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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2002-1-25
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pubmed:abstractText |
Most type I and II keratin genes are spatially and temporally regulated in a pairwise manner in epithelial tissues, where they represent the major structural proteins. Epithelia can be partitioned into simple (single-layered) and complex (multilayered) types. We compared the structural and mechanical properties of natural keratin polymers occurring in complex (K5-K14) and simple (K8-K18) epithelia. The intrinsic properties of these distantly related keratin filaments, whether dispersed or bundled in vitro, were surprisingly similar in all respects when at high polymer concentration. When type I and II assembly partners were switched to give rise to mismatched polymers (K5-K18; K8-K14), the interfilament interactions, which determine the structural and mechanical properties of keratin polymers, were significantly altered. We also show that a K5-K16 polymer exhibits lesser elasticity than K5- K14, which may help explain the inability of K16 to fully rescue the skin blistering characteristic of K14 null mice. The property of self-interaction exhibited by keratin filaments is likely to assist their function in vivo and may account for the relative paucity of cytoplasmic and keratin-specific cross-linkers. Our findings underscore the fundamental importance of pairwise polymerization and have implications for the functional significance of keratin sequence diversity.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-10064706,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-1018318,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-10477769,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-10511477,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-10679360,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-10733956,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-10747083,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-10998598,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-11013209,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-11062258,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-11179900,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-11331879,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-11372009,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-11428894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-11724817,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-1694855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-1854482,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-2414304,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-2422179,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-2478566,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-416022,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-6196784,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-7528156,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-7539810,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-7634137,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-7678835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-7979242,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-8636216,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-9011570,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-9141415,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-9157008,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-9405470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-9438837,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-9508776,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-9786957,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11809846-9916038
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1059-1524
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
382-91
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11809846-Biopolymers,
pubmed-meshheading:11809846-Elasticity,
pubmed-meshheading:11809846-Epithelial Cells,
pubmed-meshheading:11809846-Escherichia coli,
pubmed-meshheading:11809846-Gels,
pubmed-meshheading:11809846-Humans,
pubmed-meshheading:11809846-Hydrogen-Ion Concentration,
pubmed-meshheading:11809846-Intermediate Filaments,
pubmed-meshheading:11809846-Keratins,
pubmed-meshheading:11809846-Recombinant Fusion Proteins,
pubmed-meshheading:11809846-Rheology,
pubmed-meshheading:11809846-Stress, Mechanical,
pubmed-meshheading:11809846-Transformation, Genetic,
pubmed-meshheading:11809846-Viscosity
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pubmed:year |
2002
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pubmed:articleTitle |
Pairwise assembly determines the intrinsic potential for self-organization and mechanical properties of keratin filaments.
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pubmed:affiliation |
Department of Chemical Engineering, The Johns Hopkins University, Baltimore, MD 21218, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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