Cell calciumPub Date : 2024-12-01Epub Date: 2024-11-22DOI: 10.1016/j.ceca.2024.102972
Ana M. Hernández-Vega , Refugio García-Villegas , Tamara Rosenbaum
{"title":"Roles for TRPV4 in disease: A discussion of possible mechanisms","authors":"Ana M. Hernández-Vega , Refugio García-Villegas , Tamara Rosenbaum","doi":"10.1016/j.ceca.2024.102972","DOIUrl":"10.1016/j.ceca.2024.102972","url":null,"abstract":"<div><div>The transient receptor potential vanilloid 4 (TRPV4) ion channel is a ubiquitously expressed Ca<sup>2+</sup>-permeable ion channel that controls intracellular calcium ([Ca<sup>2+</sup>]<sub>i</sub>) homeostasis in various types of cells. The physiological roles for TRPV4 are tissue specific and the mechanisms behind this specificity remain mostly unclarified. It is noteworthy that mutations in the TRPV4 channel have been associated to a broad spectrum of congenital diseases, with most of these mutations mainly resulting in gain-of-function. Mutations have been identified in human patients showing a variety of phenotypes and symptoms, mostly related to skeletal and neuromuscular disorders. Since TRPV4 is so widely expressed throughout the body, it comes as no surprise that the literature is growing in evidence linking this protein to malfunction in systems other than the skeletal and neuromuscular. In this review, we summarize the expression patterns of TRPV4 in several tissues and highlight findings of recent studies that address critical structural and functional features of this channel, particularly focusing on its interactions and signaling pathways related to Ca<sup>2+</sup> entry. Moreover, we discuss the roles of TRPV4 mutations in some diseases and pinpoint some of the mechanisms underlying pathological states where TRPV4’s malfunction is prominent.</div></div>","PeriodicalId":9678,"journal":{"name":"Cell calcium","volume":"124 ","pages":"Article 102972"},"PeriodicalIF":4.3,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142749679","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Cell calciumPub Date : 2024-12-01Epub Date: 2024-10-18DOI: 10.1016/j.ceca.2024.102961
Tadashi Makio, Junsheng Chen, Thomas Simmen
{"title":"ER stress as a sentinel mechanism for ER Ca2+ homeostasis","authors":"Tadashi Makio, Junsheng Chen, Thomas Simmen","doi":"10.1016/j.ceca.2024.102961","DOIUrl":"10.1016/j.ceca.2024.102961","url":null,"abstract":"<div><div>Endoplasmic reticulum (ER) stress is triggered upon the interference with oxidative protein folding that aims to produce fully folded, disulfide-bonded and glycosylated proteins, which are then competent to exit the ER. Many of the enzymes catalyzing this process require the binding of Ca<sup>2+</sup> ions, including the chaperones BiP/GRP78, calnexin and calreticulin. The induction of ER stress with a variety of drugs interferes with chaperone Ca<sup>2+</sup> binding, increases cytosolic Ca<sup>2+</sup>through the opening of ER Ca<sup>2+</sup> channels, and activates store-operated Ca<sup>2+</sup> entry (SOCE). Posttranslational modifications (PTMs) of the ER Ca<sup>2+</sup> handling proteins through ER stress-dependent phosphorylation or oxidation control these mechanisms, as demonstrated in the case of the sarco/endoplasmic reticulum ATPase (SERCA), inositol 1,4,5 trisphosphate receptors (IP<sub>3</sub>Rs) or stromal interaction molecule 1 (STIM1). Their aim is to restore ER Ca<sup>2+</sup> homeostasis but also to increase Ca<sup>2+</sup> transfer from the ER to mitochondria during ER stress. This latter function boosts ER bioenergetics, but also triggers apoptosis if ER Ca<sup>2+</sup> signaling persists. ER Ca<sup>2+</sup> toolkit oxidative modifications upon ER stress can occur within the ER lumen or in the adjacent cytosol. Enzymes involved in this redox control include ER oxidoreductin 1 (ERO1) or the thioredoxin-family protein disulfide isomerases (PDI) and ERp57. A tight, but adaptive connection between ER Ca<sup>2+</sup> content, ER stress and mitochondrial readouts allows for the proper functioning of many tissues, including skeletal muscle, the liver, and the pancreas, where ER stress either maintains or compromises their function, depending on its extent and context. Upon mutation of key regulators of ER Ca<sup>2+</sup> signaling, diseases such as muscular defects (e.g., from mutated selenoprotein N, SEPN1/SELENON), or diabetes (e.g., from mutated PERK) are the result.</div></div>","PeriodicalId":9678,"journal":{"name":"Cell calcium","volume":"124 ","pages":"Article 102961"},"PeriodicalIF":4.3,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142544020","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Cell calciumPub Date : 2024-12-01Epub Date: 2024-09-23DOI: 10.1016/j.ceca.2024.102956
Martin J. Kelly , Jian Qiu
{"title":"TRPC5 channels play a critical role in mediating multiple behaviors in mice and men","authors":"Martin J. Kelly , Jian Qiu","doi":"10.1016/j.ceca.2024.102956","DOIUrl":"10.1016/j.ceca.2024.102956","url":null,"abstract":"","PeriodicalId":9678,"journal":{"name":"Cell calcium","volume":"124 ","pages":"Article 102956"},"PeriodicalIF":4.3,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142364556","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Cell calciumPub Date : 2024-12-01Epub Date: 2024-11-02DOI: 10.1016/j.ceca.2024.102967
Sonja Sivcev , Stephanie Constantin , Kosara Smiljanic , Srdjan J. Sokanovic , Patrick A. Fletcher , Arthur S. Sherman , Hana Zemkova , Stanko S. Stojilkovic
{"title":"Distribution and calcium signaling function of somatostatin receptor subtypes in rat pituitary","authors":"Sonja Sivcev , Stephanie Constantin , Kosara Smiljanic , Srdjan J. Sokanovic , Patrick A. Fletcher , Arthur S. Sherman , Hana Zemkova , Stanko S. Stojilkovic","doi":"10.1016/j.ceca.2024.102967","DOIUrl":"10.1016/j.ceca.2024.102967","url":null,"abstract":"<div><div>The somatostatin (SST) receptor family controls pituitary hormone secretion, but the distribution and specific roles of these receptors on the excitability and voltage-gated calcium signaling of hormone producing pituitary cells have not been fully characterized. Here we show that the rat pituitary gland expressed <em>Sstr1, Sstr2, Sstr3,</em> and <em>Sstr5</em> receptor genes in a cell type-specific manner: <em>Sstr1</em> and <em>Sstr2</em> in thyrotrophs, <em>Sstr3</em> in gonadotrophs and lactotrophs, <em>Sstr2, Sstr3</em>, and <em>Sstr5</em> in somatotrophs, and none in corticotrophs and melanotrophs. Most gonadotrophs and thyrotrophs spontaneously fired high-amplitude single action potentials, which were silenced by SST without affecting intracellular calcium concentrations. In contrast, lactotrophs and somatotrophs spontaneously fired low-amplitude plateau-bursting action potentials in conjunction with calcium transients, both of which were silenced by SST. Moreover, SST inhibited GPCR-induced voltage-gated calcium signaling and hormone secretion in all cell types expressing SST receptors, but the inhibition was more pronounced in somatotrophs. The pattern of inhibition of electrical activity and calcium signaling was consistent with both direct and indirect inhibition of voltage-gated calcium channels, the latter being driven by cell type-specific hyperpolarization. These results indicate that the action of SST in somatotrophs is enhanced by the expression of several types of SST receptors and their slow desensitization, that SST may play a role in the electrical resynchronization of gonadotrophs, thyrotrophs, and lactotrophs, and that the lack of SST receptors in corticotrophs and melanotrophs keeps them excitable and ready to responses to stress.</div></div>","PeriodicalId":9678,"journal":{"name":"Cell calcium","volume":"124 ","pages":"Article 102967"},"PeriodicalIF":4.3,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142614266","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Cell calciumPub Date : 2024-12-01Epub Date: 2024-09-12DOI: 10.1016/j.ceca.2024.102955
Riccardo Filadi , Paola Pizzo
{"title":"Endoplasmic reticulum-mitochondria lockdown in Wolfram syndrome","authors":"Riccardo Filadi , Paola Pizzo","doi":"10.1016/j.ceca.2024.102955","DOIUrl":"10.1016/j.ceca.2024.102955","url":null,"abstract":"<div><p>Wolfram syndrome (WS) is an incurable autosomal recessive disorder originally described as a mitochondriopathy. In a recent work, Liiv and colleagues found that an impaired endoplasmic reticulum (ER)-to-mitochondria calcium shuttling underlies mitochondrial dysfunction in WS models.</p></div>","PeriodicalId":9678,"journal":{"name":"Cell calcium","volume":"124 ","pages":"Article 102955"},"PeriodicalIF":4.3,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142232160","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Cell calciumPub Date : 2024-12-01Epub Date: 2024-10-21DOI: 10.1016/j.ceca.2024.102964
Felipe Tribiños, Marcelo A. Catalan
{"title":"Calcium and chloride out of sync: The role of signaling in Sjögren's salivary gland issues","authors":"Felipe Tribiños, Marcelo A. Catalan","doi":"10.1016/j.ceca.2024.102964","DOIUrl":"10.1016/j.ceca.2024.102964","url":null,"abstract":"","PeriodicalId":9678,"journal":{"name":"Cell calcium","volume":"124 ","pages":"Article 102964"},"PeriodicalIF":4.3,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142495676","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Cell calciumPub Date : 2024-12-01Epub Date: 2024-11-16DOI: 10.1016/j.ceca.2024.102971
Pablo Hernansanz-Agustín , Carmen Morales-Vidal , Enrique Calvo , Paolo Natale , Yolanda Martí-Mateos , Sara Natalia Jaroszewicz , José Luis Cabrera-Alarcón , Rebeca Acín-Pérez , Iván López-Montero , Jesús Vázquez , José Antonio Enríquez
{"title":"Electrogenic and non-electrogenic ion antiporters participate in controling membrane potential","authors":"Pablo Hernansanz-Agustín , Carmen Morales-Vidal , Enrique Calvo , Paolo Natale , Yolanda Martí-Mateos , Sara Natalia Jaroszewicz , José Luis Cabrera-Alarcón , Rebeca Acín-Pérez , Iván López-Montero , Jesús Vázquez , José Antonio Enríquez","doi":"10.1016/j.ceca.2024.102971","DOIUrl":"10.1016/j.ceca.2024.102971","url":null,"abstract":"<div><div>In a comment to our recent publication, Nicholls question our results and interpretation based on theoretical arguments that reveal a profound misunderstanding of our publication.</div></div>","PeriodicalId":9678,"journal":{"name":"Cell calcium","volume":"124 ","pages":"Article 102971"},"PeriodicalIF":4.3,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142692782","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Cell calciumPub Date : 2024-12-01Epub Date: 2024-10-18DOI: 10.1016/j.ceca.2024.102963
Jan B. Parys
{"title":"The IP3 receptor-KRAP complex at the desmosomes: A new player in the apoptotic process","authors":"Jan B. Parys","doi":"10.1016/j.ceca.2024.102963","DOIUrl":"10.1016/j.ceca.2024.102963","url":null,"abstract":"<div><div>The IP<sub>3</sub> receptor (IP<sub>3</sub>R) is a ubiquitously expressed Ca<sup>2+</sup>-release channel located in the endoplasmic reticulum (ER). Ca<sup>2+</sup> signals originating from the IP<sub>3</sub>R initiate or regulate a plethora of cellular events, including cell life and death processes, e.g. exaggerated Ca<sup>2+</sup> release from the ER to the mitochondria is a trigger for apoptosis. Recently, Cho et al. (Current Biology, 2024, DOI: 10.1016/j.cub.2024.08.057) demonstrated that in epithelial monolayers a sustained [Ca<sup>2+</sup>] elevation caused by the IP<sub>3</sub>Rs is responsible for the extrusion of adjacent apoptotic cells out of the epithelial monolayer. Interestingly, the IP<sub>3</sub>Rs involved are associated with the desmosomes via K-Ras-induced actin-interacting protein (KRAP). This study not only highlight a novel role of the IP<sub>3</sub>R in apoptosis, but also shed a new light on how KRAP -and by extension KRAP-related proteins- contribute to the regulation of IP<sub>3</sub>R activity and, more broadly, underscores the crucial role of associated proteins in determining the function of IP<sub>3</sub>Rs.</div></div>","PeriodicalId":9678,"journal":{"name":"Cell calcium","volume":"124 ","pages":"Article 102963"},"PeriodicalIF":4.3,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142495677","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}