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Abstract
We have identified a novel transformation-sensitive mRNA, which is present in cultured fibroblasts but is lacking in SV40 transformed cells as well as in many mesenchymal tumor cell lines. The corresponding gene is located on human chromosome 8 in band 8q13. The open reading frame of the mRNA encodes a protein of 1119 amino acids forming two distinct domains. The N-terminal domain consists of 18 repeats that are related to the cytoskeletal protein ankyrin. The C-terminal domain contains six putative transmembrane segments that resemble many ion channels. This overall structure is reminiscent of TRP-like proteins that function as store-operated calcium channels. The novel protein with an Mr of 130 kDa is expressed at a very low level in human fibroblasts and at a moderate level in liposarcoma cells. Overexpression in eukaryotic cells appears to interfere with normal growth, suggesting that it might play a direct or indirect role in signal transduction and growth control.
Highlights
We have recently used this model system in combination with a subtractive cDNA cloning approach to identify novel transformation-sensitive proteins [4, 5]
Molecular Cloning of p120 —We have previously reported on the preparation of a subtracted cDNA library enriched for clones that are expressed by normal but not by SV40 transformed human fibroblasts [4, 5]
The clone was used as a probe to screen a commercial cDNA library prepared from human fibroblasts with the intention to isolate the full coding region for the novel ankyrin-like protein
Summary
We have recently used this model system in combination with a subtractive cDNA cloning approach to identify novel transformation-sensitive proteins [4, 5]. The clone was used as a probe to screen a commercial cDNA library prepared from human fibroblasts with the intention to isolate the full coding region for the novel ankyrin-like protein. On a blot containing RNA from different batches of human fibroblasts (WI38, IMR90), our cDNA clones hybridized to a single band of 4.6 kilobases (Fig. 3).
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