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  PINCH2 is a new five LIM domain protein, homologous to PINCH and localized to focal adhesions

Braun, A., Bordoy, R., Stanchi, F., Moser, M., Kostka, G., Ehler, E., et al. (2003). PINCH2 is a new five LIM domain protein, homologous to PINCH and localized to focal adhesions. Experimental Cell Research, 284(2), 239-248.

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Genre: Journal Article
Alternative Title : Exp. Cell Res.

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 Creators:
Braun, A.1, Author              
Bordoy, R.1, Author              
Stanchi, F.1, Author              
Moser, M.1, Author              
Kostka, G.1, Author              
Ehler, E., Author
Brandau, O.2, Author              
Fässler, R.1, Author              
Affiliations:
1Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565147              
2Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565145              

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Free keywords: PINCH1; PINCH2; integrin-linked kinase (ILK); integrin; focal adhesion
 Abstract: PINCH is a five LIM domain protein involved in the regulation of integrin-mediated cell adhesion. It has been shown that PINCH interacts with integrin-linked kinase and Nck2. Here we describe a new isoform of PINCH, which we call PINCH2. Therefore, we rename PINCH to PINCH1. PINCH2 has an overall similarity of 92% to PINCH I and contains five LIM domains like PINCH I. While protein and gene structure of the PINCH homologues are very similar and well conserved during evolution, we observed differential expression pattern of the mRNAs. Based on northern hybridization of mouse embryo RNA, PINCH I is already detectable at E8.5. It is highly expressed during later stages of development and in all adult mouse tissues analyzed, with the highest levels in heart, lung, bladder, skin, and uterus. In contrast, significant PINCH2 expression starts at E14.5. In adult mice it is widely expressed, similar to PINCH I, but absent from spleen and thymus. In situ hybridization confirmed the Northern data and showed differential expression of PINCH1 and PINCH2 in embryonic intestine. Finally, we demonstrate that PINCH2 localizes to focal adhesions in NIH 3T3 cells and to Z-disks in primary rat cardiomyocytes. (C) 2003 Elsevier Science (USA). All rights reserved.

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Language(s): eng - English
 Dates: 2003-04-01
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41413
ISI: 000182000000007
 Degree: -

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Title: Experimental Cell Research
  Alternative Title : Exp. Cell Res.
Source Genre: Journal
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Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 284 (2) Sequence Number: - Start / End Page: 239 - 248 Identifier: ISSN: 0014-4827