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Am J Physiol Cell Physiol (February 27, 2002). doi:10.1152/ajpcell.00442.2001
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Articles in PresS, published online ahead of print February 27, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00442.2001
Submitted on September 14, 2001
Accepted on February 18, 2002

TIMAP, a novel CAAX box protein regulated by TGF-ß1 and expressed in endothelial cells

Wangsen Cao1, Subhendra N Mattagajasingh2, Hangxue Xu1, Kwanghee Kim2, Wolfgang Fierlbeck2, Jie Deng1, Charles J Lowenstein1, and Barbara J Ballermann2*

1 Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA
2 Medicine, Albert Einstein College of Medicine, Bronx, New York, USA

* To whom correspondence should be addressed. E-mail: bjballer{at}aecom.yu.edu.

Representational difference analysis of the glomerular endothelial cell response to TGF-ß1 revealed a novel gene TIMAP (TGF-ß inhibited membrane associated protein), which contains 10 exons and maps to human chromosome 20.q11.22. By Northern blot, TIMAP mRNA is highly expressed in all cultured endothelial and hematopoietic cells. The frequency of the TIMAP SAGE tag is much greater in endothelial cell SAGE databases than in non-endothelial cells. Immunofluorescence studies of rat tissues shows that anti-TIMAP antibodies localize to vascular endothelium. TGF-ß1 represses TIMAP through a protein synthesis- and histone deacetylase-dependent process. The TIMAP protein contains five ankyrin repeats, a protein phosphatase-1 interacting domain and a C-terminal CAAX box, a domain arrangement like that of MYPT3, a protein phosphatase 1 inhibitor. A GFP-TIMAP fusion protein localized to the plasma membrane in a CAAX box dependent fashion. Hence, TIMAP is a novel gene highly expressed in endothelial and hematopoietic cells, and regulated by TGF-ß1. Based on its domain structure, TIMAP may serve a signaling function, potentially through interaction with protein phosphatase 1.




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