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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Secretion of amyloidogenic gelsolin progressively compromises protein homeostasis leading to the intracellular aggregation of proteins</title><author><name sortKey="Page, Lesley J" sort="Page, Lesley J" uniqKey="Page L" first="Lesley J." last="Page">Lesley J. Page</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Suk, Ji Young" sort="Suk, Ji Young" uniqKey="Suk J" first="Ji Young" last="Suk">Ji Young Suk</name><affiliation><nlm:aff id="aff2">Departments of Chemistry and Molecular and Experimental Medicine,</nlm:aff></affiliation></author><author><name sortKey="Bazhenova, Lyudmila" sort="Bazhenova, Lyudmila" uniqKey="Bazhenova L" first="Lyudmila" last="Bazhenova">Lyudmila Bazhenova</name><affiliation><nlm:aff id="aff2">Departments of Chemistry and Molecular and Experimental Medicine,</nlm:aff></affiliation></author><author><name sortKey="Fleming, Sheila M" sort="Fleming, Sheila M" uniqKey="Fleming S" first="Sheila M." last="Fleming">Sheila M. Fleming</name><affiliation><nlm:aff id="aff6">Department of Neurobiology, The David Geffen School of Medicine, University of California, Los Angeles, CA 90095;</nlm:aff></affiliation></author><author><name sortKey="Wood, Malcolm" sort="Wood, Malcolm" uniqKey="Wood M" first="Malcolm" last="Wood">Malcolm Wood</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Jiang, Yun" sort="Jiang, Yun" uniqKey="Jiang Y" first="Yun" last="Jiang">Yun Jiang</name><affiliation><nlm:aff wicri:cut="; and" id="aff7">Department of Pathology, University of California at San Diego, La Jolla, CA 92093</nlm:aff></affiliation></author><author><name sortKey="Guo, Ling T" sort="Guo, Ling T" uniqKey="Guo L" first="Ling T." last="Guo">Ling T. Guo</name><affiliation><nlm:aff wicri:cut="; and" id="aff7">Department of Pathology, University of California at San Diego, La Jolla, CA 92093</nlm:aff></affiliation></author><author><name sortKey="Mizisin, Andrew P" sort="Mizisin, Andrew P" uniqKey="Mizisin A" first="Andrew P." last="Mizisin">Andrew P. Mizisin</name><affiliation><nlm:aff wicri:cut="; and" id="aff7">Department of Pathology, University of California at San Diego, La Jolla, CA 92093</nlm:aff></affiliation></author><author><name sortKey="Kisilevsky, Robert" sort="Kisilevsky, Robert" uniqKey="Kisilevsky R" first="Robert" last="Kisilevsky">Robert Kisilevsky</name><affiliation><nlm:aff id="aff8">Departments of Pathology and Molecular Medicine, and Biochemistry, Queen's University, Kingston, ON, Canada K7L 3N6</nlm:aff></affiliation></author><author><name sortKey="Shelton, G Diane" sort="Shelton, G Diane" uniqKey="Shelton G" first="G. Diane" last="Shelton">G. Diane Shelton</name><affiliation><nlm:aff wicri:cut="; and" id="aff7">Department of Pathology, University of California at San Diego, La Jolla, CA 92093</nlm:aff></affiliation></author><author><name sortKey="Balch, William E" sort="Balch, William E" uniqKey="Balch W" first="William E." last="Balch">William E. Balch</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation><affiliation><nlm:aff wicri:cut=", and" id="aff3">Department of Chemical Physiology</nlm:aff></affiliation><affiliation><nlm:aff wicri:cut=", and" id="aff4">Institute for Childhood and Neglected Diseases</nlm:aff></affiliation><affiliation><nlm:aff id="aff5">The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037;</nlm:aff></affiliation></author><author><name sortKey="Kelly, Jeffery W" sort="Kelly, Jeffery W" uniqKey="Kelly J" first="Jeffery W." last="Kelly">Jeffery W. Kelly</name><affiliation><nlm:aff id="aff2">Departments of Chemistry and Molecular and Experimental Medicine,</nlm:aff></affiliation><affiliation><nlm:aff id="aff5">The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037;</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">19549824</idno><idno type="pmc">2708763</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2708763</idno><idno type="RBID">PMC:2708763</idno><idno type="doi">10.1073/pnas.0811753106</idno><date when="2009">2009</date><idno type="wicri:Area/Pmc/Corpus">000654</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000654</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Secretion of amyloidogenic gelsolin progressively compromises protein homeostasis leading to the intracellular aggregation of proteins</title><author><name sortKey="Page, Lesley J" sort="Page, Lesley J" uniqKey="Page L" first="Lesley J." last="Page">Lesley J. Page</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Suk, Ji Young" sort="Suk, Ji Young" uniqKey="Suk J" first="Ji Young" last="Suk">Ji Young Suk</name><affiliation><nlm:aff id="aff2">Departments of Chemistry and Molecular and Experimental Medicine,</nlm:aff></affiliation></author><author><name sortKey="Bazhenova, Lyudmila" sort="Bazhenova, Lyudmila" uniqKey="Bazhenova L" first="Lyudmila" last="Bazhenova">Lyudmila Bazhenova</name><affiliation><nlm:aff id="aff2">Departments of Chemistry and Molecular and Experimental Medicine,</nlm:aff></affiliation></author><author><name sortKey="Fleming, Sheila M" sort="Fleming, Sheila M" uniqKey="Fleming S" first="Sheila M." last="Fleming">Sheila M. Fleming</name><affiliation><nlm:aff id="aff6">Department of Neurobiology, The David Geffen School of Medicine, University of California, Los Angeles, CA 90095;</nlm:aff></affiliation></author><author><name sortKey="Wood, Malcolm" sort="Wood, Malcolm" uniqKey="Wood M" first="Malcolm" last="Wood">Malcolm Wood</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Jiang, Yun" sort="Jiang, Yun" uniqKey="Jiang Y" first="Yun" last="Jiang">Yun Jiang</name><affiliation><nlm:aff wicri:cut="; and" id="aff7">Department of Pathology, University of California at San Diego, La Jolla, CA 92093</nlm:aff></affiliation></author><author><name sortKey="Guo, Ling T" sort="Guo, Ling T" uniqKey="Guo L" first="Ling T." last="Guo">Ling T. Guo</name><affiliation><nlm:aff wicri:cut="; and" id="aff7">Department of Pathology, University of California at San Diego, La Jolla, CA 92093</nlm:aff></affiliation></author><author><name sortKey="Mizisin, Andrew P" sort="Mizisin, Andrew P" uniqKey="Mizisin A" first="Andrew P." last="Mizisin">Andrew P. Mizisin</name><affiliation><nlm:aff wicri:cut="; and" id="aff7">Department of Pathology, University of California at San Diego, La Jolla, CA 92093</nlm:aff></affiliation></author><author><name sortKey="Kisilevsky, Robert" sort="Kisilevsky, Robert" uniqKey="Kisilevsky R" first="Robert" last="Kisilevsky">Robert Kisilevsky</name><affiliation><nlm:aff id="aff8">Departments of Pathology and Molecular Medicine, and Biochemistry, Queen's University, Kingston, ON, Canada K7L 3N6</nlm:aff></affiliation></author><author><name sortKey="Shelton, G Diane" sort="Shelton, G Diane" uniqKey="Shelton G" first="G. Diane" last="Shelton">G. Diane Shelton</name><affiliation><nlm:aff wicri:cut="; and" id="aff7">Department of Pathology, University of California at San Diego, La Jolla, CA 92093</nlm:aff></affiliation></author><author><name sortKey="Balch, William E" sort="Balch, William E" uniqKey="Balch W" first="William E." last="Balch">William E. Balch</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation><affiliation><nlm:aff wicri:cut=", and" id="aff3">Department of Chemical Physiology</nlm:aff></affiliation><affiliation><nlm:aff wicri:cut=", and" id="aff4">Institute for Childhood and Neglected Diseases</nlm:aff></affiliation><affiliation><nlm:aff id="aff5">The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037;</nlm:aff></affiliation></author><author><name sortKey="Kelly, Jeffery W" sort="Kelly, Jeffery W" uniqKey="Kelly J" first="Jeffery W." last="Kelly">Jeffery W. Kelly</name><affiliation><nlm:aff id="aff2">Departments of Chemistry and Molecular and Experimental Medicine,</nlm:aff></affiliation><affiliation><nlm:aff id="aff5">The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037;</nlm:aff></affiliation></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><idno type="eISSN">1091-6490</idno><imprint><date when="2009">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Familial amyloidosis of Finnish type (FAF) is a systemic amyloid disease associated with the deposition of proteolytic fragments of mutant (D187N/Y) plasma gelsolin. We report a mouse model of FAF featuring a muscle-specific promoter to drive D187N gelsolin synthesis. This model recapitulates the aberrant endoproteolytic cascade and the aging-associated extracellular amyloid deposition of FAF. Amyloidogenesis is observed only in tissues synthesizing human D187N gelsolin, despite the presence of full-length D187N gelsolin and its 68-kDa cleavage product in blood—demonstrating the importance of local synthesis in FAF. Loss of muscle strength was progressive in homozygous D187N gelsolin mice. The presence of misfolding-prone D187N gelsolin appears to exacerbate the age-associated decline in cellular protein homeostasis (proteostasis), reflected by the intracellular deposition of numerous proteins, a characteristic of the most common degenerative muscle disease of aging humans, sporadic inclusion body myositis.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Proc Natl Acad Sci U S A</journal-id><journal-id journal-id-type="hwp">pnas</journal-id><journal-id journal-id-type="pmc">pnas</journal-id><journal-id journal-id-type="publisher-id">PNAS</journal-id><journal-title-group><journal-title>Proceedings of the National Academy of Sciences of the United States of America</journal-title></journal-title-group><issn pub-type="ppub">0027-8424</issn><issn pub-type="epub">1091-6490</issn><publisher><publisher-name>National Academy of Sciences</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">19549824</article-id><article-id pub-id-type="pmc">2708763</article-id><article-id pub-id-type="publisher-id">8374</article-id><article-id pub-id-type="doi">10.1073/pnas.0811753106</article-id><article-categories><subj-group subj-group-type="heading"><subject>Biological Sciences</subject><subj-group><subject>Cell Biology</subject></subj-group></subj-group></article-categories><title-group><article-title>Secretion of amyloidogenic gelsolin progressively compromises protein homeostasis leading to the intracellular aggregation of proteins</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Page</surname><given-names>Lesley J.</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author"><name><surname>Suk</surname><given-names>Ji Young</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref><xref ref-type="author-notes" rid="FN1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Bazhenova</surname><given-names>Lyudmila</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref><xref ref-type="author-notes" rid="FN1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Fleming</surname><given-names>Sheila M.</given-names></name><xref ref-type="aff" rid="aff6"><sup>c</sup></xref></contrib><contrib contrib-type="author"><name><surname>Wood</surname><given-names>Malcolm</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author"><name><surname>Jiang</surname><given-names>Yun</given-names></name><xref ref-type="aff" rid="aff7"><sup>d</sup></xref></contrib><contrib contrib-type="author"><name><surname>Guo</surname><given-names>Ling T.</given-names></name><xref ref-type="aff" rid="aff7"><sup>d</sup></xref></contrib><contrib contrib-type="author"><name><surname>Mizisin</surname><given-names>Andrew P.</given-names></name><xref ref-type="aff" rid="aff7"><sup>d</sup></xref></contrib><contrib contrib-type="author"><name><surname>Kisilevsky</surname><given-names>Robert</given-names></name><xref ref-type="aff" rid="aff8"><sup>e</sup></xref></contrib><contrib contrib-type="author"><name><surname>Shelton</surname><given-names>G. Diane</given-names></name><xref ref-type="aff" rid="aff7"><sup>d</sup></xref></contrib><contrib contrib-type="author"><name><surname>Balch</surname><given-names>William E.</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref><xref ref-type="aff" rid="aff3"><sup>f</sup></xref><xref ref-type="aff" rid="aff4"><sup>g</sup></xref><xref ref-type="aff" rid="aff5"><sup>h</sup></xref><xref ref-type="corresp" rid="cor1"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Kelly</surname><given-names>Jeffery W.</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref><xref ref-type="aff" rid="aff5"><sup>h</sup></xref><xref ref-type="corresp" rid="cor1"><sup>2</sup></xref></contrib><aff id="aff1">Department of<sup>a</sup>Cell Biology,</aff><aff id="aff2"><sup>b</sup>Departments of Chemistry and Molecular and Experimental Medicine,</aff><aff id="aff3"><sup>f</sup>Department of Chemical Physiology, and</aff><aff id="aff4"><sup>g</sup>Institute for Childhood and Neglected Diseases, and</aff><aff id="aff5"><sup>h</sup>The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037;</aff><aff id="aff6"><sup>c</sup>Department of Neurobiology, The David Geffen School of Medicine, University of California, Los Angeles, CA 90095;</aff><aff id="aff7"><sup>d</sup>Department of Pathology, University of California at San Diego, La Jolla, CA 92093; and</aff><aff id="aff8"><sup>e</sup>Departments of Pathology and Molecular Medicine, and Biochemistry, Queen's University, Kingston, ON, Canada K7L 3N6</aff></contrib-group><author-notes><corresp id="cor1"><sup>2</sup>To whom correspondence may be addressed. E-mail: <email>webalch@scripps.edu</email> or <email>jkelly@scripps.edu</email></corresp><fn fn-type="edited-by"><p>Edited by Charles Weissmann, Scripps Florida, Jupiter, FL, and approved May 1, 2009</p></fn><fn fn-type="con"><p>Author contributions: L.J.P., W.E.B., and J.W.K. designed research; L.J.P., J.Y.S., L.B., Y.J., L.T.G., and A.P.M. performed research; L.J.P., S.M.F., M.W., Y.J., L.T.G., A.P.M., R.K., G.D.S., and W.E.B. analyzed data; L.J.P., G.D.S., W.E.B., and J.W.K. wrote the paper.</p></fn><fn id="FN1" fn-type="equal"><p><sup>1</sup>J.Y.S. and L.B. contributed equally to this work.</p></fn></author-notes><pub-date pub-type="ppub"><day>7</day><month>7</month><year>2009</year></pub-date><pub-date pub-type="epub"><day>19</day><month>6</month><year>2009</year></pub-date><volume>106</volume><issue>27</issue><fpage>11125</fpage><lpage>11130</lpage><history><date date-type="received"><day>20</day><month>11</month><year>2008</year></date></history><permissions></permissions><self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zpq02709011125.pdf"></self-uri><abstract><p>Familial amyloidosis of Finnish type (FAF) is a systemic amyloid disease associated with the deposition of proteolytic fragments of mutant (D187N/Y) plasma gelsolin. We report a mouse model of FAF featuring a muscle-specific promoter to drive D187N gelsolin synthesis. This model recapitulates the aberrant endoproteolytic cascade and the aging-associated extracellular amyloid deposition of FAF. Amyloidogenesis is observed only in tissues synthesizing human D187N gelsolin, despite the presence of full-length D187N gelsolin and its 68-kDa cleavage product in blood—demonstrating the importance of local synthesis in FAF. Loss of muscle strength was progressive in homozygous D187N gelsolin mice. The presence of misfolding-prone D187N gelsolin appears to exacerbate the age-associated decline in cellular protein homeostasis (proteostasis), reflected by the intracellular deposition of numerous proteins, a characteristic of the most common degenerative muscle disease of aging humans, sporadic inclusion body myositis.</p></abstract><kwd-group><kwd>amyloid</kwd><kwd>proteostasis</kwd><kwd>sporadic inclusion body myositis</kwd><kwd>FAF mouse</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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