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Article ; Online: HSPB8 counteracts tumor activity of BRAF- and NRAS-mutant melanoma cells by modulation of RAS-prenylation and autophagy.

Cristofani, Riccardo / Piccolella, Margherita / Montagnani Marelli, Marina / Tedesco, Barbara / Poletti, Angelo / Moretti, Roberta Manuela

Cell death & disease

2022 Volume 13, Issue 11, Page(s) 973

Abstract: Cutaneous melanoma is one of the most aggressive and lethal forms of skin cancer. Some specific driver mutations have been described in multiple oncogenes including BRAF and NRAS that are mutated in 60-70% and 15-20% of melanoma, respectively. The aim of ...

Abstract	Cutaneous melanoma is one of the most aggressive and lethal forms of skin cancer. Some specific driver mutations have been described in multiple oncogenes including BRAF and NRAS that are mutated in 60-70% and 15-20% of melanoma, respectively. The aim of this study was to evaluate the role of Small Heat Shock Protein B8 (HSPB8) on cell growth and migration of both BLM (BRAF
MeSH term(s)	Humans ; Melanoma/pathology ; Skin Neoplasms/genetics ; Proto-Oncogene Proteins B-raf/metabolism ; GTP Phosphohydrolases/genetics ; GTP Phosphohydrolases/metabolism ; Heat-Shock Proteins/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Prenylation ; Autophagy/genetics ; Molecular Chaperones/metabolism
Chemical Substances	Proto-Oncogene Proteins B-raf (EC 2.7.11.1) ; GTP Phosphohydrolases (EC 3.6.1.-) ; Heat-Shock Proteins ; Membrane Proteins ; BRAF protein, human (EC 2.7.11.1) ; HSPB8 protein, human ; Molecular Chaperones ; NRAS protein, human (EC 3.6.1.-)
Language	English
Publishing date	2022-11-18
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2541626-1
ISSN	2041-4889 ; 2041-4889
ISSN (online)	2041-4889
ISSN	2041-4889
DOI	10.1038/s41419-022-05365-9
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Identification of HSPB8 modulators counteracting misfolded protein accumulation in neurodegenerative diseases

Chierichetti, Marta / Cerretani, Mauro / Ciammaichella, Alina / Crippa, Valeria / Rusmini, Paola / Ferrari, Veronica / Tedesco, Barbara / Casarotto, Elena / Cozzi, Marta / Mina, Francesco / Pramaggiore, Paola / Galbiati, Mariarita / Piccolella, Margherita / Bresciani, Alberto / Cristofani, Riccardo / Poletti, Angelo

Life Sciences. 2023 June, v. 322 p.121323-

2023

Abstract: The small Heat Shock Protein B8 (HSPB8) is the core component of the Chaperone-Assisted Selective Autophagy (CASA) complex. This complex selectively targets, transports, and tags misfolded proteins for their recognition by autophagy receptors and ... ...

Abstract	The small Heat Shock Protein B8 (HSPB8) is the core component of the Chaperone-Assisted Selective Autophagy (CASA) complex. This complex selectively targets, transports, and tags misfolded proteins for their recognition by autophagy receptors and insertion into the autophagosome for clearance. CASA is essential to maintain intracellular proteostasis, especially in heart, muscle, and brain often exposed to various types of cell stresses. In neurons, HSPB8 protects against neurotoxicity caused by misfolded proteins in several models of neurodegenerative diseases; by facilitating autophagy, HSPB8 assists misfolded proteins degradation also counteracting proteasome overwhelming and inhibition. To enhance HSPB8 protective activity, we screened a library of approximately 120,000 small molecules to identify compounds capable of increasing HSPB8 gene transcription, translation, or protein stability. We found 83 active compounds active in preliminary dose-response assays and further classified them in 19 chemical classes by medicinal chemists' visual inspection. Of these 19 prototypes, 14 induced HSPB8 mRNA and protein levels in SH-SY5Y cells. Out of these 14 compounds, 3 successfully reduced the aggregation propensity of a disease-associated mutant misfolded superoxide dismutase 1 (SOD1) protein in a flow cytometry-based aggregation assay (Flow cytometric analysis of Inclusions and Trafficking (FloIT)) and induced the expression (mRNA and protein) of some autophagy receptors. Notably, the 3 hits were inactive in HSPB8-depleted cells, confirming that their protective activity is mediated by and requires HSPB8. These compounds may be highly relevant for a therapeutic approach in several human disorders, including neurodegenerative diseases, in which enhancement of CASA exerts beneficial activities.
Keywords	autophagosomes ; brain ; dose response ; flow cytometry ; heart ; heat shock proteins ; humans ; macroautophagy ; muscles ; mutants ; neurotoxicity ; proteasome endopeptidase complex ; superoxide dismutase ; therapeutics ; transcription (genetics) ; HSPB8 ; cancer ; Neurodegenerative disorders ; Neuromuscular disorders ; Chaperone-assisted selective autophagy ; Proteasome
Language	English
Dates of publication	2023-06
Publishing place	Elsevier Inc.
Document type	Article ; Online
Note	Use and reproduction
ZDB-ID	3378-9
ISSN	1879-0631 ; 0024-3205
ISSN (online)	1879-0631
ISSN	0024-3205
DOI	10.1016/j.lfs.2022.121323
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: The Role of HSPB8, a Component of the Chaperone-Assisted Selective Autophagy Machinery, in Cancer.

Cristofani, Riccardo / Piccolella, Margherita / Crippa, Valeria / Tedesco, Barbara / Montagnani Marelli, Marina / Poletti, Angelo / Moretti, Roberta M

Cells

2021 Volume 10, Issue 2

Abstract: The cellular response to cancer-induced stress is one of the major aspects regulating cancer development and progression. The Heat Shock Protein B8 (HSPB8) is a small chaperone involved in chaperone-assisted selective autophagy (CASA). CASA promotes the ... ...

Abstract	The cellular response to cancer-induced stress is one of the major aspects regulating cancer development and progression. The Heat Shock Protein B8 (HSPB8) is a small chaperone involved in chaperone-assisted selective autophagy (CASA). CASA promotes the selective degradation of proteins to counteract cell stress such as tumor-induced stress. HSPB8 is also involved in (i) the cell division machinery regulating chromosome segregation and cell cycle arrest in the G0/G1 phase and (ii) inflammation regulating dendritic cell maturation and cytokine production. HSPB8 expression and role are tumor-specific, showing a dual and opposite role. Interestingly, HSPB8 may be involved in the acquisition of chemoresistance to drugs. Despite the fact the mechanisms of HSPB8-mediated CASA activation in tumors need further studies, HSPB8 could represent an important factor in cancer induction and progression and it may be a potential target for anticancer treatment in specific types of cancer. In this review, we will discuss the molecular mechanism underlying HSPB8 roles in normal and cancer conditions. The basic mechanisms involved in anti- and pro-tumoral activities of HSPB8 are deeply discussed together with the pathways that modulate HSPB8 expression, in order to outline molecules with a beneficial effect for cancer cell growth, migration, and death.
MeSH term(s)	Autophagy ; Heat-Shock Proteins/metabolism ; Humans ; Molecular Chaperones/metabolism ; Neoplasms/genetics ; Neoplasms/pathology
Chemical Substances	HSPB8 protein, human ; Heat-Shock Proteins ; Molecular Chaperones
Language	English
Publishing date	2021-02-05
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells10020335
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Article ; Online: The Role of Small Heat Shock Proteins in Protein Misfolding Associated Motoneuron Diseases.

Tedesco, Barbara / Ferrari, Veronica / Cozzi, Marta / Chierichetti, Marta / Casarotto, Elena / Pramaggiore, Paola / Mina, Francesco / Galbiati, Mariarita / Rusmini, Paola / Crippa, Valeria / Cristofani, Riccardo / Poletti, Angelo

International journal of molecular sciences

2022 Volume 23, Issue 19

Abstract: Motoneuron diseases (MNDs) are neurodegenerative conditions associated with death of upper and/or lower motoneurons (MNs). Proteostasis alteration is a pathogenic mechanism involved in many MNDs and is due to the excessive presence of misfolded and ... ...

Abstract	Motoneuron diseases (MNDs) are neurodegenerative conditions associated with death of upper and/or lower motoneurons (MNs). Proteostasis alteration is a pathogenic mechanism involved in many MNDs and is due to the excessive presence of misfolded and aggregated proteins. Protein misfolding may be the product of gene mutations, or due to defects in the translation process, or to stress agents; all these conditions may alter the native conformation of proteins making them prone to aggregate. Alternatively, mutations in members of the protein quality control (PQC) system may determine a loss of function of the proteostasis network. This causes an impairment in the capability to handle and remove aberrant or damaged proteins. The PQC system consists of the degradative pathways, which are the autophagy and the proteasome, and a network of chaperones and co-chaperones. Among these components, Heat Shock Protein 70 represents the main factor in substrate triage to folding, refolding, or degradation, and it is assisted in this task by a subclass of the chaperone network, the small heat shock protein (sHSPs/HSPBs) family. HSPBs take part in proteostasis by bridging misfolded and aggregated proteins to the HSP70 machinery and to the degradative pathways, facilitating refolding or clearance of the potentially toxic proteins. Because of its activity against proteostasis alteration, the chaperone system plays a relevant role in the protection against proteotoxicity in MNDs. Here, we discuss the role of HSPBs in MNDs and which HSPBs may represent a valid target for therapeutic purposes.
MeSH term(s)	HSP70 Heat-Shock Proteins/genetics ; HSP70 Heat-Shock Proteins/metabolism ; Heat-Shock Proteins, Small/genetics ; Heat-Shock Proteins, Small/metabolism ; Humans ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Motor Neuron Disease/metabolism ; Motor Neurons/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Protein Folding ; Proteostasis Deficiencies/metabolism
Chemical Substances	HSP70 Heat-Shock Proteins ; Heat-Shock Proteins, Small ; Molecular Chaperones ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2022-10-04
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms231911759
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Article ; Online: Lysosomes Dysfunction Causes Mitophagy Impairment in PBMCs of Sporadic ALS Patients.

Bordoni, Matteo / Pansarasa, Orietta / Scarian, Eveljn / Cristofani, Riccardo / Leone, Roberta / Fantini, Valentina / Garofalo, Maria / Diamanti, Luca / Bernuzzi, Stefano / Gagliardi, Stella / Carelli, Stephana / Poletti, Angelo / Cereda, Cristina

Cells

2022 Volume 11, Issue 8

Abstract: Mitochondria alterations are present in tissues derived from patients and animal models, but no data are available for peripheral blood mononuclear cells (PBMCs) of ALS patients. This work aims to investigate mitophagy in PBMCs of sporadic (sALS) ... ...

Abstract	Mitochondria alterations are present in tissues derived from patients and animal models, but no data are available for peripheral blood mononuclear cells (PBMCs) of ALS patients. This work aims to investigate mitophagy in PBMCs of sporadic (sALS) patients and how this pathway can be tuned by using small molecules. We found the presence of morphologically atypical mitochondria by TEM and morphological abnormalities by MitoTracker™. We found a decreased number of healthy mitochondria in sALS PBMCs and an impairment of mitophagy with western blot and immunofluorescence. After rapamycin treatment, we found a higher increase in the LC3 marker in sALS PBMCs, while after NH4Cl treatment, we found a lower increase in the LC3 marker. Finally, mTOR-independent autophagy induction with trehalose resulted in a significant decrease in the lysosomes level sALS PBMCs. Our data suggest that the presence of morphologically altered mitochondria and an inefficient turnover of damaged mitochondria in PBMCs of sALS patients rely on the impairment of the mitophagy pathway. We also found that the induction of the mTOR-independent autophagy pathway leads to a decrease in lysosomes level, suggesting a more sensitivity of sALS PBMCs to trehalose. Such evidence suggests that trehalose could represent an effective treatment for ALS patients.
MeSH term(s)	Amyotrophic Lateral Sclerosis/metabolism ; Animals ; Humans ; Leukocytes, Mononuclear/metabolism ; Lysosomes/metabolism ; Mitophagy ; TOR Serine-Threonine Kinases/metabolism ; Trehalose/metabolism
Chemical Substances	Trehalose (B8WCK70T7I) ; TOR Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2022-04-09
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells11081272
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Article ; Online: Valosin Containing Protein (VCP): A Multistep Regulator of Autophagy.

Ferrari, Veronica / Cristofani, Riccardo / Tedesco, Barbara / Crippa, Valeria / Chierichetti, Marta / Casarotto, Elena / Cozzi, Marta / Mina, Francesco / Piccolella, Margherita / Galbiati, Mariarita / Rusmini, Paola / Poletti, Angelo

International journal of molecular sciences

2022 Volume 23, Issue 4

Abstract: Valosin containing protein (VCP) has emerged as a central protein in the regulation of the protein quality control (PQC) system. ...

Abstract	Valosin containing protein (VCP) has emerged as a central protein in the regulation of the protein quality control (PQC) system.
MeSH term(s)	Animals ; Autophagy/physiology ; Humans ; Neurodegenerative Diseases/metabolism ; Neurons/metabolism ; Proteostasis/physiology ; Valosin Containing Protein/metabolism
Chemical Substances	Valosin Containing Protein (EC 3.6.4.6)
Language	English
Publishing date	2022-02-09
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms23041939
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Article ; Online: The role of autophagy-lysosomal pathway in motor neuron diseases.

Tedesco, Barbara / Ferrari, Veronica / Cozzi, Marta / Chierichetti, Marta / Casarotto, Elena / Pramaggiore, Paola / Mina, Francesco / Piccolella, Margherita / Cristofani, Riccardo / Crippa, Valeria / Rusmini, Paola / Galbiati, Mariarita / Poletti, Angelo

Biochemical Society transactions

2022 Volume 50, Issue 5, Page(s) 1489–1503

Abstract: Motor neuron diseases (MNDs) include a broad group of diseases in which neurodegeneration mainly affects upper and/or lower motor neurons (MNs). Although the involvement of specific MNs, symptoms, age of onset, and progression differ in MNDs, the main ... ...

Abstract	Motor neuron diseases (MNDs) include a broad group of diseases in which neurodegeneration mainly affects upper and/or lower motor neurons (MNs). Although the involvement of specific MNs, symptoms, age of onset, and progression differ in MNDs, the main pathogenic mechanism common to most MNDs is represented by proteostasis alteration and proteotoxicity. This pathomechanism may be directly related to mutations in genes encoding proteins involved in the protein quality control system, particularly the autophagy-lysosomal pathway (ALP). Alternatively, proteostasis alteration can be caused by aberrant proteins that tend to misfold and to aggregate, two related processes that, over time, cannot be properly handled by the ALP. Here, we summarize the main ALP features, focusing on different routes utilized to deliver substrates to the lysosome and how the various ALP pathways intersect with the intracellular trafficking of membranes and vesicles. Next, we provide an overview of the mutated genes that have been found associated with MNDs, how these gene products are involved in different steps of ALP and related processes. Finally, we discuss how autophagy can be considered a valid therapeutic target for MNDs treatment focusing on traditional autophagy modulators and on emerging approaches to overcome their limitations.
MeSH term(s)	Humans ; Autophagy/physiology ; Lysosomes/metabolism ; Motor Neuron Disease/genetics ; Motor Neuron Disease/metabolism ; Proteostasis
Language	English
Publishing date	2022-09-29
Publishing country	England
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST20220778
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Article ; Online: Identification of HSPB8 modulators counteracting misfolded protein accumulation in neurodegenerative diseases.

Life sciences

2022 Volume 322, Page(s) 121323

Abstract: Aims: The small Heat Shock Protein B8 (HSPB8) is the core component of the Chaperone-Assisted Selective Autophagy (CASA) complex. This complex selectively targets, transports, and tags misfolded proteins for their recognition by autophagy receptors and ... ...

Abstract	Aims: The small Heat Shock Protein B8 (HSPB8) is the core component of the Chaperone-Assisted Selective Autophagy (CASA) complex. This complex selectively targets, transports, and tags misfolded proteins for their recognition by autophagy receptors and insertion into the autophagosome for clearance. CASA is essential to maintain intracellular proteostasis, especially in heart, muscle, and brain often exposed to various types of cell stresses. In neurons, HSPB8 protects against neurotoxicity caused by misfolded proteins in several models of neurodegenerative diseases; by facilitating autophagy, HSPB8 assists misfolded proteins degradation also counteracting proteasome overwhelming and inhibition. Materials and methods: To enhance HSPB8 protective activity, we screened a library of approximately 120,000 small molecules to identify compounds capable of increasing HSPB8 gene transcription, translation, or protein stability. Key findings: We found 83 active compounds active in preliminary dose-response assays and further classified them in 19 chemical classes by medicinal chemists' visual inspection. Of these 19 prototypes, 14 induced HSPB8 mRNA and protein levels in SH-SY5Y cells. Out of these 14 compounds, 3 successfully reduced the aggregation propensity of a disease-associated mutant misfolded superoxide dismutase 1 (SOD1) protein in a flow cytometry-based aggregation assay (Flow cytometric analysis of Inclusions and Trafficking (FloIT)) and induced the expression (mRNA and protein) of some autophagy receptors. Notably, the 3 hits were inactive in HSPB8-depleted cells, confirming that their protective activity is mediated by and requires HSPB8. Significance: These compounds may be highly relevant for a therapeutic approach in several human disorders, including neurodegenerative diseases, in which enhancement of CASA exerts beneficial activities.
MeSH term(s)	Humans ; Autophagy/physiology ; Heat-Shock Proteins/metabolism ; Molecular Chaperones/metabolism ; Motor Neurons/metabolism ; Neuroblastoma/metabolism ; Neurodegenerative Diseases/metabolism ; Protein Folding
Chemical Substances	Heat-Shock Proteins ; HSPB8 protein, human ; Molecular Chaperones
Language	English
Publishing date	2022-12-24
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	3378-9
ISSN	1879-0631 ; 0024-3205
ISSN (online)	1879-0631
ISSN	0024-3205
DOI	10.1016/j.lfs.2022.121323
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Article ; Online: Neurodegenerative Disease-Associated TDP-43 Fragments Are Extracellularly Secreted with CASA Complex Proteins.

Casarotto, Elena / Sproviero, Daisy / Corridori, Eleonora / Gagliani, Maria Cristina / Cozzi, Marta / Chierichetti, Marta / Cristofani, Riccardo / Ferrari, Veronica / Galbiati, Mariarita / Mina, Francesco / Piccolella, Margherita / Rusmini, Paola / Tedesco, Barbara / Gagliardi, Stella / Cortese, Katia / Cereda, Cristina / Poletti, Angelo / Crippa, Valeria

Cells

2022 Volume 11, Issue 3

Abstract: Extracellular vesicles (EVs) play a central role in neurodegenerative diseases (NDs) since they may either spread the pathology or contribute to the intracellular protein quality control (PQC) system for the cellular clearance of NDs-associated proteins. ...

Abstract	Extracellular vesicles (EVs) play a central role in neurodegenerative diseases (NDs) since they may either spread the pathology or contribute to the intracellular protein quality control (PQC) system for the cellular clearance of NDs-associated proteins. Here, we investigated the crosstalk between large (LVs) and small (SVs) EVs and PQC in the disposal of TDP-43 and its FTLD and ALS-associated C-terminal fragments (TDP-35 and TDP-25). By taking advantage of neuronal cells (NSC-34 cells), we demonstrated that both EVs types, but particularly LVs, contained TDP-43, TDP-35 and TDP-25. When the PQC system was inhibited, as it occurs in NDs, we found that TDP-35 and TDP-25 secretion via EVs increased. In line with this observation, we specifically detected TDP-35 in EVs derived from plasma of FTLD patients. Moreover, we demonstrated that both neuronal and plasma-derived EVs transported components of the chaperone-assisted selective autophagy (CASA) complex (HSP70, BAG3 and HSPB8). Neuronal EVs also contained the autophagy-related MAP1LC3B-II protein. Notably, we found that, under PQC inhibition, HSPB8, BAG3 and MAP1LC3B-II secretion paralleled that of TDP-43 species. Taken together, our data highlight the role of EVs, particularly of LVs, in the disposal of disease-associated TDP-43 species, and suggest a possible new role for the CASA complex in NDs.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Amyotrophic Lateral Sclerosis/metabolism ; Apoptosis Regulatory Proteins/metabolism ; Autophagy-Related Proteins/metabolism ; DNA-Binding Proteins/metabolism ; Extracellular Vesicles/metabolism ; Frontotemporal Lobar Degeneration ; Humans ; Molecular Chaperones/metabolism ; Neurodegenerative Diseases ; Peptide Fragments/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Apoptosis Regulatory Proteins ; Autophagy-Related Proteins ; BAG3 protein, human ; DNA-Binding Proteins ; Molecular Chaperones ; Peptide Fragments ; TARDBP protein, human ; TDP-25 protein, human
Language	English
Publishing date	2022-02-02
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells11030516
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Article ; Online: The Role of Sex and Sex Hormones in Neurodegenerative Diseases.

Vegeto, Elisabetta / Villa, Alessandro / Della Torre, Sara / Crippa, Valeria / Rusmini, Paola / Cristofani, Riccardo / Galbiati, Mariarita / Maggi, Adriana / Poletti, Angelo

Endocrine reviews

2019 Volume 41, Issue 2

Abstract: Neurodegenerative diseases (NDs) are a wide class of disorders of the central nervous system (CNS) with unknown etiology. Several factors were hypothesized to be involved in the pathogenesis of these diseases, including genetic and environmental factors. ...

Abstract	Neurodegenerative diseases (NDs) are a wide class of disorders of the central nervous system (CNS) with unknown etiology. Several factors were hypothesized to be involved in the pathogenesis of these diseases, including genetic and environmental factors. Many of these diseases show a sex prevalence and sex steroids were shown to have a role in the progression of specific forms of neurodegeneration. Estrogens were reported to be neuroprotective through their action on cognate nuclear and membrane receptors, while adverse effects of male hormones have been described on neuronal cells, although some data also suggest neuroprotective activities. The response of the CNS to sex steroids is a complex and integrated process that depends on (i) the type and amount of the cognate steroid receptor and (ii) the target cell type-either neurons, glia, or microglia. Moreover, the levels of sex steroids in the CNS fluctuate due to gonadal activities and to local metabolism and synthesis. Importantly, biochemical processes involved in the pathogenesis of NDs are increasingly being recognized as different between the two sexes and as influenced by sex steroids. The aim of this review is to present current state-of-the-art understanding on the potential role of sex steroids and their receptors on the onset and progression of major neurodegenerative disorders, namely, Alzheimer's disease, Parkinson's diseases, amyotrophic lateral sclerosis, and the peculiar motoneuron disease spinal and bulbar muscular atrophy, in which hormonal therapy is potentially useful as disease modifier.
MeSH term(s)	Female ; Gonadal Steroid Hormones/metabolism ; Humans ; Male ; Neurodegenerative Diseases/drug therapy ; Neurodegenerative Diseases/metabolism ; Receptors, Steroid/metabolism ; Sex Characteristics
Chemical Substances	Gonadal Steroid Hormones ; Receptors, Steroid
Language	English
Publishing date	2019-09-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	603096-8
ISSN	1945-7189 ; 0163-769X
ISSN (online)	1945-7189
ISSN	0163-769X
DOI	10.1210/endrev/bnz005
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