NiasCin

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BIOLOGICAL MECHANISM NOTES:

The electrostatic bonds between Niacin and Ascorbic Acid are fascinating.

The known challenge with vitamin C is overcoming its lability, particularly its degradation mainly due to the hyrolytic opening of the lactone ring in ascorbic acid. When Niacin (nicotinic acid) and Ascorbic Acid form a complex, they establish holy-like electrostatic interactions between specific charged groups of the respective molecules.

These interactions are characterized by the formation of:

1. Hydrogen bonds: Niacin’s carboxylic group (-COOH) forms hydrogen bonds with Ascorbic Acid’s enol hydroxyl groups (-OH), which completely stabilizes this susceptible lactone ring of Vitamin C.
2. Ionic interactions: Niacin’s pyridine ring also interacts with Ascorbic Acid’s negatively charged carboxylate group (-COO-), forming an ionic bond.
3. π-π stacking: The aromatic rings of Niacin and Ascorbic Acid can engage in π-π stacking interactions, which further contribute to the improved stability of their complex.

These electrostatic bonds, which thermodynamically favorably start forming in the presence of the two compounds in solution [i.e., strictly PURE, ideally deionized water; or alternatively, for higher yield, hot methanol] at equimolecular amounts, uniquely armor the supreme nutrients to be appropriately realized and utilized.

Essentially, these very pinpoint bonds are meant to form for very significant reasons! To recap…

1. Stabilize the complex: The interactions between Niacin and Ascorbic Acid help to maintain the complex’s structure and stability.
2. Enhance bioavailability: The complexation improves the solubility and bioavailability of both Niacin and Ascorbic Acid.
3. Influence biological activity: The electrostatic bonds govern the binding of the complex to specific biomolecules, including  protein receptors governing energy metabolism homeostasis through the living organism.

Understanding the electrostatic bonds between Niacin and Ascorbic Acid can provide valuable insights into their biochemical interactions and therapeutic applications.

The complexation of Niacin and Ascorbic Acid is highlighted by primarily:

1. Enhance binding affinity: The electrostatic bonds formed advance the binding affinity of the complex to GPR109A, in this way promoting the preservation and restoration of mitochondrial flux at a cellular level towards ushering in homeostatic function systematically.
2. Modulate binding specificity: The complex exhibits allosteric and conformational binding generated through the unification of niacin and ascorbic acid that is innate in enabling transactivation of signaling pathways downstream to GPR109A.

Vitamin C plays a defining role in regulating and restoring the expression of GPR109A, the receptor for Niacin ubiquitous through all living cells. This means that by way of (in-tact) Vitamin C, a higher echelon of beneficial impact is bestowed to Niacin; and vice-versa.

In the case of therapeutic intervention, by upregulating GPR109A, vitamin C potentiates the effects of Niacin, by way of:

1. Enhanced Niacin-mediated benefits: Increased GPR109A expression amplifies the beneficial effects of Niacin on lipid metabolism, inflammation, antioxidant defenses, and beyond — to futuristic levels.
2. Improved Niacin bioavailability: Upregulation of GPR109A boosts the bioavailability of Niacin and thereby its utilization.

The resurrection of GPR109A by Vitamin C evokes a complex interplay of signaling pathways and molecular interactions.

Here’s a simplified overview:

1. Vitamin C binds to specific receptors or proteins, triggering a signaling cascade.
2. This cascade activates transcription factors, such as nuclear factor erythroid 2-related factor 2 (Nrf2), which regulate gene expression.
3. Nrf2, in turn, binds to the antioxidant response element (ARE) in the promoter region of the GPR109A gene.
4. This binding event enhances the transcription of the GPR109A gene, leading to increased expression of the receptor.

The increased availability of GPR109A receptors on the cell surface allows for more efficient binding and signaling by Niacin, leading to enhanced biological effects.

Other molecular mechanisms, such as epigenetic modifications, microRNA regulation, and post-translational modifications, likely also contribute to the Vitamin C-mediated upregulation of GPR109A.

The Vitamin C-mediated upregulation of GPR109A involves a complex interplay of signaling pathways, including:

1. Nrf2-ARE pathway: Vitamin C activates Nrf2, which binds to the ARE in the GPR109A promoter, enhancing transcription.
2. PI3K-Akt pathway: Vitamin C stimulates the PI3K-Akt signaling cascade, leading to increased Nrf2 activity and GPR109A expression.
3. MAPK pathway: Vitamin C activates MAPK kinases, which phosphorylate and activate transcription factors that regulate GPR109A expression.

In terms of molecular interactions, Vitamin C binds to specific proteins, such as:

1. Vitamin C receptors: Vitamin C binds to specific receptors, like the sodium-dependent vitamin C transporter 2 (SVCT2), which triggers signaling cascades.
2. Protein kinases: Vitamin C interacts with protein kinases, like PI3K and MAPK, to activate signaling pathways.

The upregulation of GPR109A by Vitamin C also involves epigenetic modifications, such as:

1. Histone modifications: Vitamin C influences histone modifications, namely acetylation and methylation, to regulate chromatin structure and GPR109A transcription.
2. DNA methylation: Vitamin C affects DNA methylation patterns, influencing regulation of GPR109A expression.

These molecular mechanisms and interactions contribute to the complex regulation of GPR109A by Vitamin C.

Epigenetic modifications play a crucial role in GPR109A expression. Vitamin C influences epigenetic marks, such as:

1. Histone acetylation: Vitamin C increases histone acetylation, particularly at the GPR109A promoter, promoting chromatin relaxation and increased transcription.
2. DNA demethylation: Vitamin C promotes DNA demethylation, reducing methylation at specific CpG sites near the GPR109A promoter, which enhances transcription.

Protein-protein interactions are also essential for the regulation of GPR109A. Vitamin C influences the interaction between:

1. Nrf2 and Keap1: Vitamin C disrupts the Nrf2-Keap1 complex, allowing Nrf2 to translocate to the nucleus and activate GPR109A transcription.
2. PI3K and Akt: Vitamin C enhances the interaction between PI3K and Akt, increasing Akt phosphorylation and activation of downstream targets, most notably GPR109A.

Other proteins, including:

1. Vitamin C transporters (SVCTs): Vitamin C binds to SVCTs, influencing their activity and regulating Vitamin C uptake and distribution.
2. Histone-modifying enzymes: Vitamin C interacts with histone-modifying enzymes, like histone acetyltransferases (HATs) and histone deacetylases (HDACs), to regulate chromatin structure and GPR109A transcription.

These protein-protein interactions and epigenetic modifications are pivotal in the regulation of GPR109A by Vitamin C.
One of the key epigenetic mechanisms underlying the Vitamin C-mediated regulation of GPR109A is the modulation of histone modifications.

Of note, Vitamin C has been shown to:

1. Increase histone acetylation: Vitamin C treatment leads to increased acetylation of histones H3 and H4, specifically at the GPR109A promoter.
2. Enhance histone methylation: Vitamin C also influences histone methylation patterns, with increased trimethylation of histone H3 lysine 4 (H3K4me3) near the GPR109A promoter.

These histone modifications contribute to chromatin relaxation and greater accessibility of the GPR109A promoter to transcription factors.

In terms of protein-protein interactions, Vitamin C influences the binding of transcription factors to the GPR109A promoter.

For example:

1. Nrf2 binding: Vitamin C enhances the binding of Nrf2 to the GPR109A promoter, leading to increased transcriptional activation.
2. p300/CBP binding: Vitamin C also governs recruitment of the histone acetyltransferase p300/CBP to the GPR109A promoter, further enhancing histone acetylation and transcriptional activation.

These protein-protein interactions and epigenetic modifications work together to regulate GPR109A expression in response to Vitamin C.

Transcription factors:

1. Nrf2: As mentioned earlier, Nrf2 plays a crucial role in regulating GPR109A expression in recogntion of Vitamin C.
2. p53: Vitamin C also influences p53 binding to the GPR109A promoter, leading to increased transcriptional activation.
3. NF-κB: Vitamin C can modulate NF-κB binding to the GPR109A promoter, influencing inflammation-related gene expression.

Chromatin remodeling complexes:

1. SWI/SNF complex: Vitamin C treatment restores the SWI/SNF chromatin remodeling complex to the GPR109A promoter, facilitating chromatin relaxation and transcriptional activation.
2. NuRD complex: Vitamin C also influences the binding of the NuRD chromatin remodeling complex to the GPR109A promoter, regulating chromatin compaction and transcriptional repression.

Other proteins:

1. HDACs: Vitamin C can inhibit the activity of histone deacetylases (HDACs), leading to increased histone acetylation and transcriptional activation.
2. DNMTs: Vitamin C may also influence DNA methyltransferase (DNMT) activity, anchoring DNA methylation patterns and gene expression.

These transcription factors, chromatin remodeling complexes, and other proteins correspond to regulate GPR109A expression in response to Vitamin C.

Signaling pathways:

1. PI3K/Akt pathway: Vitamin C activates the PI3K/Akt signaling pathway, with ensuing phosphorylation and activation of Akt, which in turn regulates GPR109A expression.
2. MAPK/ERK pathway: Vitamin C also activates the MAPK/ERK signaling pathway, catalyzing phosphorylation and activation of ERK, which regulates GPR109A expression.
3. NF-κB pathway: Vitamin C influences the NF-κB signaling pathway, modulating inflammation-related gene expression and homeostasis, distinctively GPR109A.

Molecular mechanisms:

1. Redox regulation: Vitamin C’s antioxidant properties help regulate the redox state of the cell, influencing the activity of redox-sensitive transcription factors and signaling pathways that regulate GPR109A.
2. Epigenetic regulation: Vitamin C influences epigenetic marks, such as histone modifications and DNA methylation, to modulate GPR109A expression.
3. MicroRNA regulation: Vitamin C may also regulate microRNAs that target GPR109A, pivoting its expression.

Transcriptional regulation:

1. Transcription factor binding: Vitamin C influences the binding of transcription factors, such as Nrf2, p53, and NF-κB, to the GPR109A promoter, regulating its expression.
2. Chromatin remodeling: Vitamin C treatment enables improvements in chromatin structure, allowing for increased accessibility of the GPR109A promoter to transcription factors.

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