Vitamin A, Retinoic Acid / BACE/β-secretase Cancer Research Results

VitA,RetA, Vitamin A, Retinoic Acid: Click to Expand ⟱
Features:
Retinoic acid is a naturally occurring derivative of vitamin A (retinol).

Retinoic acid is produced in the body from dietary vitamin A. Vitamin A can be ingested in two primary forms:
• Preformed vitamin A (retinol and its esters) found in animal products like liver, dairy, and fish.
• Provitamin A carotenoids (such as beta-carotene) found in colorful fruits and vegetables. Once ingested, these compounds are converted into retinol, which can then be oxidized to retinal and further oxidized to retinoic acid.

All-trans retinoic acid (ATRA) is a key component in the treatment of acute promyelocytic leukemia (APL). In APL, ATRA induces the differentiation of malignant promyelocytes into mature granulocytes, leading to clinical remission.

-Retinoic acid can have antioxidant properties
-High levels of retinoic acid have been associated with increased ROS production and oxidative stress
-The potential prooxidant action may contribute to its anti-cancer effects by inducing oxidative damage in cancer cells, thereby enhancing apoptosis.
BACE/β-secretase, β-site APP-cleaving enzyme: Click to Expand ⟱
Source:
Type:
BACE stands for β-site APP-cleaving enzyme, also known as β-secretase. It plays a central role in the pathogenesis of Alzheimer’s disease by initiating the production of amyloid-β (Aβ) peptides, the primary components of amyloid plaques found in the brains of individuals with AD.
-inhibiting BACE1 reduces Aβ production.

BACE1 - Beta-Site APP Cleaving Enzyme 1 / β-Secretase 1

Abbreviation: BACE1, β-secretase, β-secretase 1

Type: Aspartyl protease / amyloidogenic APP-processing enzyme

Function: BACE1 is a membrane-associated aspartyl protease that performs the initial β-secretase cleavage of amyloid precursor protein (APP). This cleavage generates soluble APPβ and the membrane-bound C99 fragment, which is subsequently cleaved by γ-secretase to produce amyloid-β peptides including Aβ40 and Aβ42.

Alzheimer's Disease: ↑ Increased BACE1 expression or enzymatic activity promotes amyloidogenic APP processing and increases amyloid-β production. Elevated BACE1 activity has been reported in Alzheimer's disease and contributes to Aβ accumulation, plaque formation, synaptic dysfunction, and disease progression. BACE1 inhibition reduces Aβ production, although clinical BACE1 inhibitors have been limited by adverse effects related to the enzyme's normal physiological functions.
Scientific Papers found: Click to Expand⟱
4313- VitA,RetA,    Unraveling the molecular mechanisms of vitamin deficiency in Alzheimer's disease pathophysiology
- Review, AD, NA
*neuroP↑, memory↑, *Inflam↓, *neuroG↑, *cognitive↑, *Aβ↓, p‑tau↓, *BACE/β-secretase↓,

Showing Research Papers: 1 to 1 of 1

* indicates research on normal cells as opposed to diseased cells
Total Research Paper Matches: 1

Pathway results for Effect on Cancer / Diseased Cells:


Synaptic & Neurotransmission(tgid=18) ⓘ

p‑tau↓, 1,  

Functional Outcomes(tgid=23) ⓘ

memory↑, 1,  
Total Targets: 2

Pathway results for Effect on Normal Cells:


Proliferation, Differentiation & Cell State(tgid=12) ⓘ

neuroG↑, 1,  

Immune & Inflammatory Signaling(tgid=16) ⓘ

Inflam↓, 1,  

Protein Aggregation(tgid=19) ⓘ

Aβ↓, 1,   BACE/β-secretase↓, 1,  

Functional Outcomes(tgid=23) ⓘ

cognitive↑, 1,   neuroP↑, 1,  
Total Targets: 6

Scientific Paper Hit Count for: BACE/β-secretase, β-site APP-cleaving enzyme
Query results interpretion may depend on "conditions" listed in the research papers.
Such Conditions may include : 
  -low or high Dose
  -format for product, such as nano of lipid formations
  -different cell line effects
  -synergies with other products 
  -if effect was for normal or cancerous cells

Filter Conditions: Pro/AntiFlg:%  IllCat:%  CanType:%  Cells:%  prod#:290  Target#:1349  State#:%  Dir#:%
  wNotes=0  sortOrder:rid,rpid

 

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