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Cells
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Cell Biology in the United States: Latest Advances and Perspectives
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Cell Biology in the United States: Latest Advances and Perspectives

A topical collection in Cells (ISSN 2073-4409).

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Editor

Dr. Alexander G. Obukhov

E-Mail Website
Collection Editor
The Department of Anatomy, Cell Biology & Physiology, Indiana University School of Medicine, Indianapolis, IN, USA
Interests: TRPC channels; voltage-gated Ca2+ channels; Ca2+ influx; endothelial dysfunction; atherosclerosis
Special Issues, Collections and Topics in MDPI journals

Topical Collection Information

Dear Colleagues,

This Topic Collection aims to showcase the latest scientific advances in cell biology achieved in the United States. The scope of this Topic Collection is very broad, ranging from cell division regulation and subcellular organelle function to the mechanisms of membrane transport and cell motility. Original research articles, comprehensive reviews and perspectives will be considered. Manuscripts should describe the novel molecular and cellular mechanisms underlying the physiologically relevant phenomena or disease-related cellular processes in all disciplines, such as neuroscience, physiology, immunology, cancer cell biology, developmental biology and beyond. Manuscripts describing organoid research and cellular responses to viral infections, such as SARS-CoV-2 or HIV infection, will also be considered. Potential topics may include, but are not limited to, the following research areas:

  • Cancer cell biology and cancer stem cells.
  • CAR T-cell and other adoptive cell transfer therapies.
  • Cell cycle.
  • Cell migration.
  • Cell-to-cell communication and cell adhesion.
  • Cell growth, differentiation, aging and death.
  • Cellular metabolism.
  • Cellular mechanosensory elements.
  • Cellular mechanisms underlying human diseases.
  • Cellular photosensory elements and underlying mechanisms.
  • Cellular quality control.
  • Cytoskeletal dynamics.
  • DNA replication and repair; non-coding RNAs.
  • Hematopoiesis and stem cells.
  • Ion channel function in health and disease (transient receptor potential   channels, store-operated channels, ligand-gated ion channels, second-messenger-gated channels and voltage-gated ion channels).
  • Ion channel biophysics.
  • Membrane physiology and membrane transport.
  • Cellular organelles (mitochondria, lysosomes, peroxisomes, etc.).
  • Omics: transcriptomics, genomics, proteomics, metabolomics, glycomics, lipidomics, interactomics, fluxomics and biomics.
  • Protein synthesis and trafficking.
  • Signal transduction. 

Dr. Alexander G. Obukhov
Collection 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 collection 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. Cells 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.

Related Special Issue

Published Papers (6 papers)

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2025

Jump to: 2024, 2023, 2022

28 pages, 2711 KiB  
Article
Soluble β-Amyloid Oligomers Selectively Upregulate TRPC3 in Excitatory Neurons via Calcineurin-Coupled NFAT
by Zhengjun Wang, Dongyi Ding, Jiaxing Wang, Ling Chen, Qingming Dong, Moumita Khamrai, Yuyang Zhou, Akihiro Ishii, Kazuko Sakata, Wei Li, Jianyang Du, Thirumalini Vaithianathan, Fu-Ming Zhou and Francesca-Fang Liao
Cells 2025, 14(11), 843; https://doi.org/10.3390/cells14110843 - 4 Jun 2025
Viewed by 580
Abstract
To investigate how dysregulated transient receptor potential canonical channels (TRPCs) are associated with Alzheimer’s disease (AD), we challenged primary neurons with amyloid-β (Aβ). Both the naturally secreted or synthetic Aβ oligomers (AβOs) induced long-lasting increased TRPC3 and downregulated the TRPC6 expression in mature [...] Read more.
To investigate how dysregulated transient receptor potential canonical channels (TRPCs) are associated with Alzheimer’s disease (AD), we challenged primary neurons with amyloid-β (Aβ). Both the naturally secreted or synthetic Aβ oligomers (AβOs) induced long-lasting increased TRPC3 and downregulated the TRPC6 expression in mature excitatory neurons (CaMKIIα-high) via a Ca2+-dependent calcineurin-coupled NFAT transcriptionally and calpain-mediated protein degradation, respectively. The TRPC3 expression was also found to be upregulated in pyramidal neurons of human AD brains. The selective downregulation of the Trpc6 gene induced synaptotoxicity, while no significant effect was observed from the Trpc3-targeting siRNA, suggesting potentially differential roles of TRPC3 and 6 in modulating the synaptic morphology and functions. Electrophysiological recordings of mouse hippocampal slices overexpressing TRPC3 revealed increased neuronal hyperactivity upon the TRPC3 channel activation by its agonist. Furthermore, the AβO-mediated synaptotoxicity appeared to be positively correlated with the degrees of the induced dendritic Ca2+ flux in neurons, which was completely prevented by the co-treatment with two pyrazole-based TRPC3-selective antagonists Pyr3 or Pyr10. Taken together, our findings suggest that the aberrantly upregulated TRPC3 is another ion channel critically contributing to the process of AβO-induced Ca2+ overload, neuronal hyperexcitation, and synaptotoxicity, thus representing a potential therapeutic target of AD. Full article
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2024

Jump to: 2025, 2023, 2022

19 pages, 2985 KiB  
Article
Effects of TRPC1’s Lysines on Heteromeric TRPC5-TRPC1 Channel Function
by Isaac S. Demaree, Sanjay Kumar, Kayla Tennessen, Quyen Q. Hoang, Fletcher A. White and Alexander G. Obukhov
Cells 2024, 13(23), 2019; https://doi.org/10.3390/cells13232019 - 6 Dec 2024
Viewed by 1069
Abstract
Background: TRPC5 proteins form plasma membrane cation channels and are expressed in the nervous and cardiovascular systems. TRPC5 activation leads to cell depolarization and increases neuronal excitability, whereas a homologous TRPC1 inhibits TRPC5 function via heteromerization. The mechanism underlying the inhibitory effect of [...] Read more.
Background: TRPC5 proteins form plasma membrane cation channels and are expressed in the nervous and cardiovascular systems. TRPC5 activation leads to cell depolarization and increases neuronal excitability, whereas a homologous TRPC1 inhibits TRPC5 function via heteromerization. The mechanism underlying the inhibitory effect of TRPC1 in TRPC5/TRPC1 heteromers remains unknown. Methods: We used electrophysiological techniques to examine the roles of subunit stoichiometry and positively charged luminal residues of TRPC1 on TRPC5/TRPC1 function. We also performed molecular dynamics simulations. Results: We found that increasing the relative amount of TRPC1 in TRPC5/TRPC1 heteromers reduced histamine-induced cation influx through the heteromeric channels. Consistently, histamine-induced cation influx was small in cells co-expressing TRPC5-TRPC1 concatemers and TRPC1, and large in cells co-expressing TRPC5-TRPC1 concatemers and TRPC5. Molecular dynamics simulations revealed that the TRPC1 protein has two positively charged lysine residues that are facing the heteromeric channel pore lumen. Substitution of these lysines with asparagines decreased TRPC1’s inhibitory effect on TRPC5/TRPC1 function, indicating that these lysines may regulate cation influx through TRPC5/TRPC1 heteromers. Additionally, we established that extracellular Mg2+ inhibits cation influx through TRPC5/TRPC1, contributing to channel regulation. Conclusions: We revealed that the inhibitory effect of TRPC1 on heteromeric TRPC5/TRPC1 function likely involves luminal lysines of TRPC1. Full article
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20 pages, 18147 KiB  
Article
CD38 Inhibitor 78c Attenuates Pro-Inflammatory Cytokine Expression and Osteoclastogenesis in Macrophages
by William Lory, Nityananda Chowdhury, Bridgette Wellslager, Subramanya Pandruvada, Yan Huang, Özlem Yilmaz and Hong Yu
Cells 2024, 13(23), 1971; https://doi.org/10.3390/cells13231971 - 28 Nov 2024
Cited by 1 | Viewed by 1585
Abstract
CD38, a nicotinamide adenine dinucleotide (NAD+) glycohydrolase, increases during infection or inflammation. Therefore, we aimed to evaluate the effects of a CD38 inhibitor (78c) on NAD+ levels, IL-1β, IL-6, TNF-α cytokine expressions, and osteoclastogenesis. The results show that treatment with [...] Read more.
CD38, a nicotinamide adenine dinucleotide (NAD+) glycohydrolase, increases during infection or inflammation. Therefore, we aimed to evaluate the effects of a CD38 inhibitor (78c) on NAD+ levels, IL-1β, IL-6, TNF-α cytokine expressions, and osteoclastogenesis. The results show that treatment with 78c on murine BMMs dose-dependently reduced CD38, reversed the decline of NAD+, and inhibited IL-1β, IL-6, and TNF-α pro-inflammatory cytokine levels induced by oral pathogen Porphyromonas gingivalis (Pg) or Aggregatibacter actinomycetemcomitans (Aa) or by advanced glycation end products (AGEs). Additionally, treatment with 78c dose-dependently suppressed osteoclastogenesis and bone resorption induced by RANKL. Treatment with 78c suppressed CD38, nuclear factor kappa-B (NF-κB), phosphoinositide 3-kinase (PI3K), and mitogen-activated protein kinases (MAPKs) induced by Pg, Aa, or AGEs, and suppressed podosome components (PI3K, Pyk2, Src, F-actin, integrins, paxillin, and talin) induced by RANKL. These results from our studies support the finding that the inhibition of CD38 by 78c is a promising therapeutic strategy to treat inflammatory bone loss diseases. However, treatment with a CD38 shRNA only significantly reduced IL-1β, IL-6, and TNF-α pro-inflammatory cytokine levels induced by AGEs. Compared with controls, it had limited effects on cytokine levels induced by Pg or Aa. Treatment with the CD38 shRNA enhanced RANKL-induced osteoclastogenesis, suggesting that 78c has some off-target effects. Full article
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17 pages, 6804 KiB  
Article
Modelling Functional Thyroid Follicular Structures Using P19 Embryonal Carcinoma Cells
by Fatimah Najjar, Liming Milbauer, Chin-Wen Wei, Thomas Lerdall and Li-Na Wei
Cells 2024, 13(22), 1844; https://doi.org/10.3390/cells13221844 - 7 Nov 2024
Cited by 1 | Viewed by 940
Abstract
Thyroid gland diseases remain clinical challenges due to the lack of reliable in vitro models to examine molecular pathways of thyrocytes development, maturation, and functional maintenance. This study aimed to develop in vitro thyrocytes model using a stem cell culture, P19 embryonal carcinoma [...] Read more.
Thyroid gland diseases remain clinical challenges due to the lack of reliable in vitro models to examine molecular pathways of thyrocytes development, maturation, and functional maintenance. This study aimed to develop in vitro thyrocytes model using a stem cell culture, P19 embryonal carcinoma which requires no feeder layer, differentiation into mature and functional thyrocytes that allow molecular and genetic manipulation for studying thyroid diseases. The procedure utilizes Activin A and thyroid stimulating hormone (TSH) to first induce embryoid body endoderm formation enriched in thyrocyte progenitors. Following dissociating embryoid bodies, thyrocyte progenitors are plated in Matrigel as monolayer cultures that allows thyrocyte progenitors mature to functional thyrocytes. These thyrocytes further maturate to form follicle-like structures expressing and accumulating thyroglobulin that can be secreted into the medium upon TSH stimulation. Thyrocyte differentiation-maturation process is monitored by the expression of essential transcriptional factors and thyrocyte-specific functional genes. Further, the applicability of this system is validated by introducing a siRNA control. Following molecular manipulation, the system can still be guided to differentiate into mature and functional thyrocytes. This system spans a time frame of 14 days, suitable for detailed molecular studies to dissect pathways and molecular players in thyrocytes development and functional maintenance. Full article
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2023

Jump to: 2025, 2024, 2022

19 pages, 1907 KiB  
Article
Role of Coactivator Associated Arginine Methyltransferase 1 (CARM1) in the Regulation of the Biological Function of 1,25-Dihydroxyvitamin D3
by Leila J. Mady, Yan Zhong, Puneet Dhawan and Sylvia Christakos
Cells 2023, 12(10), 1407; https://doi.org/10.3390/cells12101407 - 17 May 2023
Cited by 3 | Viewed by 2217
Abstract
1,25-Dihydroxyvitamin D3 (1,25(OH)2D3), the hormonally active form of vitamin D, activates the nuclear vitamin D receptor (VDR) to mediate the transcription of target genes involved in calcium homeostasis as well as in non-classical 1,25(OH)2D3 actions. In [...] Read more.
1,25-Dihydroxyvitamin D3 (1,25(OH)2D3), the hormonally active form of vitamin D, activates the nuclear vitamin D receptor (VDR) to mediate the transcription of target genes involved in calcium homeostasis as well as in non-classical 1,25(OH)2D3 actions. In this study, CARM1, an arginine methyltransferase, was found to mediate coactivator synergy in the presence of GRIP1 (a primary coactivator) and to cooperate with G9a, a lysine methyltransferase, in 1,25(OH)2D3 induced transcription of Cyp24a1 (the gene involved in the metabolic inactivation of 1,25(OH)2D3). In mouse proximal renal tubule (MPCT) cells and in mouse kidney, chromatin immunoprecipitation analysis demonstrated that dimethylation of histone H3 at arginine 17, which is mediated by CARM1, occurs at Cyp24a1 vitamin D response elements in a 1,25(OH)2D3 dependent manner. Treatment with TBBD, an inhibitor of CARM1, repressed 1,25(OH)2D3 induced Cyp24a1 expression in MPCT cells, further suggesting that CARM1 is a significant coactivator of 1,25(OH)2D3 induction of renal Cyp24a1 expression. CARM1 was found to act as a repressor of second messenger-mediated induction of the transcription of CYP27B1 (involved in the synthesis of 1,25(OH)2D3), supporting the role of CARM1 as a dual function coregulator. Our findings indicate a key role for CARM1 in the regulation of the biological function of 1,25(OH)2D3. Full article
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2022

Jump to: 2025, 2024, 2023

22 pages, 1634 KiB  
Review
Regulation of cGAS Activity and Downstream Signaling
by Bhagwati Joshi, Jagdish Chandra Joshi and Dolly Mehta
Cells 2022, 11(18), 2812; https://doi.org/10.3390/cells11182812 - 8 Sep 2022
Cited by 15 | Viewed by 5409
Abstract
Cyclic GMP-AMP synthase (cGAS) is a predominant and ubiquitously expressed cytosolic onfirmedDNA sensor that activates innate immune responses by producing a second messenger, cyclic GMP-AMP (cGAMP), and the stimulator of interferon genes (STING). cGAS contains a highly disordered N-terminus, which can sense genomic/chromatin [...] Read more.
Cyclic GMP-AMP synthase (cGAS) is a predominant and ubiquitously expressed cytosolic onfirmedDNA sensor that activates innate immune responses by producing a second messenger, cyclic GMP-AMP (cGAMP), and the stimulator of interferon genes (STING). cGAS contains a highly disordered N-terminus, which can sense genomic/chromatin DNA, while the C terminal of cGAS binds dsDNA liberated from various sources, including mitochondria, pathogens, and dead cells. Furthermore, cGAS cellular localization dictates its response to foreign versus self-DNA. Recent evidence has also highlighted the importance of dsDNA-induced post-translational modifications of cGAS in modulating inflammatory responses. This review summarizes and analyzes cGAS activity regulation based on structure, sub-cellular localization, post-translational mechanisms, and Ca2+ signaling. We also discussed the role of cGAS activation in different diseases and clinical outcomes. Full article
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