Prinjha, Rabinder Kumar;
(1994)
Molecular cloning and sequence analysis of cDNAs encoding the transformation-sensitive actin cross-linking protein transgelin.
Doctoral thesis (Ph.D.), University College London (United Kingdom).
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Abstract
The central role of actin in crucial cellular activities including muscle contraction, locomotion, cytokinesis, maintenance of cell shape and movement of cell surface receptors has been widely studied. Controlled modulation of the actin cytoskeleton is mediated by an array of molecularly diverse actin associated proteins that variously regulate its polymerisation state, geometric organisation and interactions with other ligands. I have cloned cDNAs encoding the transformation-sensitive actin gelating higher molecular weight isoform of a 21kDa polypeptide doublet (protein C4) found uniformly distributed along stress fibres in normal mesenchymal cells. This isoform, designated transgelin, was found to be the product of a single gene, conserved at the nucleotide level in the H sapiens, R norvegicus, D melanogaster, and Aplysia genomes with a single strong band as far back as the fission yeast S pombe. Northern blotting identified a single mRNA that was abundantly expressed in smooth muscle tissues and cultured fibroblasts but was absent in skeletal muscle, thymus and liver tissues. SV40-transformation of 3T3 fibroblasts was found to down-regulate transgelin expression at the level of transcription or mRNA stability. The protein encoded by these cDNAs was found to be significantly related to a number of other proteins (C41, M Smith unpublished; NP25, unpublished EMBL M84725; chick calponin α and β, Takahashi & Nadal-Ginard 1991; and Drosophila mp20, Ayme-Southgate et al 1989) suggesting that they may be classified as members of a new transgelin multigene family.
Type: | Thesis (Doctoral) |
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Qualification: | Ph.D. |
Title: | Molecular cloning and sequence analysis of cDNAs encoding the transformation-sensitive actin cross-linking protein transgelin |
Open access status: | An open access version is available from UCL Discovery |
Language: | English |
Additional information: | Thesis digitised by ProQuest. |
Keywords: | (UMI)AAI10106590; Biological sciences |
URI: | https://discovery.ucl.ac.uk/id/eprint/10098739 |
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