File Download
  • No File Attached
 
Links for fulltext
(May Require Subscription)
 
Supplementary

Article: Characterization of tissue-specific LIM domain protein (FHL1C) which is an alternatively spliced isoform of a human LIM-only protein (FHL1)
  • Basic View
  • Metadata View
  • XML View
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
2013 Impact Factor: 3.368
 
DOIhttp://dx.doi.org/10.1002/jcb.1110
 
ISI Accession Number IDWOS:000169049400001
 
ReferencesReferences in Scopus
 
DC FieldValue
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
2013 Impact Factor: 3.368
 
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
 
<?xml encoding="utf-8" version="1.0"?>
<item><contributor.author>Ng, EKO</contributor.author>
<contributor.author>Lee, SMY</contributor.author>
<contributor.author>Li, HY</contributor.author>
<contributor.author>Ngai, SM</contributor.author>
<contributor.author>Tsui, SKW</contributor.author>
<contributor.author>Waye, MMY</contributor.author>
<contributor.author>Lee, CY</contributor.author>
<contributor.author>Fung, KP</contributor.author>
<date.accessioned>2010-09-17T10:37:45Z</date.accessioned>
<date.available>2010-09-17T10:37:45Z</date.available>
<date.issued>2001</date.issued>
<identifier.citation>Journal Of Cellular Biochemistry, 2001, v. 82 n. 1, p. 1-10</identifier.citation>
<identifier.issn>0730-2312</identifier.issn>
<identifier.uri>http://hdl.handle.net/10722/92157</identifier.uri>
<description.abstract>We 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&#8242; 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. &#169; 2001 Wiley-Liss, Inc.</description.abstract>
<language>eng</language>
<publisher>John Wiley &amp; Sons, Inc. The Journal&apos;s web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/35503</publisher>
<relation.ispartof>Journal of Cellular Biochemistry</relation.ispartof>
<subject>FHL1</subject>
<subject>FHL1C</subject>
<subject>KyoT2</subject>
<subject>RBP-J</subject>
<subject>SLIM1</subject>
<subject>Zinc finger protein</subject>
<title>Characterization of tissue-specific LIM domain protein (FHL1C) which is an alternatively spliced isoform of a human LIM-only protein (FHL1)</title>
<type>Article</type>
<description.nature>Link_to_subscribed_fulltext</description.nature>
<identifier.doi>10.1002/jcb.1110</identifier.doi>
<identifier.pmid>11400158</identifier.pmid>
<identifier.scopus>eid_2-s2.0-0034994307</identifier.scopus>
<relation.references>http://www.scopus.com/mlt/select.url?eid=2-s2.0-0034994307&amp;selection=ref&amp;src=s&amp;origin=recordpage</relation.references>
<identifier.volume>82</identifier.volume>
<identifier.issue>1</identifier.issue>
<identifier.spage>1</identifier.spage>
<identifier.epage>10</identifier.epage>
<identifier.isi>WOS:000169049400001</identifier.isi>
<publisher.place>United States</publisher.place>
</item>
Author Affiliations
  1. Chinese University of Hong Kong