A tropomyosin 1 induced defect in cytokinesis can be rescued by elevated expression of cofilin.

Cytokinesis in eukaryotic cells is mediated by the contractile ring, an actomyosin-based structure which provides the force required to separate daughter cells. Isoforms of the actin-binding protein tropomyosin are also localised to the contractile ring in both fission yeast and human astrocytes. Although tropomyosin is required for cytokinesis in yeast, its precise role in the contractile ring is unknown.

Smooth muscle-specific alpha tropomyosin is a marker of fully differentiated smooth muscle in lung.

Tropomyosin (Tm) is one of the major components of smooth muscle. Currently it is impossible to easily distinguish the two major smooth muscle (sm) forms of Tm at a protein level by immunohistochemistry due to lack of specific antibodies. Alpha-sm Tm contains a unique 2a exon not found in any other Tm.

An immunoproteomic approach for identification of clinical biomarkers for monitoring disease: application to cystic fibrosis.

Circulating antibodies can be used to probe protein arrays of body fluids, prepared by two-dimensional gel electrophoresis, for antigenic biomarker detection. However, detected proteins, particularly low abundance antigens, often remain unidentifiable due to proteome complexity and limiting sample amounts. Using a novel enrichment approach exploiting patient antibodies for isolation of antigenic biomarkers, we demonstrate how immunoproteomic strategies can accelerate biomarker discovery.

Renal ischemia induces tropomyosin dissociation-destabilizing microvilli microfilaments.

Ischemic-induced cell injury results in rapid duration-dependent actin-depolymerizing factor (ADF)/cofilin-mediated disruption of the apical microvilli microfilament cores. Because intestinal microvillar microfilaments are bound and stabilized in the terminal web by the actin-binding protein tropomyosin, we questioned whether a protective effect of tropomyosin localization to the terminal web of the proximal tubule microfilament cores is disrupted during ischemic injury. With tropomyosin-specific antibodies, we examined rat cortical sections under physiological conditions and following ischemic injury by confocal microscopy.

Endogenous mitochondrial oxidative stress: neurodegeneration, proteomic analysis, specific respiratory chain defects, and efficacious antioxidant therapy in superoxide dismutase 2 null mice.

Oxidative stress and mitochondrial dysfunction have been linked to neurodegenerative disorders such as Parkinson's and Alzheimer's disease. However, it is not yet understood how endogenous mitochondrial oxidative stress may result in mitochondrial dysfunction. Most prior studies have tested oxidative stress paradigms in mitochondria through either chemical inhibition of specific components of the respiratory chain, or adding an exogenous insult such as hydrogen peroxide or paraquat to directly damage mitochondria.

Avian Purkinje neuronal cultures: extrinsic control of morphology by cell type and glutamate.

An in vitro coculture system is described to study the avian Purkinje neuron and the interactions occurring with astrocytes and granule cells during development in the cerebellum. Astrocytes initially and granule cells later regulate Purkinje neuron morphology. The coculture system presented here provides an excellent system for investigating the morphological, immunocytochemical, and electrophysiological differentiation of Purkinje neurons under controlled conditions and for studying cell-cell interactions and extrinsic factors, e.

Tropomyosin isoforms from the gamma gene differing at the C-terminus are spatially and developmentally regulated in the brain.

Tropomyosin is an actin-binding protein responsible for stabilizing the actin microfilament system in the cytoskeleton of nonmuscle cells and is involved in processes such as growth, differentiation, and polarity of neuronal cells. From the gamma gene, at least 11 different isoforms have been described, with three different C-terminal exons used (9a, 9c, 9d). The precise roles that the different isoforms play are unknown.

Specification of actin filament function and molecular composition by tropomyosin isoforms.

The specific functions of greater than 40 vertebrate nonmuscle tropomyosins (Tms) are poorly understood. In this article we have tested the ability of two Tm isoforms, TmBr3 and the human homologue of Tm5 (hTM5(NM1)), to regulate actin filament function. We found that these Tms can differentially alter actin filament organization, cell size, and shape.

High-molecular-weight tropomyosins localize to the contractile rings of dividing CNS cells but are absent from malignant pediatric and adult CNS tumors.

Tropomyosin has been implicated in the control of actin filament dynamics during cell migration, morphogenesis, and cytokinesis. In order to gain insight into the role of tropomyosins in cell division, we examined their expression in developing and neoplastic brain tissue. We found that the high-molecular-weight tropomyosins are downregulated at birth, which correlates with glial cell differentiation and withdrawal of most cells from the cell cycle.