Catabolism of intact fibrillin microfibrils by neutrophil elastase, chymotrypsin and trypsin
We present ultrastructural and biochemical evidence for the turnover of intact fibrillin microfibrils by the serine proteinases, neutrophil elastase, chymotrypsin and trypsin. Rotary shadowing electron microscopy revealed that serine proteinase treatment of intact microfibrils isolated from foetal b...
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| Veröffentlicht in: | FEBS letters 1994-08, Vol.351 (1), p.85-89 |
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| creator | Kielty, Cay M. Woolley, David E. Whittaker, Stephen P. Shuttleworth, C.Adrian |
| description | We present ultrastructural and biochemical evidence for the turnover of intact fibrillin microfibrils by the serine proteinases, neutrophil elastase, chymotrypsin and trypsin. Rotary shadowing electron microscopy revealed that serine proteinase treatment of intact microfibrils isolated from foetal bovine skin resulted in extensive degradation. Microfibrils were destroyed by neutrophil elastase and effectively disrupted by chymotrypsin and trypsin, with no morphologically identifiable arrays remaining. Evidence of defined fibrillin degradation products was obtained by Western blotting of these enzyme-treated fibrillin assemblies. Fibrillin immunoprecipitated from dermal fibroblast culture medium was also comprehensively degraded by these enzymes. These observations demonstrate that serine proteinases are potent effectors for the physiological and pathological catabolism of microfibrils, and suggest a key role in elastic fibre degradation. |
| doi_str_mv | 10.1016/0014-5793(94)00818-3 |
| format | Article |
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Rotary shadowing electron microscopy revealed that serine proteinase treatment of intact microfibrils isolated from foetal bovine skin resulted in extensive degradation. Microfibrils were destroyed by neutrophil elastase and effectively disrupted by chymotrypsin and trypsin, with no morphologically identifiable arrays remaining. Evidence of defined fibrillin degradation products was obtained by Western blotting of these enzyme-treated fibrillin assemblies. Fibrillin immunoprecipitated from dermal fibroblast culture medium was also comprehensively degraded by these enzymes. 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Rotary shadowing electron microscopy revealed that serine proteinase treatment of intact microfibrils isolated from foetal bovine skin resulted in extensive degradation. Microfibrils were destroyed by neutrophil elastase and effectively disrupted by chymotrypsin and trypsin, with no morphologically identifiable arrays remaining. Evidence of defined fibrillin degradation products was obtained by Western blotting of these enzyme-treated fibrillin assemblies. Fibrillin immunoprecipitated from dermal fibroblast culture medium was also comprehensively degraded by these enzymes. These observations demonstrate that serine proteinases are potent effectors for the physiological and pathological catabolism of microfibrils, and suggest a key role in elastic fibre degradation.</description><subject>Animals</subject><subject>Blotting, Western</subject><subject>Catabolism</subject><subject>Cattle</subject><subject>Chymotrypsin - metabolism</subject><subject>Connective Tissue - metabolism</subject><subject>Connective Tissue - ultrastructure</subject><subject>Elastase</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fibrillin microfibril</subject><subject>Fibrillins</subject><subject>Humans</subject><subject>Leukocyte Elastase</subject><subject>Microfilament Proteins - metabolism</subject><subject>Pancreatic Elastase - metabolism</subject><subject>Serine proteinase</subject><subject>Skin - embryology</subject><subject>Skin - metabolism</subject><subject>Skin - ultrastructure</subject><subject>Trypsin - metabolism</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUMtq3DAUFaUhnST9gxa0KgnUqWTJsrQJJMNMEhjoJsuAkOUroiLbU8lO8d_HHg9Ztl1J956HdA5CXyi5poSKH4RQnhWlYpeKXxEiqczYB7SismQZ40J-RKt3yid0ltIvMs2SqlN0KkkphFIr9Lw2vam64FODO4d92xvbY-er6EPwLW68jd0yJlyNuIWhj93-xQcMwaTeJPiO7cvYdH0c92lSmLbGx_sFOnEmJPh8PM_R03bztH7Idj_vH9e3u8wWgrGsqEUlbF5CXeeFEIWw3BVClZxKzp0gUsmcWWekBMsq5kpROLDVFNmwEjg7R98W233sfg-Qet34ZCEE00I3JH2ISkj-TyIVZUFyoiYiX4hT-JQiOL2PvjFx1JTouXw9N6vnZrXi-lC-ZpPs69F_qBqo30XHtid8u-B_fIDxvzz1dnOXz8C8V_ywnR-6WYxgavXVQ9TJemgt1D6C7XXd-b__9A0Qqaeg</recordid><startdate>19940829</startdate><enddate>19940829</enddate><creator>Kielty, Cay M.</creator><creator>Woolley, David E.</creator><creator>Whittaker, Stephen P.</creator><creator>Shuttleworth, C.Adrian</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7T5</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19940829</creationdate><title>Catabolism of intact fibrillin microfibrils by neutrophil elastase, chymotrypsin and trypsin</title><author>Kielty, Cay M. ; Woolley, David E. ; Whittaker, Stephen P. ; Shuttleworth, C.Adrian</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5633-5d6b6c27edd256656c4f569741844f6089823cfa88ec3b3f765fecb008a37e43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Animals</topic><topic>Blotting, Western</topic><topic>Catabolism</topic><topic>Cattle</topic><topic>Chymotrypsin - metabolism</topic><topic>Connective Tissue - metabolism</topic><topic>Connective Tissue - ultrastructure</topic><topic>Elastase</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fibrillin microfibril</topic><topic>Fibrillins</topic><topic>Humans</topic><topic>Leukocyte Elastase</topic><topic>Microfilament Proteins - metabolism</topic><topic>Pancreatic Elastase - metabolism</topic><topic>Serine proteinase</topic><topic>Skin - embryology</topic><topic>Skin - metabolism</topic><topic>Skin - ultrastructure</topic><topic>Trypsin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kielty, Cay M.</creatorcontrib><creatorcontrib>Woolley, David E.</creatorcontrib><creatorcontrib>Whittaker, Stephen P.</creatorcontrib><creatorcontrib>Shuttleworth, C.Adrian</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kielty, Cay M.</au><au>Woolley, David E.</au><au>Whittaker, Stephen P.</au><au>Shuttleworth, C.Adrian</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Catabolism of intact fibrillin microfibrils by neutrophil elastase, chymotrypsin and trypsin</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1994-08-29</date><risdate>1994</risdate><volume>351</volume><issue>1</issue><spage>85</spage><epage>89</epage><pages>85-89</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>We present ultrastructural and biochemical evidence for the turnover of intact fibrillin microfibrils by the serine proteinases, neutrophil elastase, chymotrypsin and trypsin. Rotary shadowing electron microscopy revealed that serine proteinase treatment of intact microfibrils isolated from foetal bovine skin resulted in extensive degradation. Microfibrils were destroyed by neutrophil elastase and effectively disrupted by chymotrypsin and trypsin, with no morphologically identifiable arrays remaining. Evidence of defined fibrillin degradation products was obtained by Western blotting of these enzyme-treated fibrillin assemblies. Fibrillin immunoprecipitated from dermal fibroblast culture medium was also comprehensively degraded by these enzymes. These observations demonstrate that serine proteinases are potent effectors for the physiological and pathological catabolism of microfibrils, and suggest a key role in elastic fibre degradation.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>8076699</pmid><doi>10.1016/0014-5793(94)00818-3</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1994-08, Vol.351 (1), p.85-89 |
| issn | 0014-5793 1873-3468 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Blotting, Western Catabolism Cattle Chymotrypsin - metabolism Connective Tissue - metabolism Connective Tissue - ultrastructure Elastase Electrophoresis, Polyacrylamide Gel Fibrillin microfibril Fibrillins Humans Leukocyte Elastase Microfilament Proteins - metabolism Pancreatic Elastase - metabolism Serine proteinase Skin - embryology Skin - metabolism Skin - ultrastructure Trypsin - metabolism |
| title | Catabolism of intact fibrillin microfibrils by neutrophil elastase, chymotrypsin and trypsin |
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