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N Anilkumar

Publications and source records attributed to N Anilkumar.

3 recordsLinked to original sources

Fascins, and their roles in cell structure and function.

The fascins are a structurally unique and evolutionarily conserved group of actin cross-linking proteins. Fascins function in the organisation of two major forms of actin-based structures: dynamic, cortical cell protrusions and cytoplasmic microfilament bundles. The cortical structures, which include filopodia, spikes, lamellipodial ribs, oocyte microvilli and the dendrites of dendritic cells, have roles in cell-matrix adhesion, cell interactions and cell migration, whereas the cytoplasmic actin bundles appear to participate in cell architecture. We discuss the current understanding of the cellular mechanisms that regulate the binding of fascin to actin and how these processes contribute to the organisation or disassembly of cell protrusions. Although the in vivo roles of fascin have been studied principally in Drosophila, several human diseases are associated with inherited or acquired alterations in the expression of fascins. Strategies to modulate fascin-containing protrusions and thereby cell adhesive and migratory behaviour could have potential for therapeutic intervention in these conditions. The supplementary material referred to in this section can be found at http://www.interscience.wiley.com/jpages/0265-9247/suppmat/2002/v24.350.html

Actins↗

Modulation of alpha 5 beta 1 and alpha V beta 3 integrins on the cell surface during mitosis.

One of the hallmarks of cells undergoing mitotic division is their rounded morphology and reduced adhesion to the substratum. We have studied and compared the attachment of interphase and mitotic cells to substrata coated with fibronectin and vitronectin. We have found that adhesion of mitotic cells, as compared to interphase cells, is significantly reduced to fibronectin, but is higher to vitronectin. These results correlate well with the expression of alpha 5 beta 1 and alpha V beta 3 integrins, the respective receptors for fibronectin and vitronectin, on the cell surface. Mitotic cells show higher levels of alpha V beta 3 and very low levels of alpha 5 beta 1 proteins on the cell surface as compared to interphase cells. This difference in the levels of these integrins also reflects in the total amounts of fibronectin and vitronectin present on the cell surface of these cells. We have further shown, by flow cytometry, that binding of vitronectin, or the synthetic peptide -GRGDSP-, causes an increase in the intracellular levels of Ca2+ in mitotic cells, but no change is seen in the interphase cells. Binding of fibronectin to either of these cells fails to elicit any response. One interesting feature of our results is that the levels of total, i.e., cytoplasmic plus membrane bound, alpha 5 beta 1 and alpha V beta 3 integrins of mitotic and interphase cells remain the same, thus implying an alteration in the distribution of integrin chains between the plasma membrane and the cytoplasm during the conversion of interphase cells into the mitotic phase.

Animals↗

Isolation and characterization of laminin binding protein from regenerating rat liver plasma membrane.

Interaction of rat hepatocytes with laminin, the major basement membrane adhesive glycoprotein was studied. Rat fetal hepatocytes attached more to laminin than adult hepatocytes. Laminin promoted attachment of fetal hepatocytes in a concentration dependent manner and showed saturable binding pattern. Hepatocytes from CCl4 induced regenerating rat liver also attached more to laminin. The pentapeptide YIGSR derived from laminin promoted attachment of adult and fetal hepatocytes, but to a lesser extent. A 67 kDa protein was isolated from the hepatic plasma membrane of CCl4 induced regenerating rat liver by affinity chromatography over laminin sepharose. This protein appeared to be relatively abundant in regenerating liver than in normal liver. The radioiodinated 67 kDa protein could be inserted into liposomes and these liposomes attached to coverslips coated with laminin in a concentration dependent manner in a divalent cation free medium. Its specificity for laminin was also revealed by absence of significant binding to fibronectin and collagen.

Amino Acid Sequence↗