Elastin metabolism during recovery from impaired crosslink formation
Accelerated proteolysis of tropoelastin and elastin occurs in the arteries of chicks rendered nutritionally copper-deficient. The process results in part from decreased elastin crosslinking. Repletion of copper-deficient chicks with copper causes a deposition of elastin that is proteinase resistant....
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Veröffentlicht in: | Archives of biochemistry and biophysics 1990-05, Vol.278 (2), p.326-332 |
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creator | Tinker, Donald Romero-Chapman, Nadia Reiser, Karen Hyde, Dallas Rucker, Robert |
description | Accelerated proteolysis of tropoelastin and elastin occurs in the arteries of chicks rendered nutritionally copper-deficient. The process results in part from decreased elastin crosslinking. Repletion of copper-deficient chicks with copper causes a deposition of elastin that is proteinase resistant. Resistance to proteolysis is conferred within 48 h of dietary copper repletion. Deposition of aorta elastin to near normal values occurs after 3–4 days in copper-repleted chicks. Moreover, elastolysis was enhanced when the content of dehydrolysinonorleucine in elastin was abnormally low. The chemical modification of lysyl residue in elastin by citroconylation, however, did not influence the rate of elastolysis. We have shown previously that tropoelastin messenger RNA activity and synthesis are not influenced by dietary copper deprivation (1986,
Biochem. J.
236, 17–23). Rather, as demonstrated herein, the decrease in elastin content in arteries of copper-deficient birds appears to be more the result of enhanced degradation. Restoration of normal crosslinking restores deposition and imparts resistance to elastolysis. Moreover, serum appears to be a good source of elastolytic proteinases when the elastin substrate is partially or abnormally crosslinked. |
doi_str_mv | 10.1016/0003-9861(90)90267-3 |
format | Article |
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Biochem. J.
236, 17–23). Rather, as demonstrated herein, the decrease in elastin content in arteries of copper-deficient birds appears to be more the result of enhanced degradation. Restoration of normal crosslinking restores deposition and imparts resistance to elastolysis. Moreover, serum appears to be a good source of elastolytic proteinases when the elastin substrate is partially or abnormally crosslinked.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(90)90267-3</identifier><identifier>PMID: 2327789</identifier><identifier>CODEN: ABBIA4</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Amino Acids - analysis ; Analytical, structural and metabolic biochemistry ; Animals ; Aorta, Thoracic - metabolism ; Biological and medical sciences ; Chickens ; Copper - metabolism ; Cross-Linking Reagents ; elastin ; Elastin - metabolism ; Fundamental and applied biological sciences. Psychology ; Glycoproteins ; Hydrolysis ; Organ Culture Techniques ; Proteins ; Solubility ; Valine - metabolism</subject><ispartof>Archives of biochemistry and biophysics, 1990-05, Vol.278 (2), p.326-332</ispartof><rights>1990</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c399t-6fe4adfbbc4298ce484c0f4fde95d3f7b0fa6768d3a49e79aa0ab15abfe4193b3</citedby><cites>FETCH-LOGICAL-c399t-6fe4adfbbc4298ce484c0f4fde95d3f7b0fa6768d3a49e79aa0ab15abfe4193b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0003-9861(90)90267-3$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3549,27923,27924,45994</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19536849$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2327789$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tinker, Donald</creatorcontrib><creatorcontrib>Romero-Chapman, Nadia</creatorcontrib><creatorcontrib>Reiser, Karen</creatorcontrib><creatorcontrib>Hyde, Dallas</creatorcontrib><creatorcontrib>Rucker, Robert</creatorcontrib><title>Elastin metabolism during recovery from impaired crosslink formation</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Accelerated proteolysis of tropoelastin and elastin occurs in the arteries of chicks rendered nutritionally copper-deficient. The process results in part from decreased elastin crosslinking. Repletion of copper-deficient chicks with copper causes a deposition of elastin that is proteinase resistant. Resistance to proteolysis is conferred within 48 h of dietary copper repletion. Deposition of aorta elastin to near normal values occurs after 3–4 days in copper-repleted chicks. Moreover, elastolysis was enhanced when the content of dehydrolysinonorleucine in elastin was abnormally low. The chemical modification of lysyl residue in elastin by citroconylation, however, did not influence the rate of elastolysis. We have shown previously that tropoelastin messenger RNA activity and synthesis are not influenced by dietary copper deprivation (1986,
Biochem. J.
236, 17–23). Rather, as demonstrated herein, the decrease in elastin content in arteries of copper-deficient birds appears to be more the result of enhanced degradation. Restoration of normal crosslinking restores deposition and imparts resistance to elastolysis. Moreover, serum appears to be a good source of elastolytic proteinases when the elastin substrate is partially or abnormally crosslinked.</description><subject>Amino Acids - analysis</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Aorta, Thoracic - metabolism</subject><subject>Biological and medical sciences</subject><subject>Chickens</subject><subject>Copper - metabolism</subject><subject>Cross-Linking Reagents</subject><subject>elastin</subject><subject>Elastin - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins</subject><subject>Hydrolysis</subject><subject>Organ Culture Techniques</subject><subject>Proteins</subject><subject>Solubility</subject><subject>Valine - metabolism</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1L7TAQhoMoeq76DxS6Ua6LatKkSbMRxI-rILjRdZgmE4m2zTHpEfz39ngOuvOuZjHP-zLzEHLA6CmjTJ5RSnmpG8n-anqiaSVVyTfIjFEtS8obsUlm38gO-ZPzC6WMCVltk-2KV0o1ekaurjvIYxiKHkdoYxdyX7hFCsNzkdDGd0wfhU-xL0I_h5DQFTbFnLswvBY-ph7GEIc9suWhy7i_nrvk6eb68fK2vH_4d3d5cV9arvVYSo8CnG9bKyrdWBSNsNQL71DXjnvVUg9SycZxEBqVBqDQshraKcc0b_kuOV71zlN8W2AeTR-yxa6DAeMiG6UVrxnX_wVZXTeyVmICxQr8-iqhN_MUekgfhlGztGyWCs1SodHUfFk2fIodrvsXbY_uO7TWOu2P1nvIFjqfYLAh_3TrmstGLLnzFYeTtfeAyWQbcLDoJtV2NC6G3w_5BCxQmjw</recordid><startdate>19900501</startdate><enddate>19900501</enddate><creator>Tinker, Donald</creator><creator>Romero-Chapman, Nadia</creator><creator>Reiser, Karen</creator><creator>Hyde, Dallas</creator><creator>Rucker, Robert</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19900501</creationdate><title>Elastin metabolism during recovery from impaired crosslink formation</title><author>Tinker, Donald ; Romero-Chapman, Nadia ; Reiser, Karen ; Hyde, Dallas ; Rucker, Robert</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c399t-6fe4adfbbc4298ce484c0f4fde95d3f7b0fa6768d3a49e79aa0ab15abfe4193b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Amino Acids - analysis</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Aorta, Thoracic - metabolism</topic><topic>Biological and medical sciences</topic><topic>Chickens</topic><topic>Copper - metabolism</topic><topic>Cross-Linking Reagents</topic><topic>elastin</topic><topic>Elastin - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins</topic><topic>Hydrolysis</topic><topic>Organ Culture Techniques</topic><topic>Proteins</topic><topic>Solubility</topic><topic>Valine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tinker, Donald</creatorcontrib><creatorcontrib>Romero-Chapman, Nadia</creatorcontrib><creatorcontrib>Reiser, Karen</creatorcontrib><creatorcontrib>Hyde, Dallas</creatorcontrib><creatorcontrib>Rucker, Robert</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tinker, Donald</au><au>Romero-Chapman, Nadia</au><au>Reiser, Karen</au><au>Hyde, Dallas</au><au>Rucker, Robert</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Elastin metabolism during recovery from impaired crosslink formation</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1990-05-01</date><risdate>1990</risdate><volume>278</volume><issue>2</issue><spage>326</spage><epage>332</epage><pages>326-332</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><coden>ABBIA4</coden><abstract>Accelerated proteolysis of tropoelastin and elastin occurs in the arteries of chicks rendered nutritionally copper-deficient. The process results in part from decreased elastin crosslinking. Repletion of copper-deficient chicks with copper causes a deposition of elastin that is proteinase resistant. Resistance to proteolysis is conferred within 48 h of dietary copper repletion. Deposition of aorta elastin to near normal values occurs after 3–4 days in copper-repleted chicks. Moreover, elastolysis was enhanced when the content of dehydrolysinonorleucine in elastin was abnormally low. The chemical modification of lysyl residue in elastin by citroconylation, however, did not influence the rate of elastolysis. We have shown previously that tropoelastin messenger RNA activity and synthesis are not influenced by dietary copper deprivation (1986,
Biochem. J.
236, 17–23). Rather, as demonstrated herein, the decrease in elastin content in arteries of copper-deficient birds appears to be more the result of enhanced degradation. Restoration of normal crosslinking restores deposition and imparts resistance to elastolysis. Moreover, serum appears to be a good source of elastolytic proteinases when the elastin substrate is partially or abnormally crosslinked.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>2327789</pmid><doi>10.1016/0003-9861(90)90267-3</doi><tpages>7</tpages></addata></record> |
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subjects | Amino Acids - analysis Analytical, structural and metabolic biochemistry Animals Aorta, Thoracic - metabolism Biological and medical sciences Chickens Copper - metabolism Cross-Linking Reagents elastin Elastin - metabolism Fundamental and applied biological sciences. Psychology Glycoproteins Hydrolysis Organ Culture Techniques Proteins Solubility Valine - metabolism |
title | Elastin metabolism during recovery from impaired crosslink formation |
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