Article: Characterization of tissue-specific LIM domain protein (FHL1C) which is an alternatively spliced isoform of a human LIM-only protein (FHL1)

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TitleCharacterization of tissue-specific LIM domain protein (FHL1C) which is an alternatively spliced isoform of a human LIM-only protein (FHL1)
AuthorsNg, EKO1
Lee, SMY
Li, HY1
Ngai, SM1
Tsui, SKW
Waye, MMY
Lee, CY1
Fung, KP1
KeywordsFHL1
FHL1C
KyoT2
RBP-J
SLIM1
Zinc finger protein
Issue Date2001
PublisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/35503
CitationJournal Of Cellular Biochemistry, 2001, v. 82 n. 1, p. 1-10 [How to Cite?]
DOI: http://dx.doi.org/10.1002/jcb.1110
AbstractWe have cloned and characterized another alternatively spliced isoform of the human four-and-a-half LIM domain protein 1 (FHL1), designated FHL1C. FHL1C contains a single zinc finger and two tandem repeats of LIM domains at the N-terminus followed by a putative RBP-J binding region at the C-terminus. FHL1C shares the same N-terminal two-and-a-half LIM domains with FHL1 but different C-terminal protein sequences. Due to the absence of the exon 4 in FHL1 C, there is a frame-shift in the 3′ coding region. Sequence analysis indicated that FHL1C is the human homolog of murine KyoT2. The Northern blot and RT-PCR results revealed that FHL1 is widely expressed in human tissues, including skeletal muscle and heart at a high level, albeit as a relatively low abundance transcript in brain, placenta, lung, liver, kidney, pancreas, and testis. In contrast, FHL1C is specifically expressed in testis, skeletal muscle, and heart at a relatively low level compared with FHL1. The expression of FHL1C transcripts was also seen in aorta, left atrium, left, and right ventricles of human heart at low level. Immunoblot analysis using affinity-purified anti-FHL1C antipeptide antibodies confirmed a 20 kDa protein of FHL1C in human skeletal muscle and heart. Unlike FHL1 B, which is another FHL1 isoform recently reported by our group and localized predominantly in the nucleus [Lee et al., 1999], FHL1C is localized both in the nucleus and cytoplasm of mammalian cell. © 2001 Wiley-Liss, Inc.
ISSN0730-2312
2011 Impact Factor: 2.868
2011 SCImago Journal Rankings: 0.379
DOIhttp://dx.doi.org/10.1002/jcb.1110
ISI Accession Number IDWOS:000169049400001
ReferencesReferences in Scopus
DC Field
Value
dc.contributor.authorNg, EKO
dc.contributor.authorLee, SMY
dc.contributor.authorLi, HY
dc.contributor.authorNgai, SM
dc.contributor.authorTsui, SKW
dc.contributor.authorWaye, MMY
dc.contributor.authorLee, CY
dc.contributor.authorFung, KP
dc.date.accessioned2010-09-17T10:37:45Z
dc.date.available2010-09-17T10:37:45Z
dc.date.issued2001
dc.description.abstractWe have cloned and characterized another alternatively spliced isoform of the human four-and-a-half LIM domain protein 1 (FHL1), designated FHL1C. FHL1C contains a single zinc finger and two tandem repeats of LIM domains at the N-terminus followed by a putative RBP-J binding region at the C-terminus. FHL1C shares the same N-terminal two-and-a-half LIM domains with FHL1 but different C-terminal protein sequences. Due to the absence of the exon 4 in FHL1 C, there is a frame-shift in the 3′ coding region. Sequence analysis indicated that FHL1C is the human homolog of murine KyoT2. The Northern blot and RT-PCR results revealed that FHL1 is widely expressed in human tissues, including skeletal muscle and heart at a high level, albeit as a relatively low abundance transcript in brain, placenta, lung, liver, kidney, pancreas, and testis. In contrast, FHL1C is specifically expressed in testis, skeletal muscle, and heart at a relatively low level compared with FHL1. The expression of FHL1C transcripts was also seen in aorta, left atrium, left, and right ventricles of human heart at low level. Immunoblot analysis using affinity-purified anti-FHL1C antipeptide antibodies confirmed a 20 kDa protein of FHL1C in human skeletal muscle and heart. Unlike FHL1 B, which is another FHL1 isoform recently reported by our group and localized predominantly in the nucleus [Lee et al., 1999], FHL1C is localized both in the nucleus and cytoplasm of mammalian cell. © 2001 Wiley-Liss, Inc.
dc.description.natureLink_to_subscribed_fulltext
dc.identifier.citationJournal Of Cellular Biochemistry, 2001, v. 82 n. 1, p. 1-10 [How to Cite?]
DOI: http://dx.doi.org/10.1002/jcb.1110
dc.identifier.doihttp://dx.doi.org/10.1002/jcb.1110
dc.identifier.epage10
dc.identifier.isiWOS:000169049400001
dc.identifier.issn0730-2312
2011 Impact Factor: 2.868
2011 SCImago Journal Rankings: 0.379
dc.identifier.issue1
dc.identifier.pmid11400158
dc.identifier.scopuseid_2-s2.0-0034994307
dc.identifier.spage1
dc.identifier.urihttp://hdl.handle.net/10722/92157
dc.identifier.volume82
dc.languageeng
dc.publisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/35503
dc.publisher.placeUnited States
dc.relation.ispartofJournal of Cellular Biochemistry
dc.relation.referencesReferences in Scopus
dc.subjectFHL1
dc.subjectFHL1C
dc.subjectKyoT2
dc.subjectRBP-J
dc.subjectSLIM1
dc.subjectZinc finger protein
dc.titleCharacterization of tissue-specific LIM domain protein (FHL1C) which is an alternatively spliced isoform of a human LIM-only protein (FHL1)
dc.typeArticle
Author Affiliations
  1. Chinese University of Hong Kong