2091-P: Effects of Caveolin-1 on the Synthesis and Decomposition of Islet ß-Cell IAPP and Its Mechanism
Objective: Islet amyloid polypeptide(IAPP) is a major component of islet amyloid deposition in type 2 diabetic patients. Our preliminary study showed that membrane protein Caveolin-1 (Cav1) silencing inhibited β-cell apoptosis and promote insulin secretion. The purpose of this study was to investiga...
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| Veröffentlicht in: | Diabetes (New York, N.Y.) N.Y.), 2020-06, Vol.69 (Supplement_1) |
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| container_title | Diabetes (New York, N.Y.) |
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| creator | LIU, KUNYING ZENG, WEN LIN, SHUO LIN, CHUWEN XU, FEN CAI, NAN ZENG, LONGYI |
| description | Objective: Islet amyloid polypeptide(IAPP) is a major component of islet amyloid deposition in type 2 diabetic patients. Our preliminary study showed that membrane protein Caveolin-1 (Cav1) silencing inhibited β-cell apoptosis and promote insulin secretion. The purpose of this study was to investigate the regulation of Cav1 on islet β-cell IAPP and its mechanism.
Materials and Methods: Firstly, IAPP secretion of each group of primary islets was detected by ELISA, then Western blot and real-time quantitative PCR (qPCR) were used to detect the expression levels of IAPP, PAM(Peptidyl-glycine alpha-amidating monooxygenase), PC1(Prohormone Convertase-1), BACE2(Beta-secretase 2), IDE(Insulin-Degrading Enzyme), TXNIP(Thioredoxin interacting protein), and finally, it confirmed that Cav1 interacted with the protein of TXNIP by immunofluorescence confocal and co-immunoprecipitation (Co-IP).
Results: The secretion of IAPP was decreased in primary pancreatic islets and Cav1 deficiency significantly down-regulated the expression of IAPP in NIT-1 cells, while over-expression of Cav1 in βTC-6 cells significantly up-regulated the expression of IAPP. This effect correlated with Cav1 silencing leading to down-regulation of PAM expression associated with IAPP synthesis and over-expression of Cav1 leading to up-regulation of PC1 associated with IAPP synthesis. On the other hand,Cav1 deficiency resulted in the up-regulation of the expression of BACE2 and IDE, the enzymes associated with IAPP decomposition. While over-expression of Cav1 leaded to down-regulation of BACE2 and IDE. Further studies indicated that Cav1 co-localized with TXNIP, and it interacted with and regulated the expression of TXNIP, which regulates IAPP gene transcription.
Conclusion: Cav-1 can regulate the synthesis and decomposition of IAPP in islet β cell by interacting with TXNIP. This study suggests that Cav-1 may protect diabetic islet beta cells by reducing islet amyloid deposition. |
| doi_str_mv | 10.2337/db20-2091-P |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_journals_2419451993</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2419451993</sourcerecordid><originalsourceid>FETCH-LOGICAL-c643-2ed12c3761c3965fa83a6529d92d16181648ce06dd66243a01b72a1c174a1d343</originalsourceid><addsrcrecordid>eNotkMFKAzEQhoMoWKsnXyDgUaKZZJs03spadaHigj14C2mSpVu2m7rZCn0aH8YXM3VlDv9hvvkHPoSugd4xzuW9WzFKGFVAyhM0AsUV4Ux-nKIRpcAISCXP0UWMG0qpSDNC64F-wPOq8raPOFQ4N18-NHVLAIcW92uP3w9tilhHbFqHH70N212IdV-nfTooYuN7_PNNct80uJiV5R9XpLpXb9emreP2Ep1Vpon-6j_HaPk0X-YvZPH2XOSzBbEi44R5B8xyKcByJSaVmXIjJkw5xRwImILIptZT4ZwQLOOGwkoyAxZkZsDxjI_RzVC768Ln3sdeb8K-a9NHzTJQ2QSU4om6HSjbhRg7X-ldV29Nd9BA9dGkPprURze65L_XMWNS</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2419451993</pqid></control><display><type>article</type><title>2091-P: Effects of Caveolin-1 on the Synthesis and Decomposition of Islet ß-Cell IAPP and Its Mechanism</title><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><creator>LIU, KUNYING ; ZENG, WEN ; LIN, SHUO ; LIN, CHUWEN ; XU, FEN ; CAI, NAN ; ZENG, LONGYI</creator><creatorcontrib>LIU, KUNYING ; ZENG, WEN ; LIN, SHUO ; LIN, CHUWEN ; XU, FEN ; CAI, NAN ; ZENG, LONGYI</creatorcontrib><description>Objective: Islet amyloid polypeptide(IAPP) is a major component of islet amyloid deposition in type 2 diabetic patients. Our preliminary study showed that membrane protein Caveolin-1 (Cav1) silencing inhibited β-cell apoptosis and promote insulin secretion. The purpose of this study was to investigate the regulation of Cav1 on islet β-cell IAPP and its mechanism.
Materials and Methods: Firstly, IAPP secretion of each group of primary islets was detected by ELISA, then Western blot and real-time quantitative PCR (qPCR) were used to detect the expression levels of IAPP, PAM(Peptidyl-glycine alpha-amidating monooxygenase), PC1(Prohormone Convertase-1), BACE2(Beta-secretase 2), IDE(Insulin-Degrading Enzyme), TXNIP(Thioredoxin interacting protein), and finally, it confirmed that Cav1 interacted with the protein of TXNIP by immunofluorescence confocal and co-immunoprecipitation (Co-IP).
Results: The secretion of IAPP was decreased in primary pancreatic islets and Cav1 deficiency significantly down-regulated the expression of IAPP in NIT-1 cells, while over-expression of Cav1 in βTC-6 cells significantly up-regulated the expression of IAPP. This effect correlated with Cav1 silencing leading to down-regulation of PAM expression associated with IAPP synthesis and over-expression of Cav1 leading to up-regulation of PC1 associated with IAPP synthesis. On the other hand,Cav1 deficiency resulted in the up-regulation of the expression of BACE2 and IDE, the enzymes associated with IAPP decomposition. While over-expression of Cav1 leaded to down-regulation of BACE2 and IDE. Further studies indicated that Cav1 co-localized with TXNIP, and it interacted with and regulated the expression of TXNIP, which regulates IAPP gene transcription.
Conclusion: Cav-1 can regulate the synthesis and decomposition of IAPP in islet β cell by interacting with TXNIP. This study suggests that Cav-1 may protect diabetic islet beta cells by reducing islet amyloid deposition.</description><identifier>ISSN: 0012-1797</identifier><identifier>EISSN: 1939-327X</identifier><identifier>DOI: 10.2337/db20-2091-P</identifier><language>eng</language><publisher>New York: American Diabetes Association</publisher><subject>Amylin ; Apoptosis ; Beta cells ; Caveolin ; Caveolin-1 ; Decomposition ; Diabetes ; Diabetes mellitus ; Enzyme-linked immunosorbent assay ; Glycine ; Immunofluorescence ; Immunoprecipitation ; Insulin ; Insulin secretion ; Insulysin ; Membrane proteins ; Overexpression ; Pancreas ; Peptidylglycine monooxygenase ; Proprotein convertases ; Proteins ; Secretase ; Thioredoxin ; Transcription ; β-Site APP-cleaving enzyme 2</subject><ispartof>Diabetes (New York, N.Y.), 2020-06, Vol.69 (Supplement_1)</ispartof><rights>Copyright American Diabetes Association Jun 1, 2020</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>LIU, KUNYING</creatorcontrib><creatorcontrib>ZENG, WEN</creatorcontrib><creatorcontrib>LIN, SHUO</creatorcontrib><creatorcontrib>LIN, CHUWEN</creatorcontrib><creatorcontrib>XU, FEN</creatorcontrib><creatorcontrib>CAI, NAN</creatorcontrib><creatorcontrib>ZENG, LONGYI</creatorcontrib><title>2091-P: Effects of Caveolin-1 on the Synthesis and Decomposition of Islet ß-Cell IAPP and Its Mechanism</title><title>Diabetes (New York, N.Y.)</title><description>Objective: Islet amyloid polypeptide(IAPP) is a major component of islet amyloid deposition in type 2 diabetic patients. Our preliminary study showed that membrane protein Caveolin-1 (Cav1) silencing inhibited β-cell apoptosis and promote insulin secretion. The purpose of this study was to investigate the regulation of Cav1 on islet β-cell IAPP and its mechanism.
Materials and Methods: Firstly, IAPP secretion of each group of primary islets was detected by ELISA, then Western blot and real-time quantitative PCR (qPCR) were used to detect the expression levels of IAPP, PAM(Peptidyl-glycine alpha-amidating monooxygenase), PC1(Prohormone Convertase-1), BACE2(Beta-secretase 2), IDE(Insulin-Degrading Enzyme), TXNIP(Thioredoxin interacting protein), and finally, it confirmed that Cav1 interacted with the protein of TXNIP by immunofluorescence confocal and co-immunoprecipitation (Co-IP).
Results: The secretion of IAPP was decreased in primary pancreatic islets and Cav1 deficiency significantly down-regulated the expression of IAPP in NIT-1 cells, while over-expression of Cav1 in βTC-6 cells significantly up-regulated the expression of IAPP. This effect correlated with Cav1 silencing leading to down-regulation of PAM expression associated with IAPP synthesis and over-expression of Cav1 leading to up-regulation of PC1 associated with IAPP synthesis. On the other hand,Cav1 deficiency resulted in the up-regulation of the expression of BACE2 and IDE, the enzymes associated with IAPP decomposition. While over-expression of Cav1 leaded to down-regulation of BACE2 and IDE. Further studies indicated that Cav1 co-localized with TXNIP, and it interacted with and regulated the expression of TXNIP, which regulates IAPP gene transcription.
Conclusion: Cav-1 can regulate the synthesis and decomposition of IAPP in islet β cell by interacting with TXNIP. This study suggests that Cav-1 may protect diabetic islet beta cells by reducing islet amyloid deposition.</description><subject>Amylin</subject><subject>Apoptosis</subject><subject>Beta cells</subject><subject>Caveolin</subject><subject>Caveolin-1</subject><subject>Decomposition</subject><subject>Diabetes</subject><subject>Diabetes mellitus</subject><subject>Enzyme-linked immunosorbent assay</subject><subject>Glycine</subject><subject>Immunofluorescence</subject><subject>Immunoprecipitation</subject><subject>Insulin</subject><subject>Insulin secretion</subject><subject>Insulysin</subject><subject>Membrane proteins</subject><subject>Overexpression</subject><subject>Pancreas</subject><subject>Peptidylglycine monooxygenase</subject><subject>Proprotein convertases</subject><subject>Proteins</subject><subject>Secretase</subject><subject>Thioredoxin</subject><subject>Transcription</subject><subject>β-Site APP-cleaving enzyme 2</subject><issn>0012-1797</issn><issn>1939-327X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNotkMFKAzEQhoMoWKsnXyDgUaKZZJs03spadaHigj14C2mSpVu2m7rZCn0aH8YXM3VlDv9hvvkHPoSugd4xzuW9WzFKGFVAyhM0AsUV4Ux-nKIRpcAISCXP0UWMG0qpSDNC64F-wPOq8raPOFQ4N18-NHVLAIcW92uP3w9tilhHbFqHH70N212IdV-nfTooYuN7_PNNct80uJiV5R9XpLpXb9emreP2Ep1Vpon-6j_HaPk0X-YvZPH2XOSzBbEi44R5B8xyKcByJSaVmXIjJkw5xRwImILIptZT4ZwQLOOGwkoyAxZkZsDxjI_RzVC768Ln3sdeb8K-a9NHzTJQ2QSU4om6HSjbhRg7X-ldV29Nd9BA9dGkPprURze65L_XMWNS</recordid><startdate>20200601</startdate><enddate>20200601</enddate><creator>LIU, KUNYING</creator><creator>ZENG, WEN</creator><creator>LIN, SHUO</creator><creator>LIN, CHUWEN</creator><creator>XU, FEN</creator><creator>CAI, NAN</creator><creator>ZENG, LONGYI</creator><general>American Diabetes Association</general><scope>AAYXX</scope><scope>CITATION</scope><scope>K9.</scope><scope>NAPCQ</scope></search><sort><creationdate>20200601</creationdate><title>2091-P: Effects of Caveolin-1 on the Synthesis and Decomposition of Islet ß-Cell IAPP and Its Mechanism</title><author>LIU, KUNYING ; ZENG, WEN ; LIN, SHUO ; LIN, CHUWEN ; XU, FEN ; CAI, NAN ; ZENG, LONGYI</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c643-2ed12c3761c3965fa83a6529d92d16181648ce06dd66243a01b72a1c174a1d343</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Amylin</topic><topic>Apoptosis</topic><topic>Beta cells</topic><topic>Caveolin</topic><topic>Caveolin-1</topic><topic>Decomposition</topic><topic>Diabetes</topic><topic>Diabetes mellitus</topic><topic>Enzyme-linked immunosorbent assay</topic><topic>Glycine</topic><topic>Immunofluorescence</topic><topic>Immunoprecipitation</topic><topic>Insulin</topic><topic>Insulin secretion</topic><topic>Insulysin</topic><topic>Membrane proteins</topic><topic>Overexpression</topic><topic>Pancreas</topic><topic>Peptidylglycine monooxygenase</topic><topic>Proprotein convertases</topic><topic>Proteins</topic><topic>Secretase</topic><topic>Thioredoxin</topic><topic>Transcription</topic><topic>β-Site APP-cleaving enzyme 2</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>LIU, KUNYING</creatorcontrib><creatorcontrib>ZENG, WEN</creatorcontrib><creatorcontrib>LIN, SHUO</creatorcontrib><creatorcontrib>LIN, CHUWEN</creatorcontrib><creatorcontrib>XU, FEN</creatorcontrib><creatorcontrib>CAI, NAN</creatorcontrib><creatorcontrib>ZENG, LONGYI</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Premium</collection><jtitle>Diabetes (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>LIU, KUNYING</au><au>ZENG, WEN</au><au>LIN, SHUO</au><au>LIN, CHUWEN</au><au>XU, FEN</au><au>CAI, NAN</au><au>ZENG, LONGYI</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>2091-P: Effects of Caveolin-1 on the Synthesis and Decomposition of Islet ß-Cell IAPP and Its Mechanism</atitle><jtitle>Diabetes (New York, N.Y.)</jtitle><date>2020-06-01</date><risdate>2020</risdate><volume>69</volume><issue>Supplement_1</issue><issn>0012-1797</issn><eissn>1939-327X</eissn><abstract>Objective: Islet amyloid polypeptide(IAPP) is a major component of islet amyloid deposition in type 2 diabetic patients. Our preliminary study showed that membrane protein Caveolin-1 (Cav1) silencing inhibited β-cell apoptosis and promote insulin secretion. The purpose of this study was to investigate the regulation of Cav1 on islet β-cell IAPP and its mechanism.
Materials and Methods: Firstly, IAPP secretion of each group of primary islets was detected by ELISA, then Western blot and real-time quantitative PCR (qPCR) were used to detect the expression levels of IAPP, PAM(Peptidyl-glycine alpha-amidating monooxygenase), PC1(Prohormone Convertase-1), BACE2(Beta-secretase 2), IDE(Insulin-Degrading Enzyme), TXNIP(Thioredoxin interacting protein), and finally, it confirmed that Cav1 interacted with the protein of TXNIP by immunofluorescence confocal and co-immunoprecipitation (Co-IP).
Results: The secretion of IAPP was decreased in primary pancreatic islets and Cav1 deficiency significantly down-regulated the expression of IAPP in NIT-1 cells, while over-expression of Cav1 in βTC-6 cells significantly up-regulated the expression of IAPP. This effect correlated with Cav1 silencing leading to down-regulation of PAM expression associated with IAPP synthesis and over-expression of Cav1 leading to up-regulation of PC1 associated with IAPP synthesis. On the other hand,Cav1 deficiency resulted in the up-regulation of the expression of BACE2 and IDE, the enzymes associated with IAPP decomposition. While over-expression of Cav1 leaded to down-regulation of BACE2 and IDE. Further studies indicated that Cav1 co-localized with TXNIP, and it interacted with and regulated the expression of TXNIP, which regulates IAPP gene transcription.
Conclusion: Cav-1 can regulate the synthesis and decomposition of IAPP in islet β cell by interacting with TXNIP. This study suggests that Cav-1 may protect diabetic islet beta cells by reducing islet amyloid deposition.</abstract><cop>New York</cop><pub>American Diabetes Association</pub><doi>10.2337/db20-2091-P</doi></addata></record> |
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| source | EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Amylin Apoptosis Beta cells Caveolin Caveolin-1 Decomposition Diabetes Diabetes mellitus Enzyme-linked immunosorbent assay Glycine Immunofluorescence Immunoprecipitation Insulin Insulin secretion Insulysin Membrane proteins Overexpression Pancreas Peptidylglycine monooxygenase Proprotein convertases Proteins Secretase Thioredoxin Transcription β-Site APP-cleaving enzyme 2 |
| title | 2091-P: Effects of Caveolin-1 on the Synthesis and Decomposition of Islet ß-Cell IAPP and Its Mechanism |
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