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Molecular cloning and characterization of FHL2, a novel LIM domain protein preferentially expressed in human heart

A full-length cDNA clone encoding a novel LIM-only protein was isolated and sequenced from a human fetal heart cDNA library. This full-length clone consists of 1416 base pairs and has a predicted open reading frame (ORF) encoding 279 amino acids. The ORF of this polypeptide codes for the human heart...

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Bibliographic Details
Published in:Gene 1998-04, Vol.210 (2), p.345-350
Main Authors: Chan, Kwok Keung, Wing Tsui, Stephen Kwok, Lee, Simon Ming Yuen, Luk, Sharon Chui Wah, Liew, Choong Chin, Fung, Kwok Pui, Waye, Mary Miu Yee, Lee, Cheuk Yu
Format: Article
Language:English
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Summary:A full-length cDNA clone encoding a novel LIM-only protein was isolated and sequenced from a human fetal heart cDNA library. This full-length clone consists of 1416 base pairs and has a predicted open reading frame (ORF) encoding 279 amino acids. The ORF of this polypeptide codes for the human heart-specific f our and a h alf L IM-only protein 2 (FHL2). It possesses an extra zinc finger that is a half LIM domain and four repeats of LIM domain. When the human FHL2 cDNA probe was used to hybridize with poly-A RNA of various human tissues, a very strong signal could be seen in heart tissues, and only moderately low signals could be detected in placenta, skeletal muscle and ovary. Virtually no signal could be detected in brain, lung, liver, kidney, pancreas, spleen, thymus, prostate, testis, small intestine, colon or peripheral blood leukocyte. FHL2 was mapped to chromosome 2q12–q13 by fluorescent in-situ hybridization (FISH).
ISSN:0378-1119
1879-0038
DOI:10.1016/S0378-1119(97)00644-6