves-st-pierre\/#primaryimage\"},\"image\":{\"@id\":\"https:\/\/dev.inrs.ca\/en\/research\/professors\/yves-st-pierre\/#primaryimage\"},\"thumbnailUrl\":\"https:\/\/dev.inrs.ca\/wp-content\/uploads\/yves-st-pierre-inrs-professor-professeur-scaled-e1625776520371.jpg\",\"datePublished\":\"2020-08-04T23:57:34+00:00\",\"dateModified\":\"2021-07-23T13:23:40+00:00\",\"description\":\"Research Interest\u00a0The roles of galectins in cancer.\u00a0Our research focuses on the role of galectins in cancer. Galectins represent a family of evolutionarily conserved animal lectins that are widely distributed from lower invertebrates to higher vertebrates. They were initially described in 1975 in the electric eel, Electrophorus electricus, as low molecular weight, \u03b2-galactoside binding proteins. Since then, galectins have been numbered according to the order of their discovery. The 15 family members are now classified according to their structure and number of carbohydrate recognition domains (CRDs). The prototype subfamily of galectins (galectin-1, -2, -5, -7, -10, -11, -13, -14, and -15) consists of a single CRD with a short N-terminal sequence. In this subfamily, the CRD exists as a monomer that noncovalently dimerizes in solution. The tandem-repeat type subfamily members (galectin-4, -6, -8, -9, and -12) are constitutively bivalent since their gene encodes one single protein displaying two non-identical CRDs joined by a short linker peptide sequence. There is also a chimeric form of galectin (galectin-3) that contains one CRD connected to a non-lectin domain, which helps in the formation of multimers that form disorganized heterogeneous cross-linked complexes. Sequencing of galectins isolated from amphibians, birds, fish, and mammals has revealed extensive sequence similarity. In addition to the presence of a CRD, all galectins harbour a highly conserved three-dimensional structure characterized by a jelly-roll topology composed of an 11- or 12-strand anti-parallel b-sandwich of approximately 135-140 amino acid residues. The main structural differences among galectins are located in the loop regions, which contain the main flexible areas of galectins. These structural differences between galectins are believed to be responsible for variations in their carbohydrate ligand specificity and their divergent function.\u00a0It is now well established that galectins are expressed at abnormally high levels in both tumour cells and peritumoral cells. Once released in the extracellular space, galectins binds to repeating units of high density O-glycans on the peptide backbone of membrane receptors, facilitating the packing of glycosylated receptors into an ordered cross-linked lattice at the cell surface. Such cross-linking of glycosylated receptors triggers cell death or activation of other signals that regulate cell fate. On immune cells, this cascade of events has been shown to regulate both innate and acquired immune responses by killing immune cells, helping tumors escape the anti-tumoral immune response. Overexpression of galectins by cancer cells thus contributes to local and systemic immunosuppression in cancer patients. Another means by which prototypic galectins contribute to cancer is via their binding to cell surface glycoreceptors expressed on cancer cells, protecting them from negative regulation via constitutive endocytosis. By doing so, sensitivity of tumour cells to growth factors is increased, promoting growth of cancer cells. Binding of galectins on cancer cells will also promote their invasive behavior by increasing cell motility and\/or by metastatic genes, such as mmp-9. \u00a0Most studies on galectins have focused on galectin-1 and -3. Our lab got interested on galectin-7 many years ago while comparing the transcriptome of highly metastatic and non-metastatic cancer cells. We were among the first research group to show that galectin-7 plays a central role in promoting cancer progression, at least for certain types of cancer, such as lymphoma, triple-negative breast cancer and high grade serous ovarian carcinoma. We are now exploring novel means by which we could inhibit the protumorigenic activity of galecitn-7. We are also exploring the relevance of less well known galectins in cancer, such as galectin-8, galectin-14 and others. We use in vitro cell models combined to genetic engineering to understand how they work. We are also using tissue microarrays constructed from tumour samples of patients with aggressive forms of cancer, most notably patients with high fatality cancers for which there is no effective treatments.\u00a0\u00a0The development of biomarkers for monitoring climate change. In recent years, our team has used its expertise in molecular immunology and in the development of biomarkers in humans to develop new molecular biomarkers to monitor the medium and long-term impacts of climate change and pollution on aquatic environments. For this purpose, we study cells of the immune system (hemocytes) of the blue mussel, an ideal sentinel species for studying the quality of marine environments. Our team is also interested in studying the role of galectins found in invertebrates (such as the blue mussels) to better understand how the functions of these proteins have developed through evolution. These activities are taking place in collaboration with Dr. St\u00e9phane Betoulle (University of Reims) and the Institut Polaire Paul-\u00c9mile Victor (IPEV).\u00a0\u00a0BiographyDr. Yves St-Pierre obtained his B.Sc in Biology from the Universit\u00e9 of Qu\u00e9bec at Montr\u00e9al in 1985, and his M.Sc. in Virology from the Institut Armand-Frappier in 1987.\u00a0 He obtained his Ph.D. in Immunology from the University of Toronto, in 1991. He has completed his postdoctoral training in the Department of Pathology at Harvard University. He is currently Professor at INRS-Institut Armand-Frappier.\u00a0Dr. St-Pierre is interested in the role of the galectins and extracellular proteases in cancer and inflammatory disorders.\u00a0\",\"breadcrumb\":{\"@id\":\"https:\/\/dev.inrs.ca\/en\/research\/professors\/yves-st-pierre\/#breadcrumb\"},\"inLanguage\":\"en-CA\",\"potentialAction\":[{\"@type\":\"ReadAction\",\"target\":[\"https:\/\/dev.inrs.ca\/en\/research\/professors\/yves-st-pierre\/\"]}]},{\"@type\":\"ImageObject\",\"inLanguage\":\"en-CA\",\"@id\":\"https:\/\/dev.inrs.ca\/en\/research\/professors\/yves-st-pierre\/#primaryimage\",\"url\":\"https:\/\/dev.inrs.ca\/wp-content\/uploads\/yves-st-pierre-inrs-professor-professeur-scaled-e1625776520371.jpg\",\"contentUrl\":\"https:\/\/dev.inrs.ca\/wp-content\/uploads\/yves-st-pierre-inrs-professor-professeur-scaled-e1625776520371.jpg\",\"width\":1943,\"height\":2560},{\"@type\":\"BreadcrumbList\",\"@id\":\"https:\/\/dev.inrs.ca\/en\/research\/professors\/yves-st-pierre\/#breadcrumb\",\"itemListElement\":[{\"@type\":\"ListItem\",\"position\":1,\"name\":\"Research\",\"item\":\"https:\/\/dev.inrs.ca\/la-recherche\/\"},{\"@type\":\"ListItem\",\"position\":2,\"name\":\"Professors\",\"item\":\"https:\/\/dev.inrs.ca\/la-recherche\/professeurs\/\"},{\"@type\":\"ListItem\",\"position\":3,\"name\":\"Yves St-Pierre\"}]},{\"@type\":\"WebSite\",\"@id\":\"https:\/\/dev.inrs.ca\/en\/#website\",\"url\":\"https:\/\/dev.inrs.ca\/en\/\",\"name\":\"INRS\",\"description\":\"Institut national de la recherche scientifique\",\"potentialAction\":[{\"@type\":\"SearchAction\",\"target\":{\"@type\":\"EntryPoint\",\"urlTemplate\":\"https:\/\/dev.inrs.ca\/en\/?s={search_term_string}\"},\"query-input\":{\"@type\":\"PropertyValueSpecification\",\"valueRequired\":true,\"valueName\":\"search_term_string\"}}],\"inLanguage\":\"en-CA\"}]}<\/script>\n<!-- \/ Yoast SEO Premium plugin. -->","yoast_head_json":{"title":"Yves St-Pierre | INRS","description":"Research Interest\u00a0The roles of galectins in cancer.\u00a0Our research focuses on the role of galectins in cancer. Galectins represent a family of evolutionarily conserved animal lectins that are widely distributed from lower invertebrates to higher vertebrates. They were initially described in 1975 in the electric eel, Electrophorus electricus, as low molecular weight, \u03b2-galactoside binding proteins. Since then, galectins have been numbered according to the order of their discovery. The 15 family members are now classified according to their structure and number of carbohydrate recognition domains (CRDs). The prototype subfamily of galectins (galectin-1, -2, -5, -7, -10, -11, -13, -14, and -15) consists of a single CRD with a short N-terminal sequence. In this subfamily, the CRD exists as a monomer that noncovalently dimerizes in solution. The tandem-repeat type subfamily members (galectin-4, -6, -8, -9, and -12) are constitutively bivalent since their gene encodes one single protein displaying two non-identical CRDs joined by a short linker peptide sequence. There is also a chimeric form of galectin (galectin-3) that contains one CRD connected to a non-lectin domain, which helps in the formation of multimers that form disorganized heterogeneous cross-linked complexes. Sequencing of galectins isolated from amphibians, birds, fish, and mammals has revealed extensive sequence similarity. In addition to the presence of a CRD, all galectins harbour a highly conserved three-dimensional structure characterized by a jelly-roll topology composed of an 11- or 12-strand anti-parallel b-sandwich of approximately 135-140 amino acid residues. The main structural differences among galectins are located in the loop regions, which contain the main flexible areas of galectins. These structural differences between galectins are believed to be responsible for variations in their carbohydrate ligand specificity and their divergent function.\u00a0It is now well established that galectins are expressed at abnormally high levels in both tumour cells and peritumoral cells. Once released in the extracellular space, galectins binds to repeating units of high density O-glycans on the peptide backbone of membrane receptors, facilitating the packing of glycosylated receptors into an ordered cross-linked lattice at the cell surface. Such cross-linking of glycosylated receptors triggers cell death or activation of other signals that regulate cell fate. On immune cells, this cascade of events has been shown to regulate both innate and acquired immune responses by killing immune cells, helping tumors escape the anti-tumoral immune response. Overexpression of galectins by cancer cells thus contributes to local and systemic immunosuppression in cancer patients. Another means by which prototypic galectins contribute to cancer is via their binding to cell surface glycoreceptors expressed on cancer cells, protecting them from negative regulation via constitutive endocytosis. By doing so, sensitivity of tumour cells to growth factors is increased, promoting growth of cancer cells. Binding of galectins on cancer cells will also promote their invasive behavior by increasing cell motility and\/or by metastatic genes, such as mmp-9. \u00a0Most studies on galectins have focused on galectin-1 and -3. Our lab got interested on galectin-7 many years ago while comparing the transcriptome of highly metastatic and non-metastatic cancer cells. We were among the first research group to show that galectin-7 plays a central role in promoting cancer progression, at least for certain types of cancer, such as lymphoma, triple-negative breast cancer and high grade serous ovarian carcinoma. We are now exploring novel means by which we could inhibit the protumorigenic activity of galecitn-7. We are also exploring the relevance of less well known galectins in cancer, such as galectin-8, galectin-14 and others. We use in vitro cell models combined to genetic engineering to understand how they work. We are also using tissue microarrays constructed from tumour samples of patients with aggressive forms of cancer, most notably patients with high fatality cancers for which there is no effective treatments.\u00a0\u00a0The development of biomarkers for monitoring climate change. In recent years, our team has used its expertise in molecular immunology and in the development of biomarkers in humans to develop new molecular biomarkers to monitor the medium and long-term impacts of climate change and pollution on aquatic environments. For this purpose, we study cells of the immune system (hemocytes) of the blue mussel, an ideal sentinel species for studying the quality of marine environments. Our team is also interested in studying the role of galectins found in invertebrates (such as the blue mussels) to better understand how the functions of these proteins have developed through evolution. These activities are taking place in collaboration with Dr. St\u00e9phane Betoulle (University of Reims) and the Institut Polaire Paul-\u00c9mile Victor (IPEV).\u00a0\u00a0BiographyDr. Yves St-Pierre obtained his B.Sc in Biology from the Universit\u00e9 of Qu\u00e9bec at Montr\u00e9al in 1985, and his M.Sc. in Virology from the Institut Armand-Frappier in 1987.\u00a0 He obtained his Ph.D. in Immunology from the University of Toronto, in 1991. He has completed his postdoctoral training in the Department of Pathology at Harvard University. He is currently Professor at INRS-Institut Armand-Frappier.\u00a0Dr. St-Pierre is interested in the role of the galectins and extracellular proteases in cancer and inflammatory disorders.\u00a0","robots":{"index":"noindex","follow":"follow","max-snippet":"max-snippet:-1","max-image-preview":"max-image-preview:large","max-video-preview":"max-video-preview:-1"},"og_locale":"en_US","og_type":"article","og_title":"Yves St-Pierre | INRS","og_description":"Research Interest\u00a0The roles of galectins in cancer.\u00a0Our research focuses on the role of galectins in cancer. Galectins represent a family of evolutionarily conserved animal lectins that are widely distributed from lower invertebrates to higher vertebrates. They were initially described in 1975 in the electric eel, Electrophorus electricus, as low molecular weight, \u03b2-galactoside binding proteins. Since then, galectins have been numbered according to the order of their discovery. The 15 family members are now classified according to their structure and number of carbohydrate recognition domains (CRDs). The prototype subfamily of galectins (galectin-1, -2, -5, -7, -10, -11, -13, -14, and -15) consists of a single CRD with a short N-terminal sequence. In this subfamily, the CRD exists as a monomer that noncovalently dimerizes in solution. The tandem-repeat type subfamily members (galectin-4, -6, -8, -9, and -12) are constitutively bivalent since their gene encodes one single protein displaying two non-identical CRDs joined by a short linker peptide sequence. There is also a chimeric form of galectin (galectin-3) that contains one CRD connected to a non-lectin domain, which helps in the formation of multimers that form disorganized heterogeneous cross-linked complexes. Sequencing of galectins isolated from amphibians, birds, fish, and mammals has revealed extensive sequence similarity. In addition to the presence of a CRD, all galectins harbour a highly conserved three-dimensional structure characterized by a jelly-roll topology composed of an 11- or 12-strand anti-parallel b-sandwich of approximately 135-140 amino acid residues. The main structural differences among galectins are located in the loop regions, which contain the main flexible areas of galectins. These structural differences between galectins are believed to be responsible for variations in their carbohydrate ligand specificity and their divergent function.\u00a0It is now well established that galectins are expressed at abnormally high levels in both tumour cells and peritumoral cells. Once released in the extracellular space, galectins binds to repeating units of high density O-glycans on the peptide backbone of membrane receptors, facilitating the packing of glycosylated receptors into an ordered cross-linked lattice at the cell surface. Such cross-linking of glycosylated receptors triggers cell death or activation of other signals that regulate cell fate. On immune cells, this cascade of events has been shown to regulate both innate and acquired immune responses by killing immune cells, helping tumors escape the anti-tumoral immune response. Overexpression of galectins by cancer cells thus contributes to local and systemic immunosuppression in cancer patients. Another means by which prototypic galectins contribute to cancer is via their binding to cell surface glycoreceptors expressed on cancer cells, protecting them from negative regulation via constitutive endocytosis. By doing so, sensitivity of tumour cells to growth factors is increased, promoting growth of cancer cells. Binding of galectins on cancer cells will also promote their invasive behavior by increasing cell motility and\/or by metastatic genes, such as mmp-9. \u00a0Most studies on galectins have focused on galectin-1 and -3. Our lab got interested on galectin-7 many years ago while comparing the transcriptome of highly metastatic and non-metastatic cancer cells. We were among the first research group to show that galectin-7 plays a central role in promoting cancer progression, at least for certain types of cancer, such as lymphoma, triple-negative breast cancer and high grade serous ovarian carcinoma. We are now exploring novel means by which we could inhibit the protumorigenic activity of galecitn-7. We are also exploring the relevance of less well known galectins in cancer, such as galectin-8, galectin-14 and others. We use in vitro cell models combined to genetic engineering to understand how they work. We are also using tissue microarrays constructed from tumour samples of patients with aggressive forms of cancer, most notably patients with high fatality cancers for which there is no effective treatments.\u00a0\u00a0The development of biomarkers for monitoring climate change. In recent years, our team has used its expertise in molecular immunology and in the development of biomarkers in humans to develop new molecular biomarkers to monitor the medium and long-term impacts of climate change and pollution on aquatic environments. For this purpose, we study cells of the immune system (hemocytes) of the blue mussel, an ideal sentinel species for studying the quality of marine environments. Our team is also interested in studying the role of galectins found in invertebrates (such as the blue mussels) to better understand how the functions of these proteins have developed through evolution. These activities are taking place in collaboration with Dr. St\u00e9phane Betoulle (University of Reims) and the Institut Polaire Paul-\u00c9mile Victor (IPEV).\u00a0\u00a0BiographyDr. Yves St-Pierre obtained his B.Sc in Biology from the Universit\u00e9 of Qu\u00e9bec at Montr\u00e9al in 1985, and his M.Sc. in Virology from the Institut Armand-Frappier in 1987.\u00a0 He obtained his Ph.D. in Immunology from the University of Toronto, in 1991. He has completed his postdoctoral training in the Department of Pathology at Harvard University. He is currently Professor at INRS-Institut Armand-Frappier.\u00a0Dr. St-Pierre is interested in the role of the galectins and extracellular proteases in cancer and inflammatory disorders.\u00a0","og_url":"https:\/\/dev.inrs.ca\/en\/research\/professors\/yves-st-pierre\/","og_site_name":"INRS","article_publisher":"https:\/\/www.facebook.com\/inrsciences\/","article_modified_time":"2021-07-23T13:23:40+00:00","og_image":[{"width":1943,"height":2560,"url":"https:\/\/dev.inrs.ca\/wp-content\/uploads\/yves-st-pierre-inrs-professor-professeur-scaled-e1625776520371.jpg","type":"image\/jpeg"}],"twitter_card":"summary_large_image","twitter_site":"@inrsciences","schema":{"@context":"https:\/\/schema.org","@graph":[{"@type":"WebPage","@id":"https:\/\/dev.inrs.ca\/en\/research\/professors\/yves-st-pierre\/","url":"https:\/\/dev.inrs.ca\/en\/research\/professors\/yves-st-pierre\/","name":"Yves St-Pierre | INRS","isPartOf":{"@id":"https:\/\/dev.inrs.ca\/en\/#website"},"primaryImageOfPage":{"@id":"https:\/\/dev.inrs.ca\/en\/research\/professors\/yves-st-pierre\/#primaryimage"},"image":{"@id":"https:\/\/dev.inrs.ca\/en\/research\/professors\/yves-st-pierre\/#primaryimage"},"thumbnailUrl":"https:\/\/dev.inrs.ca\/wp-content\/uploads\/yves-st-pierre-inrs-professor-professeur-scaled-e1625776520371.jpg","datePublished":"2020-08-04T23:57:34+00:00","dateModified":"2021-07-23T13:23:40+00:00","description":"Research Interest\u00a0The roles of galectins in cancer.\u00a0Our research focuses on the role of galectins in cancer. Galectins represent a family of evolutionarily conserved animal lectins that are widely distributed from lower invertebrates to higher vertebrates. They were initially described in 1975 in the electric eel, Electrophorus electricus, as low molecular weight, \u03b2-galactoside binding proteins. Since then, galectins have been numbered according to the order of their discovery. The 15 family members are now classified according to their structure and number of carbohydrate recognition domains (CRDs). The prototype subfamily of galectins (galectin-1, -2, -5, -7, -10, -11, -13, -14, and -15) consists of a single CRD with a short N-terminal sequence. In this subfamily, the CRD exists as a monomer that noncovalently dimerizes in solution. The tandem-repeat type subfamily members (galectin-4, -6, -8, -9, and -12) are constitutively bivalent since their gene encodes one single protein displaying two non-identical CRDs joined by a short linker peptide sequence. There is also a chimeric form of galectin (galectin-3) that contains one CRD connected to a non-lectin domain, which helps in the formation of multimers that form disorganized heterogeneous cross-linked complexes. Sequencing of galectins isolated from amphibians, birds, fish, and mammals has revealed extensive sequence similarity. In addition to the presence of a CRD, all galectins harbour a highly conserved three-dimensional structure characterized by a jelly-roll topology composed of an 11- or 12-strand anti-parallel b-sandwich of approximately 135-140 amino acid residues. The main structural differences among galectins are located in the loop regions, which contain the main flexible areas of galectins. These structural differences between galectins are believed to be responsible for variations in their carbohydrate ligand specificity and their divergent function.\u00a0It is now well established that galectins are expressed at abnormally high levels in both tumour cells and peritumoral cells. Once released in the extracellular space, galectins binds to repeating units of high density O-glycans on the peptide backbone of membrane receptors, facilitating the packing of glycosylated receptors into an ordered cross-linked lattice at the cell surface. Such cross-linking of glycosylated receptors triggers cell death or activation of other signals that regulate cell fate. On immune cells, this cascade of events has been shown to regulate both innate and acquired immune responses by killing immune cells, helping tumors escape the anti-tumoral immune response. Overexpression of galectins by cancer cells thus contributes to local and systemic immunosuppression in cancer patients. Another means by which prototypic galectins contribute to cancer is via their binding to cell surface glycoreceptors expressed on cancer cells, protecting them from negative regulation via constitutive endocytosis. By doing so, sensitivity of tumour cells to growth factors is increased, promoting growth of cancer cells. Binding of galectins on cancer cells will also promote their invasive behavior by increasing cell motility and\/or by metastatic genes, such as mmp-9. \u00a0Most studies on galectins have focused on galectin-1 and -3. Our lab got interested on galectin-7 many years ago while comparing the transcriptome of highly metastatic and non-metastatic cancer cells. We were among the first research group to show that galectin-7 plays a central role in promoting cancer progression, at least for certain types of cancer, such as lymphoma, triple-negative breast cancer and high grade serous ovarian carcinoma. We are now exploring novel means by which we could inhibit the protumorigenic activity of galecitn-7. We are also exploring the relevance of less well known galectins in cancer, such as galectin-8, galectin-14 and others. We use in vitro cell models combined to genetic engineering to understand how they work. We are also using tissue microarrays constructed from tumour samples of patients with aggressive forms of cancer, most notably patients with high fatality cancers for which there is no effective treatments.\u00a0\u00a0The development of biomarkers for monitoring climate change. In recent years, our team has used its expertise in molecular immunology and in the development of biomarkers in humans to develop new molecular biomarkers to monitor the medium and long-term impacts of climate change and pollution on aquatic environments. For this purpose, we study cells of the immune system (hemocytes) of the blue mussel, an ideal sentinel species for studying the quality of marine environments. Our team is also interested in studying the role of galectins found in invertebrates (such as the blue mussels) to better understand how the functions of these proteins have developed through evolution. These activities are taking place in collaboration with Dr. St\u00e9phane Betoulle (University of Reims) and the Institut Polaire Paul-\u00c9mile Victor (IPEV).\u00a0\u00a0BiographyDr. Yves St-Pierre obtained his B.Sc in Biology from the Universit\u00e9 of Qu\u00e9bec at Montr\u00e9al in 1985, and his M.Sc. in Virology from the Institut Armand-Frappier in 1987.\u00a0 He obtained his Ph.D. in Immunology from the University of Toronto, in 1991. He has completed his postdoctoral training in the Department of Pathology at Harvard University. He is currently Professor at INRS-Institut Armand-Frappier.\u00a0Dr. St-Pierre is interested in the role of the galectins and extracellular proteases in cancer and inflammatory disorders.\u00a0","breadcrumb":{"@id":"https:\/\/dev.inrs.ca\/en\/research\/professors\/yves-st-pierre\/#breadcrumb"},"inLanguage":"en-CA","potentialAction":[{"@type":"ReadAction","target":["https:\/\/dev.inrs.ca\/en\/research\/professors\/yves-st-pierre\/"]}]},{"@type":"ImageObject","inLanguage":"en-CA","@id":"https:\/\/dev.inrs.ca\/en\/research\/professors\/yves-st-pierre\/#primaryimage","url":"https:\/\/dev.inrs.ca\/wp-content\/uploads\/yves-st-pierre-inrs-professor-professeur-scaled-e1625776520371.jpg","contentUrl":"https:\/\/dev.inrs.ca\/wp-content\/uploads\/yves-st-pierre-inrs-professor-professeur-scaled-e1625776520371.jpg","width":1943,"height":2560},{"@type":"BreadcrumbList","@id":"https:\/\/dev.inrs.ca\/en\/research\/professors\/yves-st-pierre\/#breadcrumb","itemListElement":[{"@type":"ListItem","position":1,"name":"Research","item":"https:\/\/dev.inrs.ca\/la-recherche\/"},{"@type":"ListItem","position":2,"name":"Professors","item":"https:\/\/dev.inrs.ca\/la-recherche\/professeurs\/"},{"@type":"ListItem","position":3,"name":"Yves St-Pierre"}]},{"@type":"WebSite","@id":"https:\/\/dev.inrs.ca\/en\/#website","url":"https:\/\/dev.inrs.ca\/en\/","name":"INRS","description":"Institut national de la recherche scientifique","potentialAction":[{"@type":"SearchAction","target":{"@type":"EntryPoint","urlTemplate":"https:\/\/dev.inrs.ca\/en\/?s={search_term_string}"},"query-input":{"@type":"PropertyValueSpecification","valueRequired":true,"valueName":"search_term_string"}}],"inLanguage":"en-CA"}]}},"_links":{"self":[{"href":"https:\/\/dev.inrs.ca\/en\/wp-json\/wp\/v2\/professor\/13510","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/dev.inrs.ca\/en\/wp-json\/wp\/v2\/professor"}],"about":[{"href":"https:\/\/dev.inrs.ca\/en\/wp-json\/wp\/v2\/types\/professor"}],"author":[{"embeddable":true,"href":"https:\/\/dev.inrs.ca\/en\/wp-json\/wp\/v2\/users\/1"}],"up":[{"embeddable":true,"href":"https:\/\/dev.inrs.ca\/en\/wp-json\/wp\/v2\/pages\/13241"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/dev.inrs.ca\/en\/wp-json\/wp\/v2\/media\/55638"}],"wp:attachment":[{"href":"https:\/\/dev.inrs.ca\/en\/wp-json\/wp\/v2\/media?parent=13510"}],"wp:term":[{"taxonomy":"sectors","embeddable":true,"href":"https:\/\/dev.inrs.ca\/en\/wp-json\/wp\/v2\/sectors?post=13510"},{"taxonomy":"expertise","embeddable":true,"href":"https:\/\/dev.inrs.ca\/en\/wp-json\/wp\/v2\/expertise?post=13510"},{"taxonomy":"taxo_thematic","embeddable":true,"href":"https:\/\/dev.inrs.ca\/en\/wp-json\/wp\/v2\/taxo_thematic?post=13510"},{"taxonomy":"professor_program","embeddable":true,"href":"https:\/\/dev.inrs.ca\/en\/wp-json\/wp\/v2\/professor_program?post=13510"},{"taxonomy":"professor_education_offer","embeddable":true,"href":"https:\/\/dev.inrs.ca\/en\/wp-json\/wp\/v2\/professor_education_offer?post=13510"},{"taxonomy":"expertise_groups","embeddable":true,"href":"https:\/\/dev.inrs.ca\/en\/wp-json\/wp\/v2\/expertise_groups?post=13510"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}