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

scholarly journals Filamin A Is a Regulator of Blood-Testis Barrier Assembly during Postnatal Development in the Rat Testis

Endocrinology ◽  
2012 ◽  
Vol 153 (10) ◽  
pp. 5023-5035 ◽  
Author(s):  
Wenhui Su ◽  
Dolores D. Mruk ◽  
Pearl P. Y. Lie ◽  
Wing-yee Lui ◽  
C. Yan Cheng
Keyword(s):  
Postnatal Development ◽  
Sertoli Cell ◽  
Actin Filament ◽  
Permeability Barrier ◽  
Filamin A ◽  
Rat Testis ◽  
Filament Network ◽  
Blood Testis Barrier

Abstract The blood-testis barrier (BTB) is an important ultrastructure in the testis. A delay in its assembly during postnatal development leads to meiotic arrest. Also, a disruption of the BTB by toxicants in adult rats leads to a failure in spermatogonial differentiation. However, the regulation of BTB assembly remains unknown. Herein, filamin A, an actin filament cross-linker that is known to maintain and regulate cytoskeleton structure and function in other epithelia, was shown to be highly expressed during the assembly of Sertoli cell BTB in vitro and postnatal development of BTB in vivo, perhaps being used to maintain the actin filament network at the BTB. A knockdown of filamin A by RNA interference was found to partially perturb the Sertoli cell tight junction (TJ) permeability barrier both in vitro and in vivo. Interestingly, this down-regulating effect on the TJ barrier function after the knockdown of filamin A was associated with a mis-localization of both TJ and basal ectoplasmic specialization proteins. Filamin A knockdown also induced a disorganization of the actin filament network in Sertoli cells in vitro and in vivo. Collectively, these findings illustrate that filamin A regulates BTB assembly by recruiting these proteins to the microenvironment in the seminiferous epithelium to serve as the building blocks. In short, filamin A participates in BTB assembly by regulating protein recruitment during postnatal development in the rat testis.

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.

scholarly journals Response of an actin filament network model under cyclic stretching through a coarse grained Monte Carlo approach

2011 ◽  
Vol 274 (1) ◽  
pp. 109-119 ◽  
Author(s):  
John Kang ◽  
Robert L. Steward ◽  
YongTae Kim ◽  
Russell S. Schwartz ◽  
Philip R. LeDuc ◽  
...  
Keyword(s):  
Monte Carlo ◽  
Network Model ◽  
Actin Filament ◽  
Coarse Grained ◽  
Monte Carlo Approach ◽  
Cyclic Stretching ◽  
Filament Network

scholarly journals Regulation of spermiogenesis, spermiation and blood–testis barrier dynamics: novel insights from studies on Eps8 and Arp3

2011 ◽  
Vol 435 (3) ◽  
pp. 553-562 ◽  
Author(s):  
C. Yan Cheng ◽  
Dolores D. Mruk
Keyword(s):  
Sertoli Cell ◽  
Morphological Changes ◽  
Growth Factor Receptor ◽  
Adhesion Protein ◽  
Apical Compartment ◽  
Epidermal Growth ◽  
Actin Regulatory Proteins ◽  
Filament Network ◽  
Ectoplasmic Specialization ◽  
Blood Testis Barrier

Spermiogenesis in the mammalian testis is the most critical post-meiotic developmental event occurring during spermatogenesis in which haploid spermatids undergo extensive cellular, molecular and morphological changes to form spermatozoa. Spermatozoa are then released from the seminiferous epithelium at spermiation. At the same time, the BTB (blood–testis barrier) undergoes restructuring to facilitate the transit of preleptotene spermatocytes from the basal to the apical compartment. Thus meiotic divisions take place behind the BTB in the apical compartment to form spermatids. These germ cells enter spermiogenesis to transform into elongating spermatids and then into spermatozoa to replace those that were released in the previous cycle. However, the mole-cular regulators that control spermiogenesis, in particular the dynamic changes that occur at the Sertoli cell–spermatid interface and at the BTB, are not entirely known. This is largely due to the lack of suitable animal models which can be used to study these events. During the course of our investigation to develop adjudin [1-(2,4-dichlorobenzyl)-1H-indazole-3-carbohydrazide] as a potential male contraceptive, this drug was shown to ‘accelerate’ spermiation by inducing the release of premature spermatids from the epithelium. Using this model, we have identified several molecules that are crucial in regulating the actin filament network and the unique adhesion protein complex at the Sertoli cell–spermatid interface known as the apical ES (ectoplasmic specialization). In the present review, we critically evaluate these and other findings in the literature as they relate to the restricted temporal and spatial expression of two actin regulatory proteins, namely Eps8 (epidermal growth factor receptor pathway substrate 8) and Arp3 (actin-related protein 3), which regulate these events.

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