Downregulation of the Ubiquitin-Proteasome System in Normal Colonic Macrophages and Reinduction in Inflammatory Bowel Disease
Background: In normal mucosa, intestinal lamina propria macrophages (IMACs) maintain tolerance against food antigens and the commensal bacterial flora. Several mechanisms have been identified that mediate tolerance. The ubiquitin-proteasome system (UPS) is a large multiprotein complex that degrades...
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| Veröffentlicht in: | Digestion 2012-01, Vol.86 (1), p.34-47 |
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| creator | Hetzenecker, A.M. Seidl, M.C. Kosovac, K. Herfarth, H. Kellermeier, S. Obermeier, F. Falk, W. Schoelmerich, J. Hausmann, M. Rogler, G. |
| description | Background: In normal mucosa, intestinal lamina propria macrophages (IMACs) maintain tolerance against food antigens and the commensal bacterial flora. Several mechanisms have been identified that mediate tolerance. The ubiquitin-proteasome system (UPS) is a large multiprotein complex that degrades cellular proteins. As the UPS may modulate immune functions of IMACs, we performed a detailed investigation of UPS expression and function under normal conditions and in cells derived from patients suffering from inflammatory bowel disease (IBD). Methods: IMACs were isolated from intestinal mucosa. mRNA expression of macrophages differentiated in vitro (i.v. MACs) and IMACs was compared by Affymetrix® oligonucleotide arrays. Quantitative Taqman-PCR was performed on five exemplary proteasomal and five ubiquitinylation genes each. Proteins were analyzed by immunohistochemistry and Western blotting. Proteasome function was assessed by a fluorimetric test. Results: Affymetrix analysis showed downregulation of mRNA expression of almost all represented proteasomal and of 22 ubiquitination-associated genes in IMACs as compared to i.v. MACs and monocytes. By quantitative PCR, up to tenfold higher mRNA expression of 10 exemplary genes of the UPS (UBE2A, UBE2D2, UBE2L6, USP14, UBB and ATPase2, β2, β5, β2i/MECL-1, β5i/LMP7) was demonstrated in i.v. MACs as compared to IMACs. Immunohistochemistry and Western blots confirmed these findings in intestinal mucosa of controls and patients suffering from diverticulitis. In contrast, a significant increase in protein amounts was found in mucosa of patients with IBD. Conclusion: Reduced expression of subunits of the UPS in IMACs of normal mucosa supports the concept of the presence of a nonreactive, anergic macrophage phenotype in the gut under normal conditions. Reinduction in IMACs of IBD mucosa reflects activated IMACs which can present antigenic peptides and thus support inflammation. |
| doi_str_mv | 10.1159/000336353 |
| format | Article |
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Several mechanisms have been identified that mediate tolerance. The ubiquitin-proteasome system (UPS) is a large multiprotein complex that degrades cellular proteins. As the UPS may modulate immune functions of IMACs, we performed a detailed investigation of UPS expression and function under normal conditions and in cells derived from patients suffering from inflammatory bowel disease (IBD). Methods: IMACs were isolated from intestinal mucosa. mRNA expression of macrophages differentiated in vitro (i.v. MACs) and IMACs was compared by Affymetrix® oligonucleotide arrays. Quantitative Taqman-PCR was performed on five exemplary proteasomal and five ubiquitinylation genes each. Proteins were analyzed by immunohistochemistry and Western blotting. Proteasome function was assessed by a fluorimetric test. Results: Affymetrix analysis showed downregulation of mRNA expression of almost all represented proteasomal and of 22 ubiquitination-associated genes in IMACs as compared to i.v. MACs and monocytes. By quantitative PCR, up to tenfold higher mRNA expression of 10 exemplary genes of the UPS (UBE2A, UBE2D2, UBE2L6, USP14, UBB and ATPase2, β2, β5, β2i/MECL-1, β5i/LMP7) was demonstrated in i.v. MACs as compared to IMACs. Immunohistochemistry and Western blots confirmed these findings in intestinal mucosa of controls and patients suffering from diverticulitis. In contrast, a significant increase in protein amounts was found in mucosa of patients with IBD. Conclusion: Reduced expression of subunits of the UPS in IMACs of normal mucosa supports the concept of the presence of a nonreactive, anergic macrophage phenotype in the gut under normal conditions. Reinduction in IMACs of IBD mucosa reflects activated IMACs which can present antigenic peptides and thus support inflammation.</description><identifier>ISSN: 0012-2823</identifier><identifier>EISSN: 1421-9867</identifier><identifier>DOI: 10.1159/000336353</identifier><identifier>PMID: 22710419</identifier><identifier>CODEN: DIGEBW</identifier><language>eng</language><publisher>Basel, Switzerland: S. Karger AG</publisher><subject>Adenosine Triphosphatases - genetics ; Cell Differentiation ; Cells, Cultured ; Colitis, Ulcerative - enzymology ; Colitis, Ulcerative - genetics ; Colon - enzymology ; Crohn Disease - enzymology ; Crohn Disease - genetics ; Diverticulitis - enzymology ; Diverticulitis - genetics ; Down-Regulation ; Humans ; Inflammatory bowel disease ; Intestinal Mucosa - enzymology ; Macrophages - enzymology ; Microarray Analysis ; Mitochondrial Proton-Translocating ATPases - genetics ; Mitochondrial Proton-Translocating ATPases - metabolism ; Original Paper ; Proteasome Endopeptidase Complex - genetics ; Proteasome Endopeptidase Complex - metabolism ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; Sarcoplasmic Reticulum Calcium-Transporting ATPases - genetics ; Sarcoplasmic Reticulum Calcium-Transporting ATPases - metabolism ; Ubiquitin - genetics ; Ubiquitin - metabolism ; Ubiquitin Thiolesterase - genetics ; Ubiquitin Thiolesterase - metabolism ; Ubiquitin-Conjugating Enzymes - genetics ; Ubiquitin-Conjugating Enzymes - metabolism ; Ubiquitin-Protein Ligase Complexes - blood ; Ubiquitin-Protein Ligase Complexes - genetics ; Ubiquitin-Protein Ligase Complexes - metabolism</subject><ispartof>Digestion, 2012-01, Vol.86 (1), p.34-47</ispartof><rights>2012 S. Karger AG, Basel</rights><rights>Copyright © 2012 S. Karger AG, Basel.</rights><rights>Copyright (c) 2012 S. Karger AG, Basel</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c435t-77ade1ddce93598db1d1eca74c189dc67b37e5de8ac1f40c33b8973f292d10b53</citedby><cites>FETCH-LOGICAL-c435t-77ade1ddce93598db1d1eca74c189dc67b37e5de8ac1f40c33b8973f292d10b53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2429,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22710419$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hetzenecker, A.M.</creatorcontrib><creatorcontrib>Seidl, M.C.</creatorcontrib><creatorcontrib>Kosovac, K.</creatorcontrib><creatorcontrib>Herfarth, H.</creatorcontrib><creatorcontrib>Kellermeier, S.</creatorcontrib><creatorcontrib>Obermeier, F.</creatorcontrib><creatorcontrib>Falk, W.</creatorcontrib><creatorcontrib>Schoelmerich, J.</creatorcontrib><creatorcontrib>Hausmann, M.</creatorcontrib><creatorcontrib>Rogler, G.</creatorcontrib><title>Downregulation of the Ubiquitin-Proteasome System in Normal Colonic Macrophages and Reinduction in Inflammatory Bowel Disease</title><title>Digestion</title><addtitle>Digestion</addtitle><description>Background: In normal mucosa, intestinal lamina propria macrophages (IMACs) maintain tolerance against food antigens and the commensal bacterial flora. Several mechanisms have been identified that mediate tolerance. The ubiquitin-proteasome system (UPS) is a large multiprotein complex that degrades cellular proteins. As the UPS may modulate immune functions of IMACs, we performed a detailed investigation of UPS expression and function under normal conditions and in cells derived from patients suffering from inflammatory bowel disease (IBD). Methods: IMACs were isolated from intestinal mucosa. mRNA expression of macrophages differentiated in vitro (i.v. MACs) and IMACs was compared by Affymetrix® oligonucleotide arrays. Quantitative Taqman-PCR was performed on five exemplary proteasomal and five ubiquitinylation genes each. Proteins were analyzed by immunohistochemistry and Western blotting. Proteasome function was assessed by a fluorimetric test. Results: Affymetrix analysis showed downregulation of mRNA expression of almost all represented proteasomal and of 22 ubiquitination-associated genes in IMACs as compared to i.v. MACs and monocytes. By quantitative PCR, up to tenfold higher mRNA expression of 10 exemplary genes of the UPS (UBE2A, UBE2D2, UBE2L6, USP14, UBB and ATPase2, β2, β5, β2i/MECL-1, β5i/LMP7) was demonstrated in i.v. MACs as compared to IMACs. Immunohistochemistry and Western blots confirmed these findings in intestinal mucosa of controls and patients suffering from diverticulitis. In contrast, a significant increase in protein amounts was found in mucosa of patients with IBD. Conclusion: Reduced expression of subunits of the UPS in IMACs of normal mucosa supports the concept of the presence of a nonreactive, anergic macrophage phenotype in the gut under normal conditions. Reinduction in IMACs of IBD mucosa reflects activated IMACs which can present antigenic peptides and thus support inflammation.</description><subject>Adenosine Triphosphatases - genetics</subject><subject>Cell Differentiation</subject><subject>Cells, Cultured</subject><subject>Colitis, Ulcerative - enzymology</subject><subject>Colitis, Ulcerative - genetics</subject><subject>Colon - enzymology</subject><subject>Crohn Disease - enzymology</subject><subject>Crohn Disease - genetics</subject><subject>Diverticulitis - enzymology</subject><subject>Diverticulitis - genetics</subject><subject>Down-Regulation</subject><subject>Humans</subject><subject>Inflammatory bowel disease</subject><subject>Intestinal Mucosa - enzymology</subject><subject>Macrophages - enzymology</subject><subject>Microarray Analysis</subject><subject>Mitochondrial Proton-Translocating ATPases - genetics</subject><subject>Mitochondrial Proton-Translocating ATPases - metabolism</subject><subject>Original Paper</subject><subject>Proteasome Endopeptidase Complex - genetics</subject><subject>Proteasome Endopeptidase Complex - metabolism</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>Sarcoplasmic Reticulum Calcium-Transporting ATPases - genetics</subject><subject>Sarcoplasmic Reticulum Calcium-Transporting ATPases - metabolism</subject><subject>Ubiquitin - genetics</subject><subject>Ubiquitin - metabolism</subject><subject>Ubiquitin Thiolesterase - genetics</subject><subject>Ubiquitin Thiolesterase - metabolism</subject><subject>Ubiquitin-Conjugating Enzymes - genetics</subject><subject>Ubiquitin-Conjugating Enzymes - metabolism</subject><subject>Ubiquitin-Protein Ligase Complexes - blood</subject><subject>Ubiquitin-Protein Ligase Complexes - genetics</subject><subject>Ubiquitin-Protein Ligase Complexes - metabolism</subject><issn>0012-2823</issn><issn>1421-9867</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><recordid>eNpd0Utv3CAUBWAUtUqmaRfZVxVSNunCLReMbZbtpI9I6UNtsrYwXE9IbZiArWgW_e8lncksskJIH0eXewg5AfYOQKr3jDEhKiHFAVlAyaFQTVU_IwvGgBe84eKIvEjp9uGqSnFIjjivgZWgFuTvebj3EVfzoCcXPA09nW6QXnfubnaT88XPGCbUKYxIf2_ShCN1nn4PcdQDXYYheGfoN21iWN_oFSaqvaW_0Hk7m_-BWV_4ftDjqKcQN_RjuMeBnruUQ_Eled7rIeGr3XlMrj9_ulp-LS5_fLlYfrgsTCnkVNS1tgjWGlRCqsZ2YAGNrksDjbKmqjtRo7TYaAN9yYwQXaNq0XPFLbBOimNyts1dx3A3Y5ra0SWDw6A9hjm1kPcnRSkbyPT0Cb0Nc_R5uqyU5FUFnGf1dqvyx1OK2Lfr6EYdNxm1D520-06yfbNLnLsR7V4-lpDB6y34o-MK4x7s3v8D5j2Qxg</recordid><startdate>20120101</startdate><enddate>20120101</enddate><creator>Hetzenecker, A.M.</creator><creator>Seidl, M.C.</creator><creator>Kosovac, K.</creator><creator>Herfarth, H.</creator><creator>Kellermeier, S.</creator><creator>Obermeier, F.</creator><creator>Falk, W.</creator><creator>Schoelmerich, J.</creator><creator>Hausmann, M.</creator><creator>Rogler, G.</creator><general>S. 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genetics</topic><topic>Cell Differentiation</topic><topic>Cells, Cultured</topic><topic>Colitis, Ulcerative - enzymology</topic><topic>Colitis, Ulcerative - genetics</topic><topic>Colon - enzymology</topic><topic>Crohn Disease - enzymology</topic><topic>Crohn Disease - genetics</topic><topic>Diverticulitis - enzymology</topic><topic>Diverticulitis - genetics</topic><topic>Down-Regulation</topic><topic>Humans</topic><topic>Inflammatory bowel disease</topic><topic>Intestinal Mucosa - enzymology</topic><topic>Macrophages - enzymology</topic><topic>Microarray Analysis</topic><topic>Mitochondrial Proton-Translocating ATPases - genetics</topic><topic>Mitochondrial Proton-Translocating ATPases - metabolism</topic><topic>Original Paper</topic><topic>Proteasome Endopeptidase Complex - genetics</topic><topic>Proteasome Endopeptidase Complex - metabolism</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Messenger - metabolism</topic><topic>Sarcoplasmic Reticulum Calcium-Transporting ATPases - genetics</topic><topic>Sarcoplasmic Reticulum Calcium-Transporting ATPases - metabolism</topic><topic>Ubiquitin - genetics</topic><topic>Ubiquitin - metabolism</topic><topic>Ubiquitin Thiolesterase - genetics</topic><topic>Ubiquitin Thiolesterase - metabolism</topic><topic>Ubiquitin-Conjugating Enzymes - genetics</topic><topic>Ubiquitin-Conjugating Enzymes - metabolism</topic><topic>Ubiquitin-Protein Ligase Complexes - blood</topic><topic>Ubiquitin-Protein Ligase Complexes - genetics</topic><topic>Ubiquitin-Protein Ligase Complexes - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hetzenecker, A.M.</creatorcontrib><creatorcontrib>Seidl, M.C.</creatorcontrib><creatorcontrib>Kosovac, K.</creatorcontrib><creatorcontrib>Herfarth, H.</creatorcontrib><creatorcontrib>Kellermeier, S.</creatorcontrib><creatorcontrib>Obermeier, F.</creatorcontrib><creatorcontrib>Falk, W.</creatorcontrib><creatorcontrib>Schoelmerich, J.</creatorcontrib><creatorcontrib>Hausmann, M.</creatorcontrib><creatorcontrib>Rogler, G.</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>Calcium & Calcified Tissue 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>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>ProQuest One Community College</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</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>SIRS Editorial</collection><collection>MEDLINE - Academic</collection><jtitle>Digestion</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hetzenecker, A.M.</au><au>Seidl, M.C.</au><au>Kosovac, K.</au><au>Herfarth, H.</au><au>Kellermeier, S.</au><au>Obermeier, F.</au><au>Falk, W.</au><au>Schoelmerich, J.</au><au>Hausmann, M.</au><au>Rogler, G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Downregulation of the Ubiquitin-Proteasome System in Normal Colonic Macrophages and Reinduction in Inflammatory Bowel Disease</atitle><jtitle>Digestion</jtitle><addtitle>Digestion</addtitle><date>2012-01-01</date><risdate>2012</risdate><volume>86</volume><issue>1</issue><spage>34</spage><epage>47</epage><pages>34-47</pages><issn>0012-2823</issn><eissn>1421-9867</eissn><coden>DIGEBW</coden><abstract>Background: In normal mucosa, intestinal lamina propria macrophages (IMACs) maintain tolerance against food antigens and the commensal bacterial flora. Several mechanisms have been identified that mediate tolerance. The ubiquitin-proteasome system (UPS) is a large multiprotein complex that degrades cellular proteins. As the UPS may modulate immune functions of IMACs, we performed a detailed investigation of UPS expression and function under normal conditions and in cells derived from patients suffering from inflammatory bowel disease (IBD). Methods: IMACs were isolated from intestinal mucosa. mRNA expression of macrophages differentiated in vitro (i.v. MACs) and IMACs was compared by Affymetrix® oligonucleotide arrays. Quantitative Taqman-PCR was performed on five exemplary proteasomal and five ubiquitinylation genes each. Proteins were analyzed by immunohistochemistry and Western blotting. Proteasome function was assessed by a fluorimetric test. Results: Affymetrix analysis showed downregulation of mRNA expression of almost all represented proteasomal and of 22 ubiquitination-associated genes in IMACs as compared to i.v. MACs and monocytes. By quantitative PCR, up to tenfold higher mRNA expression of 10 exemplary genes of the UPS (UBE2A, UBE2D2, UBE2L6, USP14, UBB and ATPase2, β2, β5, β2i/MECL-1, β5i/LMP7) was demonstrated in i.v. MACs as compared to IMACs. Immunohistochemistry and Western blots confirmed these findings in intestinal mucosa of controls and patients suffering from diverticulitis. In contrast, a significant increase in protein amounts was found in mucosa of patients with IBD. Conclusion: Reduced expression of subunits of the UPS in IMACs of normal mucosa supports the concept of the presence of a nonreactive, anergic macrophage phenotype in the gut under normal conditions. Reinduction in IMACs of IBD mucosa reflects activated IMACs which can present antigenic peptides and thus support inflammation.</abstract><cop>Basel, Switzerland</cop><pub>S. Karger AG</pub><pmid>22710419</pmid><doi>10.1159/000336353</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adenosine Triphosphatases - genetics Cell Differentiation Cells, Cultured Colitis, Ulcerative - enzymology Colitis, Ulcerative - genetics Colon - enzymology Crohn Disease - enzymology Crohn Disease - genetics Diverticulitis - enzymology Diverticulitis - genetics Down-Regulation Humans Inflammatory bowel disease Intestinal Mucosa - enzymology Macrophages - enzymology Microarray Analysis Mitochondrial Proton-Translocating ATPases - genetics Mitochondrial Proton-Translocating ATPases - metabolism Original Paper Proteasome Endopeptidase Complex - genetics Proteasome Endopeptidase Complex - metabolism RNA, Messenger - genetics RNA, Messenger - metabolism Sarcoplasmic Reticulum Calcium-Transporting ATPases - genetics Sarcoplasmic Reticulum Calcium-Transporting ATPases - metabolism Ubiquitin - genetics Ubiquitin - metabolism Ubiquitin Thiolesterase - genetics Ubiquitin Thiolesterase - metabolism Ubiquitin-Conjugating Enzymes - genetics Ubiquitin-Conjugating Enzymes - metabolism Ubiquitin-Protein Ligase Complexes - blood Ubiquitin-Protein Ligase Complexes - genetics Ubiquitin-Protein Ligase Complexes - metabolism |
| title | Downregulation of the Ubiquitin-Proteasome System in Normal Colonic Macrophages and Reinduction in Inflammatory Bowel Disease |
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