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Article: Defective prelamin A processing and muscular and adipocyte alterations in Zmpste24 metalloproteinase-deficient mice

TitleDefective prelamin A processing and muscular and adipocyte alterations in Zmpste24 metalloproteinase-deficient mice
Authors
Issue Date2002
PublisherNature Publishing Group. The Journal's web site is located at http://www.genetics.nature.com
Citation
Nature Genetics, 2002, v. 31 n. 1, p. 94-99 How to Cite?
AbstractThe mouse ortholog of human FACE-1, Zmpste24, is a multi-spanning membrane protein widely distributed in mammalian tissues and structurally related to Afc1p/ste24p, a yeast metalloproteinase involved in the maturation of fungal pheromones. Disruption of the gene Zmpste24 caused severe growth retardation and premature death in homozygous-null mice. Histopathological analysis of the mutant mice revealed several abnormalities, including dilated cardiomyopathy, muscular dystrophy and lipodystrophy. These alterations are similar to those developed by mice deficient in A-type lamin, a major component of the nuclear lamina, and phenocopy most defects observed in humans with diverse congenital laminopathies. In agreement with this finding, Zmpste24-null mice are defective in the proteolytic processing of prelamin A. This deficiency in prelamin A maturation leads to the generation of abnormalities in nuclear architecture that probably underlie the many phenotypes observed in both mice and humans with mutations in the lamin A gene. These results indicate that prelamin A is a specific substrate for Zmpste24 and demonstrate the usefulness of genetic approaches for identifying the in vivo substrates of proteolytic enzymes.
Persistent Identifierhttp://hdl.handle.net/10722/147473
ISSN
2015 Impact Factor: 31.616
2015 SCImago Journal Rankings: 23.762
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorPendás, AMen_US
dc.contributor.authorZhou, Zen_US
dc.contributor.authorCadiñanos, Jen_US
dc.contributor.authorFreije, JMPen_US
dc.contributor.authorWang, Jen_US
dc.contributor.authorHultenby, Ken_US
dc.contributor.authorAstudillo, Aen_US
dc.contributor.authorWernerson, Aen_US
dc.contributor.authorRodríguez, Fen_US
dc.contributor.authorTryggvason, Ken_US
dc.contributor.authorLópez-Otín, Cen_US
dc.date.accessioned2012-05-29T06:03:58Z-
dc.date.available2012-05-29T06:03:58Z-
dc.date.issued2002en_US
dc.identifier.citationNature Genetics, 2002, v. 31 n. 1, p. 94-99en_US
dc.identifier.issn1061-4036en_US
dc.identifier.urihttp://hdl.handle.net/10722/147473-
dc.description.abstractThe mouse ortholog of human FACE-1, Zmpste24, is a multi-spanning membrane protein widely distributed in mammalian tissues and structurally related to Afc1p/ste24p, a yeast metalloproteinase involved in the maturation of fungal pheromones. Disruption of the gene Zmpste24 caused severe growth retardation and premature death in homozygous-null mice. Histopathological analysis of the mutant mice revealed several abnormalities, including dilated cardiomyopathy, muscular dystrophy and lipodystrophy. These alterations are similar to those developed by mice deficient in A-type lamin, a major component of the nuclear lamina, and phenocopy most defects observed in humans with diverse congenital laminopathies. In agreement with this finding, Zmpste24-null mice are defective in the proteolytic processing of prelamin A. This deficiency in prelamin A maturation leads to the generation of abnormalities in nuclear architecture that probably underlie the many phenotypes observed in both mice and humans with mutations in the lamin A gene. These results indicate that prelamin A is a specific substrate for Zmpste24 and demonstrate the usefulness of genetic approaches for identifying the in vivo substrates of proteolytic enzymes.en_US
dc.languageengen_US
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.genetics.nature.comen_US
dc.relation.ispartofNature Geneticsen_US
dc.subject.meshAdipocytes - Metabolism - Pathologyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCell Nucleus - Pathologyen_US
dc.subject.meshFemaleen_US
dc.subject.meshHumansen_US
dc.subject.meshMaleen_US
dc.subject.meshMembrane Proteins - Deficiency - Geneticsen_US
dc.subject.meshMetalloendopeptidases - Deficiency - Geneticsen_US
dc.subject.meshMiceen_US
dc.subject.meshMice, Inbred C57blen_US
dc.subject.meshMice, Knockouten_US
dc.subject.meshMuscles - Metabolism - Pathologyen_US
dc.subject.meshMyocardium - Pathologyen_US
dc.subject.meshNuclear Proteins - Metabolismen_US
dc.subject.meshPhenotypeen_US
dc.subject.meshProtein Precursors - Metabolismen_US
dc.subject.meshProtein Processing, Post-Translationalen_US
dc.titleDefective prelamin A processing and muscular and adipocyte alterations in Zmpste24 metalloproteinase-deficient miceen_US
dc.typeArticleen_US
dc.identifier.emailZhou, Z:zhongjun@hkucc.hku.hken_US
dc.identifier.authorityZhou, Z=rp00503en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1038/ng871en_US
dc.identifier.pmid11923874-
dc.identifier.scopuseid_2-s2.0-0036578920en_US
dc.identifier.hkuros84048-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0036578920&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume31en_US
dc.identifier.issue1en_US
dc.identifier.spage94en_US
dc.identifier.epage99en_US
dc.identifier.isiWOS:000175362500022-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridPendás, AM=35595485200en_US
dc.identifier.scopusauthoridZhou, Z=8631856300en_US
dc.identifier.scopusauthoridCadiñanos, J=6506257822en_US
dc.identifier.scopusauthoridFreije, JMP=7005118867en_US
dc.identifier.scopusauthoridWang, J=8631854400en_US
dc.identifier.scopusauthoridHultenby, K=7005799638en_US
dc.identifier.scopusauthoridAstudillo, A=6701460023en_US
dc.identifier.scopusauthoridWernerson, A=6602175836en_US
dc.identifier.scopusauthoridRodríguez, F=7402203048en_US
dc.identifier.scopusauthoridTryggvason, K=7102025185en_US
dc.identifier.scopusauthoridLópez-Otín, C=7102600806en_US

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