Dysfunction of the ER chaperone BiP accelerates the renal tubular injury
Tubular-interstitial injury plays a key role in the progression of chronic kidney disease. Although endoplasmic reticulum (ER) stress plays significant roles in the development of chronic diseases such as neurodegenerative disease, cardiomyopathy and diabetes mellitus, its pathophysiological role in...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 2008-02, Vol.366 (4), p.1048-1053 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1053 |
|---|---|
| container_issue | 4 |
| container_start_page | 1048 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 366 |
| creator | Kimura, Keita Jin, Hisayo Ogawa, Makoto Aoe, Tomohiko |
| description | Tubular-interstitial injury plays a key role in the progression of chronic kidney disease. Although endoplasmic reticulum (ER) stress plays significant roles in the development of chronic diseases such as neurodegenerative disease, cardiomyopathy and diabetes mellitus, its pathophysiological role in chronic renal tubular cell injury remains unknown. BiP is an essential chaperone molecule that helps with proper protein folding in the ER. Recently, we have produced a knock-in mouse that expresses a mutant-BiP in which the retrieval sequence to the ER is deleted in order to elucidate physiological processes that are sensitive to ER functions in adulthood. The heterozygous mutant-BiP mice showed significant tubular-interstitial lesions with aging. Furthermore, proteinuria induced by chronic protein overload accelerated the tubular-interstitial lesions in the mutant mice, accompanying caspase-12 activation and tubular cell apoptosis. These results suggest that the ER stress pathway is significantly involved in the pathophysiology of chronic renal tubular-interstitial injury in vivo. |
| doi_str_mv | 10.1016/j.bbrc.2007.12.098 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_70196024</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006291X07027052</els_id><sourcerecordid>70196024</sourcerecordid><originalsourceid>FETCH-LOGICAL-c420t-ff178d9b193e9616964fc89a147f62904e1db0b3a6b72939442c38ed6a6d48343</originalsourceid><addsrcrecordid>eNp9kE1Lw0AURQdRbK3-AReSlbvE9ybjJANutNYPKCii4G6YTF7olDSpM4nQf29qC-5cvc25l_sOY-cICQLKq2VSFN4mHCBLkCeg8gM2RlAQcwRxyMYAIGOu8HPETkJYAiAKqY7ZCHO8zhXyMXu634Sqb2zn2iZqq6hbUDR7i-zCrMm3DUV37jUy1lJN3nQUfgFPjamjri_62vjINcveb07ZUWXqQGf7O2EfD7P36VM8f3l8nt7OYys4dHFVYZaXqkCVkpIolRSVzZVBkVWSKxCEZQFFamSRcZUqIbhNcyqlkaXIU5FO2OWud-3br55Cp1cuDPNq01DbB50BKgl8C_IdaH0bgqdKr71bGb_RCHrrTy_11p_e-tPI9eBvCF3s2_tiReVfZC9sAG52AA0_fjvyOlhHjaXSebKdLlv3X_8PuzuAMg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>70196024</pqid></control><display><type>article</type><title>Dysfunction of the ER chaperone BiP accelerates the renal tubular injury</title><source>MEDLINE</source><source>Access via ScienceDirect (Elsevier)</source><creator>Kimura, Keita ; Jin, Hisayo ; Ogawa, Makoto ; Aoe, Tomohiko</creator><creatorcontrib>Kimura, Keita ; Jin, Hisayo ; Ogawa, Makoto ; Aoe, Tomohiko</creatorcontrib><description>Tubular-interstitial injury plays a key role in the progression of chronic kidney disease. Although endoplasmic reticulum (ER) stress plays significant roles in the development of chronic diseases such as neurodegenerative disease, cardiomyopathy and diabetes mellitus, its pathophysiological role in chronic renal tubular cell injury remains unknown. BiP is an essential chaperone molecule that helps with proper protein folding in the ER. Recently, we have produced a knock-in mouse that expresses a mutant-BiP in which the retrieval sequence to the ER is deleted in order to elucidate physiological processes that are sensitive to ER functions in adulthood. The heterozygous mutant-BiP mice showed significant tubular-interstitial lesions with aging. Furthermore, proteinuria induced by chronic protein overload accelerated the tubular-interstitial lesions in the mutant mice, accompanying caspase-12 activation and tubular cell apoptosis. These results suggest that the ER stress pathway is significantly involved in the pathophysiology of chronic renal tubular-interstitial injury in vivo.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2007.12.098</identifier><identifier>PMID: 18158912</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Aging ; Animals ; Animals, Newborn ; Apoptosis ; Caspase 12 - metabolism ; Caspase-12 ; Cattle ; Chaperone ; Endoplasmic Reticulum - pathology ; Endoplasmic reticulum stress ; Enzyme Activation ; Heat-Shock Proteins - metabolism ; Heterozygote ; Homozygote ; Kidney Diseases - enzymology ; Kidney Diseases - pathology ; Kidney Tubules - enzymology ; Kidney Tubules - pathology ; Mice ; Mice, Inbred C57BL ; Molecular Chaperones - metabolism ; Mutant Proteins - metabolism ; Mutation - genetics ; Protein overload nephropathy ; Proteinuria - pathology ; Serum Albumin, Bovine ; Tubular-interstitial injury</subject><ispartof>Biochemical and biophysical research communications, 2008-02, Vol.366 (4), p.1048-1053</ispartof><rights>2007 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c420t-ff178d9b193e9616964fc89a147f62904e1db0b3a6b72939442c38ed6a6d48343</citedby><cites>FETCH-LOGICAL-c420t-ff178d9b193e9616964fc89a147f62904e1db0b3a6b72939442c38ed6a6d48343</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2007.12.098$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18158912$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kimura, Keita</creatorcontrib><creatorcontrib>Jin, Hisayo</creatorcontrib><creatorcontrib>Ogawa, Makoto</creatorcontrib><creatorcontrib>Aoe, Tomohiko</creatorcontrib><title>Dysfunction of the ER chaperone BiP accelerates the renal tubular injury</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Tubular-interstitial injury plays a key role in the progression of chronic kidney disease. Although endoplasmic reticulum (ER) stress plays significant roles in the development of chronic diseases such as neurodegenerative disease, cardiomyopathy and diabetes mellitus, its pathophysiological role in chronic renal tubular cell injury remains unknown. BiP is an essential chaperone molecule that helps with proper protein folding in the ER. Recently, we have produced a knock-in mouse that expresses a mutant-BiP in which the retrieval sequence to the ER is deleted in order to elucidate physiological processes that are sensitive to ER functions in adulthood. The heterozygous mutant-BiP mice showed significant tubular-interstitial lesions with aging. Furthermore, proteinuria induced by chronic protein overload accelerated the tubular-interstitial lesions in the mutant mice, accompanying caspase-12 activation and tubular cell apoptosis. These results suggest that the ER stress pathway is significantly involved in the pathophysiology of chronic renal tubular-interstitial injury in vivo.</description><subject>Aging</subject><subject>Animals</subject><subject>Animals, Newborn</subject><subject>Apoptosis</subject><subject>Caspase 12 - metabolism</subject><subject>Caspase-12</subject><subject>Cattle</subject><subject>Chaperone</subject><subject>Endoplasmic Reticulum - pathology</subject><subject>Endoplasmic reticulum stress</subject><subject>Enzyme Activation</subject><subject>Heat-Shock Proteins - metabolism</subject><subject>Heterozygote</subject><subject>Homozygote</subject><subject>Kidney Diseases - enzymology</subject><subject>Kidney Diseases - pathology</subject><subject>Kidney Tubules - enzymology</subject><subject>Kidney Tubules - pathology</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Molecular Chaperones - metabolism</subject><subject>Mutant Proteins - metabolism</subject><subject>Mutation - genetics</subject><subject>Protein overload nephropathy</subject><subject>Proteinuria - pathology</subject><subject>Serum Albumin, Bovine</subject><subject>Tubular-interstitial injury</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1Lw0AURQdRbK3-AReSlbvE9ybjJANutNYPKCii4G6YTF7olDSpM4nQf29qC-5cvc25l_sOY-cICQLKq2VSFN4mHCBLkCeg8gM2RlAQcwRxyMYAIGOu8HPETkJYAiAKqY7ZCHO8zhXyMXu634Sqb2zn2iZqq6hbUDR7i-zCrMm3DUV37jUy1lJN3nQUfgFPjamjri_62vjINcveb07ZUWXqQGf7O2EfD7P36VM8f3l8nt7OYys4dHFVYZaXqkCVkpIolRSVzZVBkVWSKxCEZQFFamSRcZUqIbhNcyqlkaXIU5FO2OWud-3br55Cp1cuDPNq01DbB50BKgl8C_IdaH0bgqdKr71bGb_RCHrrTy_11p_e-tPI9eBvCF3s2_tiReVfZC9sAG52AA0_fjvyOlhHjaXSebKdLlv3X_8PuzuAMg</recordid><startdate>20080222</startdate><enddate>20080222</enddate><creator>Kimura, Keita</creator><creator>Jin, Hisayo</creator><creator>Ogawa, Makoto</creator><creator>Aoe, Tomohiko</creator><general>Elsevier Inc</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>7X8</scope></search><sort><creationdate>20080222</creationdate><title>Dysfunction of the ER chaperone BiP accelerates the renal tubular injury</title><author>Kimura, Keita ; Jin, Hisayo ; Ogawa, Makoto ; Aoe, Tomohiko</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c420t-ff178d9b193e9616964fc89a147f62904e1db0b3a6b72939442c38ed6a6d48343</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Aging</topic><topic>Animals</topic><topic>Animals, Newborn</topic><topic>Apoptosis</topic><topic>Caspase 12 - metabolism</topic><topic>Caspase-12</topic><topic>Cattle</topic><topic>Chaperone</topic><topic>Endoplasmic Reticulum - pathology</topic><topic>Endoplasmic reticulum stress</topic><topic>Enzyme Activation</topic><topic>Heat-Shock Proteins - metabolism</topic><topic>Heterozygote</topic><topic>Homozygote</topic><topic>Kidney Diseases - enzymology</topic><topic>Kidney Diseases - pathology</topic><topic>Kidney Tubules - enzymology</topic><topic>Kidney Tubules - pathology</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Molecular Chaperones - metabolism</topic><topic>Mutant Proteins - metabolism</topic><topic>Mutation - genetics</topic><topic>Protein overload nephropathy</topic><topic>Proteinuria - pathology</topic><topic>Serum Albumin, Bovine</topic><topic>Tubular-interstitial injury</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kimura, Keita</creatorcontrib><creatorcontrib>Jin, Hisayo</creatorcontrib><creatorcontrib>Ogawa, Makoto</creatorcontrib><creatorcontrib>Aoe, Tomohiko</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kimura, Keita</au><au>Jin, Hisayo</au><au>Ogawa, Makoto</au><au>Aoe, Tomohiko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dysfunction of the ER chaperone BiP accelerates the renal tubular injury</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2008-02-22</date><risdate>2008</risdate><volume>366</volume><issue>4</issue><spage>1048</spage><epage>1053</epage><pages>1048-1053</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Tubular-interstitial injury plays a key role in the progression of chronic kidney disease. Although endoplasmic reticulum (ER) stress plays significant roles in the development of chronic diseases such as neurodegenerative disease, cardiomyopathy and diabetes mellitus, its pathophysiological role in chronic renal tubular cell injury remains unknown. BiP is an essential chaperone molecule that helps with proper protein folding in the ER. Recently, we have produced a knock-in mouse that expresses a mutant-BiP in which the retrieval sequence to the ER is deleted in order to elucidate physiological processes that are sensitive to ER functions in adulthood. The heterozygous mutant-BiP mice showed significant tubular-interstitial lesions with aging. Furthermore, proteinuria induced by chronic protein overload accelerated the tubular-interstitial lesions in the mutant mice, accompanying caspase-12 activation and tubular cell apoptosis. These results suggest that the ER stress pathway is significantly involved in the pathophysiology of chronic renal tubular-interstitial injury in vivo.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>18158912</pmid><doi>10.1016/j.bbrc.2007.12.098</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 2008-02, Vol.366 (4), p.1048-1053 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_70196024 |
| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Aging Animals Animals, Newborn Apoptosis Caspase 12 - metabolism Caspase-12 Cattle Chaperone Endoplasmic Reticulum - pathology Endoplasmic reticulum stress Enzyme Activation Heat-Shock Proteins - metabolism Heterozygote Homozygote Kidney Diseases - enzymology Kidney Diseases - pathology Kidney Tubules - enzymology Kidney Tubules - pathology Mice Mice, Inbred C57BL Molecular Chaperones - metabolism Mutant Proteins - metabolism Mutation - genetics Protein overload nephropathy Proteinuria - pathology Serum Albumin, Bovine Tubular-interstitial injury |
| title | Dysfunction of the ER chaperone BiP accelerates the renal tubular injury |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-23T10%3A51%3A04IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Dysfunction%20of%20the%20ER%20chaperone%20BiP%20accelerates%20the%20renal%20tubular%20injury&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Kimura,%20Keita&rft.date=2008-02-22&rft.volume=366&rft.issue=4&rft.spage=1048&rft.epage=1053&rft.pages=1048-1053&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1016/j.bbrc.2007.12.098&rft_dat=%3Cproquest_cross%3E70196024%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=70196024&rft_id=info:pmid/18158912&rft_els_id=S0006291X07027052&rfr_iscdi=true |