A5020828897- Ion Transport and Channel Regulation
- ATP Synthase and ATPases Research
- RNA Research and Splicing
- Muscle Physiology and Disorders
- MicroRNA in disease regulation
- Advanced Fluorescence Microscopy Techniques
- Neonatal Respiratory Health Research
- 14-3-3 protein interactions
- Ion channel regulation and function
- Cell Image Analysis Techniques
- Advanced Electron Microscopy Techniques and Applications
- Photoreceptor and optogenetics research
- Exercise and Physiological Responses
- Glycosylation and Glycoproteins Research
- Connexins and lens biology
- Sarcoma Diagnosis and Treatment
- Genetic Neurodegenerative Diseases
- Heme Oxygenase-1 and Carbon Monoxide
- Adipose Tissue and Metabolism
- Bone Metabolism and Diseases
- Galectins and Cancer Biology
- Mitochondrial Function and Pathology
- Electrolyte and hormonal disorders
- Escherichia coli research studies
- Biofield Effects and Biophysics
University of Bari Aldo Moro
1995-2022
Harvard University
2020
Brigham and Women's Hospital
2020
Rockefeller University
2020
Federation of American Societies for Experimental Biology
2020
National Institutes of Health
2020
Yale University
2020
Regulation of water homeostasis is a central feature nervous system pathophysiology. In this context, several lines evidence suggest crucial role for the channel aquaporin-4 (AQP4) and its plasma membrane supramolecular organization as key element. Here, we demonstrate expression in tissues additional isoforms AQP4 characterized by C-terminal extension generated programmed translational readthrough. These extended (AQP4ex) display perivascular polarization dystrophin-dependent pools. AQP4ex...
Abstract The glial water channel protein aquaporin-4 (AQP4) forms heterotetramers in the plasma membrane made of M23-AQP4 and M1-AQP4 isoforms. isoform ratio controls AQP4 aggregation into supramolecular structures called orthogonal arrays particles (AQP4-OAP). role OAP malignant gliomas is still unclear. In this study, we demonstrate that aggregation/disaggregation influences biology glioma cells. Selective expression OAP-forming (AQP4-OAP) triggered cell shape changes cells associated with...
Astrocytes are non-neuronal cells that govern the homeostatic regulation of brain through ions and water transport, Ca
Two major isoforms of aquaporin-4 (AQP4) have been described in human tissue. Here we report the identification and functional analysis an alternatively spliced transcript AQP4, AQP4-Δ4, that lacks exon 4. In transfected cells AQP4-Δ4 is mainly retained endoplasmic reticulum shows no water transport properties. When into stably expressing surface expression full-length protein reduced. Furthermore, activity cotransfectants diminished comparison to transfectants only AQP4. The observed...
Abstract Astrocyte endfeet are endowed with aquaporin‐4 (AQP4)‐based assemblies called orthogonal arrays of particles (OAPs) whose function is still unclear. To investigate the OAPs and AQP4 tetramers, we have generated a novel “OAP‐null” mouse model selectively lacking OAP forming M23‐AQP4 isoform. We demonstrated that transcript levels were not reduced by using qPCR. Blue native (BN)/SDS‐PAGE Western blot performed on OAP‐null brain primary astrocyte cultures showed complete depletion...
Astrocyte proliferation and migration toward injured Central Nervous System (CNS) areas are key features of astrogliosis glial scar formation. Even though it is known that intracellular environmental Reactive Oxygen Nitrogen Species (RONS) affect astrocyte behaviour in physiological pathophysiological conditions, their effects on the growth astrocytes still unclear. Plasma-technologies emerging medicine as a tool to generate RONS for treating cells directly or through Plasma Activated Liquid...
Abstract In astrocytes, unknown mechanisms regulate the expression of M1 and M23 isoforms water channel aquaporin‐4 (M1‐AQP4 M23‐AQP4). The ratio between these two controls AQP4 assembly state in plasma membrane known as orthogonal arrays particles (OAPs). To give new insights into mechanisms, here, we explore regulation spinal cord a CRISPR/Cas9 M23‐null mouse model (M23‐null). OAP assembly, perivascular localization M1‐AQP4 protein were drastically reduced. heterozygous, was proportionally...
The CNS plasma-membrane water channel aquaporin-4 (AQP4) is expressed as two major isoforms able to aggregate into supramolecular assemblies known 'orthogonal arrays of particles' (OAPs). OAP subnanometric features are largely unknown mainly because a method for the expression, isolation, and crystallization integral human OAPs has not been developed. Here, OAP-forming isoform M23-AQP4 was in insect mammalian cell lines AQP4 evaluated. Native size exclusion chromatography employed isolate...
<div>Abstract<p>The glial water channel protein aquaporin-4 (AQP4) forms heterotetramers in the plasma membrane made of M23-AQP4 and M1-AQP4 isoforms. The isoform ratio controls AQP4 aggregation into supramolecular structures called orthogonal arrays particles (AQP4-OAP). role OAP malignant gliomas is still unclear. In this study, we demonstrate that aggregation/disaggregation influences biology glioma cells. Selective expression OAP-forming (AQP4-OAP) triggered cell shape...
<p>Supplementary Figure s1. M23-AQP4 C-terminus analysis for the ability to induce morphological changes in glioma cells. a) Schematic representation of untagged and mCherry-tagged isoforms used (b). b) Immuno fluorescence U87 U251 cells transfected with tagged isoforms. AQP4 (red) Phallodin (green) visualize F-actin. No were induced by when mCherry was used. Scale bar 50 µm. c) Quantification alterations observed experiments described (a). The histobar shows percentage altered...
<p>Supplementary Figure s1. M23-AQP4 C-terminus analysis for the ability to induce morphological changes in glioma cells. a) Schematic representation of untagged and mCherry-tagged isoforms used (b). b) Immuno fluorescence U87 U251 cells transfected with tagged isoforms. AQP4 (red) Phallodin (green) visualize F-actin. No were induced by when mCherry was used. Scale bar 50 µm. c) Quantification alterations observed experiments described (a). The histobar shows percentage altered...
<div>Abstract<p>The glial water channel protein aquaporin-4 (AQP4) forms heterotetramers in the plasma membrane made of M23-AQP4 and M1-AQP4 isoforms. The isoform ratio controls AQP4 aggregation into supramolecular structures called orthogonal arrays particles (AQP4-OAP). role OAP malignant gliomas is still unclear. In this study, we demonstrate that aggregation/disaggregation influences biology glioma cells. Selective expression OAP-forming (AQP4-OAP) triggered cell shape...