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Electron Microscopy in Molecules Analysis
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Electron Microscopy in Molecules Analysis

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Analytical Chemistry".

Deadline for manuscript submissions: closed (31 May 2022) | Viewed by 9773

Special Issue Editor

Prof. Dr. Paola Lenzi

E-Mail Website
Guest Editor
Department of Translational Research and, New Technologies in Medicine and Surgery, Human Anatomy, Università di Pisa, Pisa, Italy
Interests: autophagy; ubiquitin proteasome pathway; transmission electron microscopy; mitochondria; cellular ultrastructure; neurodegeneration; brain tumor; drug abuse

Special Issue Information

Dear Colleagues,

Transmission electron microscopy provides detailed morphological and quantitative information of specific molecules within cells as well as information on the chemical composition of different cellular structures. In particular, molecules belonging to different cell pathways can be evaluated in situ using an immunological approach that takes advantage of immunogold particles. This Special Issue will cover various outcomes of imaging molecules at the ultrastructural level. It is expected that authors contribute with original papers and reviews dealing with the physiological and pathological roles of molecules stoichiometrically identified in cells using immunogold. The Special Issue is expected to collect studies performed in different organs and systems along with different animal species and may include in vitro studies. This Special Issue should contain contributions discussing all the aspects broadly indicated by the keywords.

Prof. Dr. Paola Lenzi
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • immune cytochemistry
  • ultrastructural morphometry
  • autophagy
  • ubiquitin proteasome pathway
  • mitochondria

Published Papers (5 papers)

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Research

15 pages, 57969 KiB  
Article
Connexin Expression in Human Minor Salivary Glands: An Immunohistochemical Microscopy Study
by Alessandra Falleni, Stefania Moscato, Giovanni Fulvio, Enza Polizzi, Margherita Bernardeschi, Francesco Bianchi, Valentina Donati, Manuela Cabiati, Chiara Ippolito, Silvia Del Ry, Chiara Baldini and Letizia Mattii
Molecules 2022, 27(18), 5926; https://doi.org/10.3390/molecules27185926 - 12 Sep 2022
Viewed by 1137
Abstract
Connexins (Cxs) are transmembrane proteins involved in the formation of hemichannels and gap junctions (GJs). GJs are involved in various physiological functions, including secretion in glandular tissue. It has been demonstrated that Cx26, Cx32, and Cx43 are mainly expressed in glands, but no [...] Read more.
Connexins (Cxs) are transmembrane proteins involved in the formation of hemichannels and gap junctions (GJs). GJs are involved in various physiological functions, including secretion in glandular tissue. It has been demonstrated that Cx26, Cx32, and Cx43 are mainly expressed in glands, but no data are available in human salivary glands to date. The aim of our study was to investigate the presence and the localization of Cxs in human minor labial salivary glands. Immunofluorescence and immunoelectron microscopy were employed to evaluate the Cx26, Cx32, and Cx43 protein in human labial salivary gland biopsies (hLSGBs). RT-PCR was also used to detect their mRNA expression. Cx expression was found at both the mRNA and protein levels in all hLSGBs analysed. Cxs were observed at the level of the duct and acinar cells, as well as in myoepithelial cells. The localization of the three Cx types was very similar, suggesting colocalization of these Cxs in the same connexons. These results demonstrated the presence of Cxs in human salivary glands for the first time. Moreover, the few samples with primary Sjögren’s Syndrome analysed only by immunofluorescence showed an alteration of the Cx expression, indicating that these proteins could be involved in salivary gland dysfunctions. Full article
(This article belongs to the Special Issue Electron Microscopy in Molecules Analysis)
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28 pages, 7608 KiB  
Article
Within the Ischemic Penumbra, Sub-Cellular Compartmentalization of Heat Shock Protein 70 Overlaps with Autophagy Proteins and Fails to Merge with Lysosomes
by Federica Mastroiacovo, Francesca Biagioni, Paola Lenzi, Gloria Lazzeri, Michela Ferrucci, Stefano Puglisi-Allegra, Alessandro Frati, Ferdinando Nicoletti and Francesco Fornai
Molecules 2022, 27(10), 3122; https://doi.org/10.3390/molecules27103122 - 13 May 2022
Cited by 1 | Viewed by 1887
Abstract
The brain area which surrounds the frankly ischemic region is named the area penumbra. In this area, most cells are spared although their oxidative metabolism is impaired. area penumbra is routinely detected by immunostaining of a molecule named Heat Shock Protein 70 [...] Read more.
The brain area which surrounds the frankly ischemic region is named the area penumbra. In this area, most cells are spared although their oxidative metabolism is impaired. area penumbra is routinely detected by immunostaining of a molecule named Heat Shock Protein 70 (HSP70). Within the area penumbra, autophagy-related proteins also increase. Therefore, in the present study, the autophagy-related microtubule-associated protein I/II-Light Chain 3 (LC3) was investigated within the area penumbra along with HSP70. In C57 black mice, ischemia was induced by permanent occlusion of the distal part of the middle cerebral artery. Immunofluorescence and electron microscopy show that LC3 and HSP70 are overexpressed and co-localize within the area penumbra in the same cells and within similar subcellular compartments. In the area penumbra, marked loss of co-localization of HSP70 and LC3-positive autophagy vacuoles, with lysosomal-associated membrane protein 1 (LAMP1) or cathepsin-D-positive lysosome vacuoles occurs. This study indicates that, within the area penumbra, a failure of autophagolysosomes depends on defective compartmentalization of LC3, LAMP1 and cathepsin-D and a defect in merging between autophagosomes and lysosomes. Such a deleterious effect is likely to induce a depletion of autophagolysosomes and cell clearing systems, which needs to be rescued in the process of improving neuronal survival. Full article
(This article belongs to the Special Issue Electron Microscopy in Molecules Analysis)
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13 pages, 4249 KiB  
Article
Subcellular Localization of Connexin 26 in Cardiomyocytes and in Cardiomyocyte-Derived Extracellular Vesicles
by Alessandra Falleni, Stefania Moscato, Antonietta R. M. Sabbatini, Margherita Bernardeschi, Francesco Bianchi, Antonella Cecchettini and Letizia Mattii
Molecules 2021, 26(21), 6726; https://doi.org/10.3390/molecules26216726 - 06 Nov 2021
Cited by 5 | Viewed by 1878
Abstract
Connexins (Cxs) are a family of membrane-spanning proteins, expressed in vertebrates and named according to their molecular weight. They are involved in tissue homeostasis, and they function by acting at several communication levels. Cardiac Cxs are responsible for regular heart function and, among [...] Read more.
Connexins (Cxs) are a family of membrane-spanning proteins, expressed in vertebrates and named according to their molecular weight. They are involved in tissue homeostasis, and they function by acting at several communication levels. Cardiac Cxs are responsible for regular heart function and, among them, Cx26 and Cx43 are widely expressed throughout the heart. Cx26 is present in vessels, as well as in cardiomyocytes, and its localization is scattered all over the cell aside from at the intercalated discs as is the case for the other cardiac Cxs. However, having been found in cardiomyocytes only recently, both its subcellular localization and its functional characterization in cardiomyocytes remain poorly understood. Therefore, in this study we aimed to obtain further data on the localization of Cx26 at the subcellular level. Our TEM immunogold analyses were performed on rat heart ventricles and differentiated H9c2 cardiac cell sections as well as on differentiated H9c2 derived extracellular vesicles. The results confirmed the absence of Cx26 at intercalated discs and showed the presence of Cx26 at the level of different subcellular compartments. The peculiar localization at the level of extracellular vesicles suggested a specific role for cardiac Cx26 in inter-cellular communication in an independent gap junction manner. Full article
(This article belongs to the Special Issue Electron Microscopy in Molecules Analysis)
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20 pages, 8276 KiB  
Article
Stoichiometric Analysis of Shifting in Subcellular Compartmentalization of HSP70 within Ischemic Penumbra
by Federica Mastroiacovo, Francesca Biagioni, Paola Lenzi, Larisa Ryskalin, Stefano Puglisi-Allegra, Ferdinando Nicoletti, Alessandro Frati and Francesco Fornai
Molecules 2021, 26(12), 3578; https://doi.org/10.3390/molecules26123578 - 11 Jun 2021
Cited by 3 | Viewed by 1850
Abstract
The heat shock protein (HSP) 70 is considered the main hallmark in preclinical studies to stain the peri-infarct region defined area penumbra in preclinical models of brain ischemia. This protein is also considered as a potential disease modifier, which may improve the outcome [...] Read more.
The heat shock protein (HSP) 70 is considered the main hallmark in preclinical studies to stain the peri-infarct region defined area penumbra in preclinical models of brain ischemia. This protein is also considered as a potential disease modifier, which may improve the outcome of ischemic damage. In fact, the molecule HSP70 acts as a chaperonine being able to impact at several level the homeostasis of neurons. Despite being used routinely to stain area penumbra in light microscopy, the subcellular placement of this protein within area penumbra neurons, to our knowledge, remains undefined. This is key mostly when considering studies aimed at deciphering the functional role of this protein as a determinant of neuronal survival. The general subcellular placement of HSP70 was grossly reported in studies using confocal microscopy, although no direct visualization of this molecule at electron microscopy was carried out. The present study aims to provide a direct evidence of HSP70 within various subcellular compartments. In detail, by using ultrastructural morphometry to quantify HSP70 stoichiometrically detected by immuno-gold within specific organelles we could compare the compartmentalization of the molecule within area penumbra compared with control brain areas. The study indicates that two cell compartments in control conditions own a high density of HSP70, cytosolic vacuoles and mitochondria. In these organelles, HSP70 is present in amount exceeding several-fold the presence in the cytosol. Remarkably, within area penumbra a loss of such a specific polarization is documented. This leads to the depletion of HSP70 from mitochondria and mostly cell vacuoles. Such an effect is expected to lead to significant variations in the ability of HSP70 to exert its physiological roles. The present findings, beyond defining the neuronal compartmentalization of HSP70 within area penumbra may lead to a better comprehension of its beneficial/detrimental role in promoting neuronal survival. Full article
(This article belongs to the Special Issue Electron Microscopy in Molecules Analysis)
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14 pages, 3498 KiB  
Article
Effect of Alpha-1 Antitrypsin on CFTR Levels in Primary Human Airway Epithelial Cells Grown at the Air-Liquid-Interface
by Frauke Stanke, Sabina Janciauskiene, Stephanie Tamm, Sabine Wrenger, Ellen Luise Raddatz, Danny Jonigk and Peter Braubach
Molecules 2021, 26(9), 2639; https://doi.org/10.3390/molecules26092639 - 30 Apr 2021
Cited by 2 | Viewed by 2295
Abstract
The cystic fibrosis transmembrane conductance regulator (CFTR) gene is influenced by the fundamental cellular processes like epithelial differentiation/polarization, regeneration and epithelial–mesenchymal transition. Defects in CFTR protein levels and/or function lead to decreased airway surface liquid layer facilitating microbial colonization and inflammation. The SERPINA1 [...] Read more.
The cystic fibrosis transmembrane conductance regulator (CFTR) gene is influenced by the fundamental cellular processes like epithelial differentiation/polarization, regeneration and epithelial–mesenchymal transition. Defects in CFTR protein levels and/or function lead to decreased airway surface liquid layer facilitating microbial colonization and inflammation. The SERPINA1 gene, encoding alpha1-antitrypsin (AAT) protein, is one of the genes implicated in CF, however it remains unknown whether AAT has any influence on CFTR levels. In this study we assessed CFTR protein levels in primary human lung epithelial cells grown at the air-liquid-interface (ALI) alone or pre-incubated with AAT by Western blots and immunohistochemistry. Histological analysis of ALI inserts revealed CFTR- and AAT-positive cells but no AAT-CFTR co-localization. When 0.5 mg/mL of AAT was added to apical or basolateral compartments of pro-inflammatory activated ALI cultures, CFTR levels increased relative to activated ALIs. This finding suggests that AAT is CFTR-modulating protein, albeit its effects may depend on the concentration and the route of administration. Human lung epithelial ALI cultures provide a useful tool for studies in detail how AAT or other pharmaceuticals affect the levels and activity of CFTR. Full article
(This article belongs to the Special Issue Electron Microscopy in Molecules Analysis)
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