Plastins: Versatile modulators of actin organization in (patho)physiological cellular processes

Department of Medical Protein Research, Flanders Interuniversity Institute for Biotechnology (VIB), Ghent University, Faculty of Medicine and Health Sciences, Albert Baertsoenkaai 3, B-9000 Ghent, Belgium.
Acta Pharmacologica Sinica (Impact Factor: 2.91). 08/2005; 26(7):769-79. DOI: 10.1111/j.1745-7254.2005.00145.x
Source: PubMed


Many actin-binding proteins are expressed in eukaryotic cells. These polypeptides assist in stabilizing and rearranging the organization of the actin cytoskeleton in response to external stimuli, or during cell migration and adhesion. Here we review a particular set of actin-binding proteins called plastins. Plastins (also called fimbrins) belong to a subclass of actin-binding proteins known as actin bundling proteins. Three isoforms have been characterized in mammals: T-plastin is expressed in cells from solid tissue, whereas L-plastin occurs predominantly in hematopoietic cells. The third isoform, I-plastin, is specifically expressed in the small intestine, colon and kidney. These proteins share the unique property of cross-linking actin filaments into tight bundles. Although plastins are primarily involved in regulation of the actin cytoskeleton, they possess some unique features. For instance, they are implicated in invasion by pathogenic bacteria such as Shigella flexneri and Salmonella typhimurium. Also, L-plastin plays an important role in leukocyte function. T-plastin, on the other hand, is possibly involved in DNA repair. Finally, both T- and L-plastin are implicated in several diseases, and L-plastin is considered to be a valuable marker for cancer.

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    • "The results showed that a high level of L-plastin expression was identified in RMCCA1 cells cultured in matrix gel (Fig. 2B). A previous study demonstrated that L-plastin localizes to actin-rich membrane structures involved in locomotion, adhesion and immune defense, thereby implying that L-plastin is involved in the organization of the actin cytoskeleton (17). In addition, L-plastin has also been detected in solid tumors of epithelial and mesenchymal origin and has been suggested to be involved in cancer cell invasion (18). "
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    ABSTRACT: The function of the extracellular matrix (ECM) in the tumor microenvironment is not limited to forming a barrier against tumor invasion. As demonstrated in pathological specimens, cholangiocarcinoma samples exhibit an enrichment of the ECM surrounding the tumor cells. In this study, we examined involvement of the ECM in the regulation of the invasiveness of cholangiocarcinoma cells. The RMCCA1 cholangiocarcinoma cell line was cultured in culture plates either with or without a coating of reconstituted ECM basement membrane preparation (BD Matrigel matrix). In vitro invasion assays were then performed. In addition, the protein expression profile of the cell line was examined using two-dimensional gel electrophoresis and liquid chromatography-tandem mass spectrometry. The proteins expressed and their functional associations with cancer progression were determined. Culturing the RMCCA1 cell line in the BD Matrigel matrix induced cell invasion. Numerous proteins were induced by culturing the RMCCA1 cells in the matrix gel. The expression of L-plastin, an actin-binding protein, was significantly upregulated. The knockdown of L-plastin expression by siRNA silencing significantly suppressed the cellular response to matrix gel-stimulated cancer cell invasion. The ECM promotes the invasiveness of cholangiocarcinoma cells by upregulating L-plastin. These findings suggest the potential exploitation of this mechanism as a means of inhibiting the invasiveness of cholangiocarcinoma cells.
    Oncology letters 09/2014; 8(3):993-1000. DOI:10.3892/ol.2014.2239 · 1.55 Impact Factor
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    • "The Plastin3 gene is not repressed during this transformation and therefore can be used to identify those CTCs that are in transition. Plastin3 (PLS3) is located on chromosome Xq23 and functions to polymerize actin fibers38. Yokobori et al showed that patients with PLS3-positive CTCs in peripheral blood had significantly shorter disease-free survival than PLS3-negative patients. "
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    Journal of Cancer 03/2014; 5(4):272-280. DOI:10.7150/jca.8871 · 3.27 Impact Factor
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    • "Plastins are a family of actin-binding proteins that cross-link actin filaments into tight bundles facilitating the actin filament turn-over [21]. T-plastin is present during the early stages of the intestinal epithelia cell differentiation and is essential for the formation and expression of the microvilli [21]. Furthermore, it has been shown that T-plastin is involved in the cytoskeletal rearrangement during infections with intestinal bacteria stimulating cell rounding and increasing of the length and density of microvilli among other effects [22] [23]. "
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    ABSTRACT: Echinostoma caproni (Trematoda: Echinostomatidae) is an intestinal trematode that has been used as experimental model to investigate the factors determining the expulsion of intestinal helminths. We analyze the changes in the protein expression and glycosylation induced by E. caproni in Wistar rat, a host of low compatibility in which the parasites are rapidly rejected. To determine the changes in protein expression, two-dimensional difference gel electrophoresis was employed using protein extracts from the intestine of naïve and infected rats. The patterns of glycosylation were analyzed by lectin blotting. Those spots showing differential expression or glycosylation were analyzed by mass spectrometry. A total of 33 protein spots differentially expressed were identified (26 were found to be over-expressed and 7 down-regulated). Moreover, E. caproni induced changes in the glycosylation status of 8 proteins that were successfully identified. Most of these proteins were related to the cytoskeleton and the maintenance of the functional integrity of the ileal epithelium. This suggests that the regeneration of the intestinal tissue is a major effector mechanism responsible for the early expulsion of this helminth. Furthermore, several proteins involved in the energy metabolism were also altered in the ileum of rats as a consequence of the E. caproni infection. Our analysis provides essential new insights in the factors determining the natural expulsion of intestinal parasitic helminths from their hosts. The results obtained contribute to a better understanding of the effective mechanisms involved in the defense against the intestinal helminths. The identification of proteins in the intestine that become modified in their expression or glycosylation in hosts in which the parasite are rapidly rejected may serve for the development of tool for the control of these infections.
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