Interactions between carboxypeptidase M and kinin B1 receptor in endothelial cells
Introduction Carboxypeptidase M (CPM) is a glycosylphosphatidylinositol anchored enzyme that plays an important role in the kallikrein–kinin system (KKS). CPM catalytic domain hydrolyzes Arg from C-terminal peptides (i.e., bradykinin and kallidin), generating des-Arg-kinins, the agonists of B 1 rece...
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| Veröffentlicht in: | Inflammation research 2019-10, Vol.68 (10), p.845-855 |
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| creator | Guimarães, Paola Bianchi da Silva, Rafael Filippelli Hoff, Carolina Caldas Fernandes, Liliam Nakaie, Clovis Ryuichi Chagas, Jair Ribeiro Carmona, Adriana Karaoglanovic Bader, Michael Pesquero, João Bosco |
| description | Introduction
Carboxypeptidase M (CPM) is a glycosylphosphatidylinositol anchored enzyme that plays an important role in the kallikrein–kinin system (KKS). CPM catalytic domain hydrolyzes Arg from C-terminal peptides (i.e., bradykinin and kallidin), generating des-Arg-kinins, the agonists of B
1
receptor (B
1
R). It is known that CPM and kinin B
1
R are co-localized in the plasma membrane microdomains, where they interact with each other, facilitating receptor signaling.
Aims
We hypothesized here that this CPM-B
1
R interaction could also affect the activity of the enzyme.
Methods
Thus, in this work, we evaluated the impact of B
1
R presence or absence on CPM activity and expression, using primary culture of microvascular endothelial cells from wild-type, kinin B
1
R knockout mice (B
1
−/−
), and transgenic rats overexpressing B
1
receptor exclusively in the endothelium. In addition, HEK293T cells, as wells as B
1
−/−
primary culture of endothelial cells, both transfected with B
1
R, were also used.
Results
CPM expression and activity were downregulated in cells of knockout mice compared to control and this reduction was rescued after B
1
R transfection. Cells overexpressing B
1
R presented higher levels of CPM mRNA, protein, and activity. This profile was reverted by pre-incubation with the B
1
R antagonist, R715, in highly expressing receptor cells.
Conclusions
Our data show that kinin B
1
R positively modulates both CPM expression and activity, suggesting that CPM-B
1
R interaction in membrane microdomains might affect enzyme activity, beyond interfering in receptors signaling. This work highlights the interactions among different components of KKS and contributes to a better understanding of its patho-physiological role. |
| doi_str_mv | 10.1007/s00011-019-01264-6 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2244145940</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2244145940</sourcerecordid><originalsourceid>FETCH-LOGICAL-c375t-d4c8351b596cfc30d228cbe48bf8ecb0e541817e2beac1b36475491b1da55893</originalsourceid><addsrcrecordid>eNp9kE1LAzEQhoMotlb_gAcJePGymkmyu9mjih8FRZAevIUkO9XVbbYmW9R_b2qrggcPIQnzzDvDQ8g-sGNgrDyJjDGAjEGVDi9kVmyQIUjOsoqph830ZlxkQgk2IDsxPidcccW3yUAAByWlHJL7se8xGNc3nY_UYv-G6KkzwXbvH3Oc901tItJbanxNXxrfeHoGNKBLpS7Q9EVfd_0Tto1pqcO2jbtka2raiHvre0QmlxeT8-vs5u5qfH56kzlR5n1WS6dEDjavCjd1gtWcK2dRKjtV6CzDXIKCErlF48CKQpa5rMBCbfJcVWJEjlax89C9LjD2etbE5QLGY7eImnMpQeaVZAk9_IM-d4vg03JLSkBZCFEmiq8oF7oYA071PDQzEz40ML0UrlfCdRKuv4TrIjUdrKMXdob1T8u34QSIFRBTyT9i-J39T-wnFSqKtw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2243176337</pqid></control><display><type>article</type><title>Interactions between carboxypeptidase M and kinin B1 receptor in endothelial cells</title><source>MEDLINE</source><source>Springer Online Journals Complete</source><creator>Guimarães, Paola Bianchi ; da Silva, Rafael Filippelli ; Hoff, Carolina Caldas ; Fernandes, Liliam ; Nakaie, Clovis Ryuichi ; Chagas, Jair Ribeiro ; Carmona, Adriana Karaoglanovic ; Bader, Michael ; Pesquero, João Bosco</creator><creatorcontrib>Guimarães, Paola Bianchi ; da Silva, Rafael Filippelli ; Hoff, Carolina Caldas ; Fernandes, Liliam ; Nakaie, Clovis Ryuichi ; Chagas, Jair Ribeiro ; Carmona, Adriana Karaoglanovic ; Bader, Michael ; Pesquero, João Bosco</creatorcontrib><description>Introduction
Carboxypeptidase M (CPM) is a glycosylphosphatidylinositol anchored enzyme that plays an important role in the kallikrein–kinin system (KKS). CPM catalytic domain hydrolyzes Arg from C-terminal peptides (i.e., bradykinin and kallidin), generating des-Arg-kinins, the agonists of B
1
receptor (B
1
R). It is known that CPM and kinin B
1
R are co-localized in the plasma membrane microdomains, where they interact with each other, facilitating receptor signaling.
Aims
We hypothesized here that this CPM-B
1
R interaction could also affect the activity of the enzyme.
Methods
Thus, in this work, we evaluated the impact of B
1
R presence or absence on CPM activity and expression, using primary culture of microvascular endothelial cells from wild-type, kinin B
1
R knockout mice (B
1
−/−
), and transgenic rats overexpressing B
1
receptor exclusively in the endothelium. In addition, HEK293T cells, as wells as B
1
−/−
primary culture of endothelial cells, both transfected with B
1
R, were also used.
Results
CPM expression and activity were downregulated in cells of knockout mice compared to control and this reduction was rescued after B
1
R transfection. Cells overexpressing B
1
R presented higher levels of CPM mRNA, protein, and activity. This profile was reverted by pre-incubation with the B
1
R antagonist, R715, in highly expressing receptor cells.
Conclusions
Our data show that kinin B
1
R positively modulates both CPM expression and activity, suggesting that CPM-B
1
R interaction in membrane microdomains might affect enzyme activity, beyond interfering in receptors signaling. This work highlights the interactions among different components of KKS and contributes to a better understanding of its patho-physiological role.</description><identifier>ISSN: 1023-3830</identifier><identifier>EISSN: 1420-908X</identifier><identifier>DOI: 10.1007/s00011-019-01264-6</identifier><identifier>PMID: 31218444</identifier><language>eng</language><publisher>Cham: Springer International Publishing</publisher><subject>Allergology ; Animals ; Biomedical and Life Sciences ; Biomedicine ; Bradykinin ; Carboxypeptidase ; Carboxypeptidase M ; Catalysis ; Cell culture ; Cells, Cultured ; Dermatology ; Endothelial cells ; Endothelial Cells - metabolism ; Endothelium ; Enzymatic activity ; Enzyme activity ; Enzymes ; Glycosylphosphatidylinositol ; GPI-Linked Proteins - genetics ; GPI-Linked Proteins - metabolism ; Humans ; Immunology ; Kallikrein ; Kinins ; Lung - cytology ; Metalloendopeptidases - genetics ; Metalloendopeptidases - metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Microvasculature ; mRNA ; Neurology ; Original Research Paper ; Peptides ; Pharmacology/Toxicology ; Rats, Sprague-Dawley ; Rats, Transgenic ; Receptor, Bradykinin B1 - genetics ; Receptor, Bradykinin B1 - metabolism ; Receptors ; Rheumatology ; Signaling ; Transfection ; Transgenic mice</subject><ispartof>Inflammation research, 2019-10, Vol.68 (10), p.845-855</ispartof><rights>Springer Nature Switzerland AG 2019</rights><rights>Inflammation Research is a copyright of Springer, (2019). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-d4c8351b596cfc30d228cbe48bf8ecb0e541817e2beac1b36475491b1da55893</citedby><cites>FETCH-LOGICAL-c375t-d4c8351b596cfc30d228cbe48bf8ecb0e541817e2beac1b36475491b1da55893</cites><orcidid>0000-0002-4507-632X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00011-019-01264-6$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00011-019-01264-6$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31218444$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Guimarães, Paola Bianchi</creatorcontrib><creatorcontrib>da Silva, Rafael Filippelli</creatorcontrib><creatorcontrib>Hoff, Carolina Caldas</creatorcontrib><creatorcontrib>Fernandes, Liliam</creatorcontrib><creatorcontrib>Nakaie, Clovis Ryuichi</creatorcontrib><creatorcontrib>Chagas, Jair Ribeiro</creatorcontrib><creatorcontrib>Carmona, Adriana Karaoglanovic</creatorcontrib><creatorcontrib>Bader, Michael</creatorcontrib><creatorcontrib>Pesquero, João Bosco</creatorcontrib><title>Interactions between carboxypeptidase M and kinin B1 receptor in endothelial cells</title><title>Inflammation research</title><addtitle>Inflamm. Res</addtitle><addtitle>Inflamm Res</addtitle><description>Introduction
Carboxypeptidase M (CPM) is a glycosylphosphatidylinositol anchored enzyme that plays an important role in the kallikrein–kinin system (KKS). CPM catalytic domain hydrolyzes Arg from C-terminal peptides (i.e., bradykinin and kallidin), generating des-Arg-kinins, the agonists of B
1
receptor (B
1
R). It is known that CPM and kinin B
1
R are co-localized in the plasma membrane microdomains, where they interact with each other, facilitating receptor signaling.
Aims
We hypothesized here that this CPM-B
1
R interaction could also affect the activity of the enzyme.
Methods
Thus, in this work, we evaluated the impact of B
1
R presence or absence on CPM activity and expression, using primary culture of microvascular endothelial cells from wild-type, kinin B
1
R knockout mice (B
1
−/−
), and transgenic rats overexpressing B
1
receptor exclusively in the endothelium. In addition, HEK293T cells, as wells as B
1
−/−
primary culture of endothelial cells, both transfected with B
1
R, were also used.
Results
CPM expression and activity were downregulated in cells of knockout mice compared to control and this reduction was rescued after B
1
R transfection. Cells overexpressing B
1
R presented higher levels of CPM mRNA, protein, and activity. This profile was reverted by pre-incubation with the B
1
R antagonist, R715, in highly expressing receptor cells.
Conclusions
Our data show that kinin B
1
R positively modulates both CPM expression and activity, suggesting that CPM-B
1
R interaction in membrane microdomains might affect enzyme activity, beyond interfering in receptors signaling. This work highlights the interactions among different components of KKS and contributes to a better understanding of its patho-physiological role.</description><subject>Allergology</subject><subject>Animals</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Bradykinin</subject><subject>Carboxypeptidase</subject><subject>Carboxypeptidase M</subject><subject>Catalysis</subject><subject>Cell culture</subject><subject>Cells, Cultured</subject><subject>Dermatology</subject><subject>Endothelial cells</subject><subject>Endothelial Cells - metabolism</subject><subject>Endothelium</subject><subject>Enzymatic activity</subject><subject>Enzyme activity</subject><subject>Enzymes</subject><subject>Glycosylphosphatidylinositol</subject><subject>GPI-Linked Proteins - genetics</subject><subject>GPI-Linked Proteins - metabolism</subject><subject>Humans</subject><subject>Immunology</subject><subject>Kallikrein</subject><subject>Kinins</subject><subject>Lung - cytology</subject><subject>Metalloendopeptidases - genetics</subject><subject>Metalloendopeptidases - metabolism</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Mice, Knockout</subject><subject>Microvasculature</subject><subject>mRNA</subject><subject>Neurology</subject><subject>Original Research Paper</subject><subject>Peptides</subject><subject>Pharmacology/Toxicology</subject><subject>Rats, Sprague-Dawley</subject><subject>Rats, Transgenic</subject><subject>Receptor, Bradykinin B1 - genetics</subject><subject>Receptor, Bradykinin B1 - metabolism</subject><subject>Receptors</subject><subject>Rheumatology</subject><subject>Signaling</subject><subject>Transfection</subject><subject>Transgenic mice</subject><issn>1023-3830</issn><issn>1420-908X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><recordid>eNp9kE1LAzEQhoMotlb_gAcJePGymkmyu9mjih8FRZAevIUkO9XVbbYmW9R_b2qrggcPIQnzzDvDQ8g-sGNgrDyJjDGAjEGVDi9kVmyQIUjOsoqph830ZlxkQgk2IDsxPidcccW3yUAAByWlHJL7se8xGNc3nY_UYv-G6KkzwXbvH3Oc901tItJbanxNXxrfeHoGNKBLpS7Q9EVfd_0Tto1pqcO2jbtka2raiHvre0QmlxeT8-vs5u5qfH56kzlR5n1WS6dEDjavCjd1gtWcK2dRKjtV6CzDXIKCErlF48CKQpa5rMBCbfJcVWJEjlax89C9LjD2etbE5QLGY7eImnMpQeaVZAk9_IM-d4vg03JLSkBZCFEmiq8oF7oYA071PDQzEz40ML0UrlfCdRKuv4TrIjUdrKMXdob1T8u34QSIFRBTyT9i-J39T-wnFSqKtw</recordid><startdate>20191001</startdate><enddate>20191001</enddate><creator>Guimarães, Paola Bianchi</creator><creator>da Silva, Rafael Filippelli</creator><creator>Hoff, Carolina Caldas</creator><creator>Fernandes, Liliam</creator><creator>Nakaie, Clovis Ryuichi</creator><creator>Chagas, Jair Ribeiro</creator><creator>Carmona, Adriana Karaoglanovic</creator><creator>Bader, Michael</creator><creator>Pesquero, João Bosco</creator><general>Springer International Publishing</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7T5</scope><scope>7T7</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>BENPR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>H94</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-4507-632X</orcidid></search><sort><creationdate>20191001</creationdate><title>Interactions between carboxypeptidase M and kinin B1 receptor in endothelial cells</title><author>Guimarães, Paola Bianchi ; da Silva, Rafael Filippelli ; Hoff, Carolina Caldas ; Fernandes, Liliam ; Nakaie, Clovis Ryuichi ; Chagas, Jair Ribeiro ; Carmona, Adriana Karaoglanovic ; Bader, Michael ; Pesquero, João Bosco</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-d4c8351b596cfc30d228cbe48bf8ecb0e541817e2beac1b36475491b1da55893</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Allergology</topic><topic>Animals</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Bradykinin</topic><topic>Carboxypeptidase</topic><topic>Carboxypeptidase M</topic><topic>Catalysis</topic><topic>Cell culture</topic><topic>Cells, Cultured</topic><topic>Dermatology</topic><topic>Endothelial cells</topic><topic>Endothelial Cells - metabolism</topic><topic>Endothelium</topic><topic>Enzymatic activity</topic><topic>Enzyme activity</topic><topic>Enzymes</topic><topic>Glycosylphosphatidylinositol</topic><topic>GPI-Linked Proteins - genetics</topic><topic>GPI-Linked Proteins - metabolism</topic><topic>Humans</topic><topic>Immunology</topic><topic>Kallikrein</topic><topic>Kinins</topic><topic>Lung - cytology</topic><topic>Metalloendopeptidases - genetics</topic><topic>Metalloendopeptidases - metabolism</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Mice, Knockout</topic><topic>Microvasculature</topic><topic>mRNA</topic><topic>Neurology</topic><topic>Original Research Paper</topic><topic>Peptides</topic><topic>Pharmacology/Toxicology</topic><topic>Rats, Sprague-Dawley</topic><topic>Rats, Transgenic</topic><topic>Receptor, Bradykinin B1 - genetics</topic><topic>Receptor, Bradykinin B1 - metabolism</topic><topic>Receptors</topic><topic>Rheumatology</topic><topic>Signaling</topic><topic>Transfection</topic><topic>Transgenic mice</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Guimarães, Paola Bianchi</creatorcontrib><creatorcontrib>da Silva, Rafael Filippelli</creatorcontrib><creatorcontrib>Hoff, Carolina Caldas</creatorcontrib><creatorcontrib>Fernandes, Liliam</creatorcontrib><creatorcontrib>Nakaie, Clovis Ryuichi</creatorcontrib><creatorcontrib>Chagas, Jair Ribeiro</creatorcontrib><creatorcontrib>Carmona, Adriana Karaoglanovic</creatorcontrib><creatorcontrib>Bader, Michael</creatorcontrib><creatorcontrib>Pesquero, João Bosco</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><jtitle>Inflammation research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Guimarães, Paola Bianchi</au><au>da Silva, Rafael Filippelli</au><au>Hoff, Carolina Caldas</au><au>Fernandes, Liliam</au><au>Nakaie, Clovis Ryuichi</au><au>Chagas, Jair Ribeiro</au><au>Carmona, Adriana Karaoglanovic</au><au>Bader, Michael</au><au>Pesquero, João Bosco</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interactions between carboxypeptidase M and kinin B1 receptor in endothelial cells</atitle><jtitle>Inflammation research</jtitle><stitle>Inflamm. Res</stitle><addtitle>Inflamm Res</addtitle><date>2019-10-01</date><risdate>2019</risdate><volume>68</volume><issue>10</issue><spage>845</spage><epage>855</epage><pages>845-855</pages><issn>1023-3830</issn><eissn>1420-908X</eissn><abstract>Introduction
Carboxypeptidase M (CPM) is a glycosylphosphatidylinositol anchored enzyme that plays an important role in the kallikrein–kinin system (KKS). CPM catalytic domain hydrolyzes Arg from C-terminal peptides (i.e., bradykinin and kallidin), generating des-Arg-kinins, the agonists of B
1
receptor (B
1
R). It is known that CPM and kinin B
1
R are co-localized in the plasma membrane microdomains, where they interact with each other, facilitating receptor signaling.
Aims
We hypothesized here that this CPM-B
1
R interaction could also affect the activity of the enzyme.
Methods
Thus, in this work, we evaluated the impact of B
1
R presence or absence on CPM activity and expression, using primary culture of microvascular endothelial cells from wild-type, kinin B
1
R knockout mice (B
1
−/−
), and transgenic rats overexpressing B
1
receptor exclusively in the endothelium. In addition, HEK293T cells, as wells as B
1
−/−
primary culture of endothelial cells, both transfected with B
1
R, were also used.
Results
CPM expression and activity were downregulated in cells of knockout mice compared to control and this reduction was rescued after B
1
R transfection. Cells overexpressing B
1
R presented higher levels of CPM mRNA, protein, and activity. This profile was reverted by pre-incubation with the B
1
R antagonist, R715, in highly expressing receptor cells.
Conclusions
Our data show that kinin B
1
R positively modulates both CPM expression and activity, suggesting that CPM-B
1
R interaction in membrane microdomains might affect enzyme activity, beyond interfering in receptors signaling. This work highlights the interactions among different components of KKS and contributes to a better understanding of its patho-physiological role.</abstract><cop>Cham</cop><pub>Springer International Publishing</pub><pmid>31218444</pmid><doi>10.1007/s00011-019-01264-6</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0002-4507-632X</orcidid></addata></record> |
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| ispartof | Inflammation research, 2019-10, Vol.68 (10), p.845-855 |
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| language | eng |
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| source | MEDLINE; Springer Online Journals Complete |
| subjects | Allergology Animals Biomedical and Life Sciences Biomedicine Bradykinin Carboxypeptidase Carboxypeptidase M Catalysis Cell culture Cells, Cultured Dermatology Endothelial cells Endothelial Cells - metabolism Endothelium Enzymatic activity Enzyme activity Enzymes Glycosylphosphatidylinositol GPI-Linked Proteins - genetics GPI-Linked Proteins - metabolism Humans Immunology Kallikrein Kinins Lung - cytology Metalloendopeptidases - genetics Metalloendopeptidases - metabolism Mice Mice, Inbred C57BL Mice, Knockout Microvasculature mRNA Neurology Original Research Paper Peptides Pharmacology/Toxicology Rats, Sprague-Dawley Rats, Transgenic Receptor, Bradykinin B1 - genetics Receptor, Bradykinin B1 - metabolism Receptors Rheumatology Signaling Transfection Transgenic mice |
| title | Interactions between carboxypeptidase M and kinin B1 receptor in endothelial cells |
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