Several recent studies have demonstrated that the direct precursor of vitamin D, the calcifediol [25(OH)D], through the binding to the nuclear vitamin D receptor (VDR), is able to regulate the expression of many genes involved in several cellular processes. Considering that itself may function as a VDR ligand, although with a lower affinity, respect than the active form of vitamin D, we have assumed that 25(OH)D by binding the VDR could have a vitamin's D activity such as activating non-genomic pathways, and in particular we selected mesenchymal stem cells derived from human adipose tissue (hADMSCs) for the in vitro assessment of the intracellular Ca mobilization in response to 25(OH)D. Our result reveals the ability of 25(OH)D to activate rapid, non-genomic pathways, such as an increase of intracellular Ca levels, similar to what observed with the biologically active form of vitamin D. hADMSCs loaded with Fluo-4 AM exhibited a rapid and sustained increase in intracellular Ca concentration as a result of exposure to 10 M of 25(OH)D. In this work, we show for the first time the in vitro ability of 25(OH)D to induce a rapid increase of intracellular Ca levels in hADMSCs. These findings represent an important step to better understand the non-genomic effects of vitamin D and its role in endocrine system.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8707877PMC
http://dx.doi.org/10.3390/nu13124227DOI Listing

Publication Analysis

Top Keywords

increase intracellular
12
non-genomic effects
8
active form
8
form vitamin
8
non-genomic pathways
8
ability 25ohd
8
intracellular levels
8
vitamin
5
25ohd
5
vitro non-genomic
4

Similar Publications

The transmembrane protein Synapse Differentiation Induced Gene 4 (SynDIG4) functions as an auxiliary factor of AMPA receptors (AMPARs) and plays a critical role in excitatory synapse plasticity as well as hippocampal-dependent learning and memory. Mice lacking SynDIG4 have reduced surface expression of GluA1 and GluA2 and are impaired in single tetanus-induced long-term potentiation and NMDA receptor (NMDAR)-dependent long-term depression. These findings suggest that SynDIG4 may play an important role in regulating AMPAR distribution through intracellular trafficking mechanisms; however, the precise roles by which SynDIG4 governs AMPAR distribution remain unclear.

View Article and Find Full Text PDF

Unlabelled: Crosstalk between autophagy, host cell death, and inflammatory host responses to bacterial pathogens enables effective innate immune responses that limit bacterial growth while minimizing coincidental host damage. ( ) thwarts innate immune defense mechanisms in alveolar macrophages (AMs) during the initial stages of infection and in recruited bone marrow-derived cells during later stages of infection. However, how protective inflammatory responses are achieved during infection and the variation of the response in different macrophage subtypes remain obscure.

View Article and Find Full Text PDF

Obesity, insulin resistance, and a host of environmental and genetic factors can drive hyperglycemia, causing β-cells to compensate by increasing insulin production and secretion. In type 2 diabetes (T2D), β-cells under these conditions eventually fail. Rare β-cell diseases like congenital hyperinsulinism (HI) also cause inappropriate insulin secretion, and some HI patients develop diabetes.

View Article and Find Full Text PDF

Mammalian red blood cells are generated via a terminal erythroid differentiation pathway culminating in cell polarization and enucleation. Actin filament polymerization is critical for enucleation, but the molecular regulatory mechanisms remain poorly understood. We utilized publicly available RNA-seq and proteomics datasets to mine for actin-binding proteins and actin- nucleation factors differentially expressed during human erythroid differentiation and discovered that a focal adhesion protein-Tensin-1-dramatically increases in expression late in differentiation.

View Article and Find Full Text PDF

Unlabelled: Endocytic recycling of transmembrane proteins is essential to cell signaling, ligand uptake, protein traffic and degradation. The intracellular domains of many transmembrane proteins are ubiquitylated, which promotes their internalization by clathrin-mediated endocytosis. How might this enhanced internalization impact endocytic uptake of transmembrane proteins that lack ubiquitylation? Recent work demonstrates that diverse transmembrane proteins compete for space within highly crowded endocytic structures, suggesting that enhanced internalization of one group of transmembrane proteins may come at the expense of other groups.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!