scholarly journals Disassembly of subplasmalemmal actin filament network and redistribution of adseverin during catecholamine release in the bovine chromaffin cell.

1993 ◽  
Vol 61 ◽  
pp. 293
Author(s):  
Takashi Sakurai ◽  
Etsuo Hashimoto ◽  
Seiji Nakamura ◽  
Konosuke Kumakura ◽  
Yoshiaki Nonomura
Keyword(s):  
Actin Filament ◽  
Chromaffin Cell ◽  
Catecholamine Release ◽  
Bovine Chromaffin Cell ◽  
Filament Network

scholarly journals Cortical filamentous actin disassembly and scinderin redistribution during chromaffin cell stimulation precede exocytosis, a phenomenon not exhibited by gelsolin.

1991 ◽  
Vol 113 (5) ◽  
pp. 1057-1067 ◽  
Author(s):  
M L Vitale ◽  
A Rodríguez Del Castillo ◽  
L Tchakarov ◽  
J M Trifaró
Keyword(s):  
Actin Filament ◽  
Chromaffin Cells ◽  
Chromaffin Cell ◽  
Catecholamine Secretion ◽  
Cortical Region ◽  
Cortical Surface ◽  
Filamentous Actin ◽  
Cell Stimulation ◽  
Rhodamine Phalloidin ◽  
Filament Networks

Immunofluorescence and cytochemical studies have demonstrated that filamentous actin is mainly localized in the cortical surface of the chromaffin cell. It has been suggested that these actin filament networks act as a barrier to the secretory granules, impeding their contact with the plasma membrane. Stimulation of chromaffin cells produces a disassembly of actin filament networks, implying the removal of the barrier. The presence of gelsolin and scinderin, two Ca(2+)-dependent actin filament severing proteins, in the cortical surface of the chromaffin cells, suggests the possibility that cell stimulation brings about activation of one or more actin filament severing proteins with the consequent disruption of actin networks. Therefore, biochemical studies and fluorescence microscopy experiments with scinderin and gelsolin antibodies and rhodamine-phalloidin, a probe for filamentous actin, were performed in cultured chromaffin cells to study the distribution of scinderin, gelsolin, and filamentous actin during cell stimulation and to correlate the possible changes with catecholamine secretion. Here we report that during nicotinic stimulation or K(+)-evoked depolarization, subcortical scinderin but not gelsolin is redistributed and that this redistribution precedes catecholamine secretion. The rearrangement of scinderin in patches is mediated by nicotinic receptors. Cell stimulation produces similar patterns of distribution of scinderin and filamentous actin. However, after the removal of the stimulus, the recovery of scinderin cortical pattern of distribution is faster than F-actin reassembly, suggesting that scinderin is bound in the cortical region of the cell to a component other than F-actin. We also demonstrate that peripheral actin filament disassembly and subplasmalemmal scinderin redistribution are calcium-dependent events. Moreover, experiments with an antibody against dopamine-beta-hydroxylase suggest that exocytosis sites are preferentially localized to areas of F-actin disassembly.

scholarly journals The actin filament network associated to Sertoli cell ectoplasmic specializations

BIOCELL ◽  
2011 ◽  
Vol 35 (3) ◽  
pp. 81-90 ◽  
Author(s):  
JUAN CARLOS CAVICCHIA ◽  
MABEL F覵COLO ◽  
JORGE IBA袳Z ◽  
CHRISTOPHER LILLIG ◽  
FRANCISCO CAPANI
Keyword(s):  
Sertoli Cell ◽  
Actin Filament ◽  
Filament Network

Short-Term Immunosuppression Enhances Long-Term Survival of Bovine Chromaffin Cell Xenografts in Rat Cns

1992 ◽  
Vol 1 (1) ◽  
pp. 33-41 ◽  
Author(s):  
John D. Ortega ◽  
Jacqueline Sagen ◽  
George D. Pappas
Keyword(s):  
Blood Brain Barrier ◽  
Chromaffin Cells ◽  
Chromaffin Cell ◽  
Short Term ◽  
Term Survival ◽  
Long Term Survival ◽  
Bovine Chromaffin Cell ◽  
Bovine Chromaffin Cells ◽  
Rat Cns

Xenogeneic donors, a largely untapped resource, would solve many of the problems associated with the limited availability of human donor tissue for neural transplantation. Previous work in our laboratory has revealed that xenografts of isolated bovine chromaffin cells survive transplantation into the periaqueductal gray (PAG) of immunosuppressed adult rats. Electron microscopic analysis reveals that graft sites contain healthy chromaffin cells, but do not contain host immune cells typical of graft rejection. The aim of the current study was to assess the necessary conditions for long-term survival of bovine chromaffin cell xenografts in the central nervous system (CNS). In particular, the need for short-course vs. permanent immunosuppressive therapy with cyclosporine A (CsA) for the long-term survival of grafted bovine chromaffin cells was addressed. Grafts from animals receiving continuous CsA treatment for either 3, 6, or 12 wk contained large clumps of dopamines-β-hydroxylase (DBH) positive cells in contrast to the few surviving cells observed in nonimmunosuppressed animals. In addition, grafts from animals that had CsA treatment terminated at 3 or 6 wk contained similarly large clumps of DBH-positive cells. Furthermore, short-term immunosuppression (3 wk) appeared to enhance the long-term survival of grafted cells, since clumps of DBH staining cells could still be positively identified in the host PAG at least 1 yr after transplantation. Complete rejection of graft tissue depends on several factors, such as blood–brain barrier integrity, the presence of major histocompatability complex (MHC) antigens in either the host or graft, and the status of the host immune system. By using a suspension of isolated bovine chromaffin cells, potential MHC antigen presenting cells, such as endothelial cells, are eliminated. In addition, CsA treatment may negate the immunologic consequences of increased blood–brain barrier permeability following surgical trauma by attenuating the host cell mediated response. In summary, long-term survival of isolated chromaffin cell xenografts in the rat CNS may be attained by a short-term course of CsA.

scholarly journals Modeling Mechanotransduction Signaling through Actin Filament Network Deformation Linked to Biochemical Response

2013 ◽  
Vol 104 (2) ◽  
pp. 317a-318a ◽  
Author(s):  
John Kang ◽  
Kathy M. Puskar ◽  
Russell S. Schwartz ◽  
Philip R. LeDuc
Keyword(s):  
Actin Filament ◽  
Biochemical Response ◽  
Filament Network

Involvement of the cortical actin filament network of neutrophil leucocytes during phagocytosis

1984 ◽  
Vol 12 (6) ◽  
pp. 983-987 ◽  
Author(s):  
PETER SHETERLINE ◽  
JANET E. RICKARD ◽  
R. CLIVE RICHARDS
Keyword(s):  
Actin Filament ◽  
Cortical Actin ◽  
Filament Network

scholarly journals A Myopathy-linked Desmin Mutation Perturbs Striated Muscle Actin Filament Architecture

2009 ◽  
Vol 20 (3) ◽  
pp. 834-845 ◽  
Author(s):  
Gloria M. Conover ◽  
Syerra N. Henderson ◽  
Carol C. Gregorio
Keyword(s):  
Actin Filament ◽  
Thin Filament ◽  
Striated Muscle ◽  
Solid Phase ◽  
Skeletal Muscle Atrophy ◽  
Binding Assays ◽  
Concomitant Increase ◽  
Solid Phase Binding ◽  
Intracellular Aggregates ◽  
Filament Network

Desmin interacts with nebulin establishing a direct link between the intermediate filament network and sarcomeres at the Z-discs. Here, we examined a desmin mutation, E245D, that is located within the coil IB (nebulin-binding) region of desmin and that has been reported to cause human cardiomyopathy and skeletal muscle atrophy. We show that the coil IB region of desmin binds to C-terminal nebulin (modules 160-164) with high affinity, whereas binding of this desmin region containing the E245D mutation appears to enhance its interaction with nebulin in solid-phase binding assays. Expression of the desmin-E245D mutant in myocytes displaces endogenous desmin and C-terminal nebulin from the Z-discs with a concomitant increase in the formation of intracellular aggregates, reminiscent of a major histological hallmark of desmin-related myopathies. Actin filament architecture was strikingly perturbed in myocytes expressing the desmin-E245D mutant because most sarcomeres contained elongated or shorter actin filaments. Our findings reveal a novel role for desmin intermediate filaments in modulating actin filament lengths and organization. Collectively, these data suggest that the desmin E245D mutation interferes with the ability of nebulin to precisely regulate thin filament lengths, providing new insights into the potential molecular consequences of expression of certain disease-associated desmin mutations.

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