Expression of Dystrophins and the Dystrophin-Associated-Protein Complex by Pituicytes in Culture

Bougrid, Abdelkader; Claudepierre, Thomas; Picaud, Serge; Ayad, G.; Mornet, Dominique; Dorbani-Mamine, Latifa; Rendón, Álvaro; Darbei͏̈da, Halima

doi:10.1007/s11064-011-0466-6

Cited by 4 publications

(3 citation statements)

References 59 publications

(62 reference statements)

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“…AVP and OXT have the ability to reverse the stellation of pituicytes and return them to their original shape by activating Cdc42, another small GTPase that reorganizes the actin cytoskeleton in a cortical position ( 65 – 67 ). The complex of dystrophins and dystrophin-associated-protein expressed on pituicytes interacts with laminin and the extracellular matrix, which may play a role in the retraction and reinsertion of the cellular processes of pituicytes during neuro-glial reorganization ( 68 ).…”

Section: Activity-dependent Neuro-glial Reorganizationmentioning

confidence: 99%

Advances in Understanding of Structural Reorganization in the Hypothalamic Neurosecretory System

Miyata

2017

Front. Endocrinol.

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The hypothalamic neurosecretory system synthesizes neuropeptides in hypothalamic nuclei and releases them from axonal terminals into the circulation in the neurohypophysis (NH) and median eminence (ME). This system plays a crucial role in regulating body fluid homeostasis and social behaviors as well as reproduction, growth, metabolism, and stress responses, and activity-dependent structural reorganization has been reported. Current knowledge on dynamic structural reorganization in the NH and ME, in which the axonal terminals of neurosecretory neurons directly contact the basement membrane (BM) of a fenestrated vasculature, is discussed herein. Glial cells, pituicytes in the NH and tanycytes in the ME, engulf axonal terminals and interpose their cellular processes between axonal terminals and the BM when hormonal demands are low. Increasing demands for neurosecretion result in the retraction of the cellular processes of glial cells from axonal terminals and the BM, permitting increased neurovascular contact. The shape conversion of pituicytes and tanycytes is mediated by neurotransmitters and sex steroid hormones, respectively. The NH and ME have a rough vascular BM profile of wide perivascular spaces and specialized extension structures called "perivascular protrusions." Perivascular protrusions, the insides of which are occupied by the cellular processes of vascular mural cells pericytes, contribute to increasing neurovascular contact and, thus, the efficient diffusion of hypothalamic neuropeptides. A chronic physiological stimulation has been shown to increase perivascular protrusions via the shape conversion of pericytes and the profile of the vascular surface. Continuous angiogenesis occurs in the NH and ME of healthy normal adult rodents depending on the signaling of vascular endothelial growth factor (VEGF). The inhibition of VEGF signaling suppresses the proliferation of endothelial cells (ECs) and promotes their apoptosis, which results in decreases in the population of ECs and axonal terminals. Pituicytes and tanycytes are continuously replaced by the proliferation and differentiation of stem/progenitor cells, which may be regulated by matching those of ECs and axonal terminals. In conclusion, structural reorganization in the NH and ME is caused by the activity-dependent shape conversion of glial cells and vascular mural cells as well as the proliferation of endothelial and glial cells by angiogenesis and gliogenesis, respectively.

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Section: Activity-dependent Neuro-glial Reorganizationmentioning

confidence: 99%

Advances in Understanding of Structural Reorganization in the Hypothalamic Neurosecretory System

Miyata

2017

Front. Endocrinol.

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“…On the other hand, Dp71 was found together with β-dystroglycan, α-syntrophin, and neuronal nitric oxide synthase (nNOS) in the membrane of mouse spermatozoa, in which Dp71 appears to be critical for proper localization of α-syntrophin, nNOS, the voltagedependent sodium ion (Na + ) and potassium ion (K + ) channels and, ultimately, for flagellar morphology [50]. Furthermore, Dp71f and several members of the DAPC including dystroglycans, δ-, γ-sarcoglycans, α-dystrobrevin-1, and α-1syntrophin are expressed in pituicytes, resident glia of the neurohypophyses, implying the formation of a DAPClike complex in these particular cells [51]. Likewise, expression of Dp71d and mRNAs for β-dystroglycan, α-and β-dystrobrevins, and α-, βI-, βII-, and γII-syntrophins was found in both visceral and subcutaneous rat adipose depots, suggesting a role for this complex in adipose biology [52].…”

Section: Formation and Distribution Of The Dp71-containing Dystrophinmentioning

confidence: 99%

Dystrophin Dp71: The Smallest but Multifunctional Product of the Duchenne Muscular Dystrophy Gene

et al. 2011

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Dystrophin Dp71 is expressed in all tissues, with the exception of skeletal muscle, and is the main Duchenne muscular dystrophy (DMD) gene product in brain. As full-length dystrophin does in skeletal muscle, Dp71 associates with dystroglycans, sarcoglycans, dystrobrevins, syntrophins, and accessory proteins to form the dystrophin-associated protein complex (DAPC) in non-muscle tissues. Although it has been nearly 20 years since the discovery of Dp71, its study has become relevant only recently due to its direct involvement with the two main DMD non-muscular phenotypes: cognitive impairment and abnormal retinal physiology. In this review, we describe the historical background of Dp71 and the experimental models developed for its study. Additionally, we present and discuss the experimental evidence supporting the participation of Dp71 in different cellular processes, including cell adhesion, water homeostasis, cell division, and nuclear architecture. The functional diversity of Dp71 is attributed to the formation of Dp71-containing DAPC in numerous cell types and different subcellular compartments, including in plasma membrane and nucleus, as well as to the capability of Dp71-containing DAPC to work as the scaffold for proper clustering and anchoring of structural and signaling proteins to the plasma membrane and of nuclear envelope proteins to the inner nuclear membrane.

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“…Transfected PC12 Tet-ON and PC12 cells were immunostained as previously described (Aragon et al 2011) using the anti-cMyc antibody for recombinant Myc-Dp71 proteins and counterstained with JAF (to β-dystroglycan) or C4 (to α1-syntrophin) antibodies (Bougrid et al 2011). Alexa Fluor 488-(catalog number: A21202; Invitrogen) and Alexa Fluor 594-conjugated (catalog number: A21207; Invitrogen) secondary antibodies were used to detect the primary antibody signal.…”

Section: Immunofluorescence Assaysmentioning

confidence: 99%

Identification of Dp71 Isoforms Expressed in PC12 Cells: Subcellular Localization and Colocalization with β-Dystroglycan and α1-Syntrophin

et al. 2015

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Several dystrophin Dp71 messenger RNA (mRNA) alternative splice variants have been described. According to the splicing of exon 78 or intron 77, Dp71 proteins are grouped as Dp71d, Dp71f, and Dp71e, and each group has a specific C-terminal end. In this study, we explored the expression of Dp71 isoforms at the complementary DNA (cDNA) level and the subcellular localization of recombinant Myc-Dp71 proteins in PC12 cells. We determined that PC12 cells express Dp71a, Dp71c, Dp71ab, Dp71e, and Dp71ec mRNA splice variants. In undifferentiated and nerve growth factor-differentiated PC12 Tet-ON cells, Dp71a, Dp71ab, and Dp71e were found to localize and colocalize with β-dystroglycan and α1-syntrophin in the periphery/cytoplasm, while Dp71c and Dp71ec were mainly localized in the cell periphery and showed less colocalization with β-dystroglycan and α1-syntrophin. The levels of Dp71a, Dp71e, and Dp71ec were increased in the nucleus of differentiated PC12 Tet-ON cells compared to undifferentiated cells. Dp71 isoforms were also localized in neurite extensions and growth cones.

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Expression of Dystrophins and the Dystrophin-Associated-Protein Complex by Pituicytes in Culture

Cited by 4 publications

References 59 publications

Advances in Understanding of Structural Reorganization in the Hypothalamic Neurosecretory System

Advances in Understanding of Structural Reorganization in the Hypothalamic Neurosecretory System

Dystrophin Dp71: The Smallest but Multifunctional Product of the Duchenne Muscular Dystrophy Gene

Identification of Dp71 Isoforms Expressed in PC12 Cells: Subcellular Localization and Colocalization with β-Dystroglycan and α1-Syntrophin

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