Aspirin -acetylsalicylic acid / Vim Cancer Research Results

ASA, Aspirin -acetylsalicylic acid: Click to Expand ⟱
Features: nonsteroidal anti-inflammatory drug (NSAID)
Aspirin irreversibly inhibits COX-1 and modifies the enzymatic activity of COX-2. COX-2 normally produces prostanoids, most of which are proinflammatory.

-Aspirin irreversibly inhibits the enzyme cyclooxygenase-1 (COX-1). This inhibition reduces the production of thromboxane A₂, a potent promoter of platelet aggregation.
-low-dose aspirin is frequently used for the prevention of cardiovascular events such as heart attacks and strokes in individuals at risk.

Aspirin (acetylsalicylic acid; ASA) — an acetylating salicylate NSAID that irreversibly inhibits cyclooxygenase (COX) enzymes, producing anti-inflammatory, analgesic/antipyretic, and (at low dose) antiplatelet effects via sustained suppression of platelet thromboxane A₂ (TXA₂). It is a small-molecule oral drug (OTC and prescription formulations; immediate-release and enteric-coated). Standard abbreviations include ASA and “low-dose aspirin” (typically 75–100 mg/day in many guidelines/trials). In cancer biology, the most industry-relevant hypotheses center on platelet COX-1/TXA₂ suppression (metastasis/immune effects) plus COX-2/PGE₂ suppression (inflammatory tumor microenvironment), with clinical signals that are context- and biomarker-dependent.

Primary mechanisms (ranked):

  1. Platelet COX-1 acetylation → TXA₂ ↓ → platelet activation/aggregation ↓ (systemic antiplatelet axis; downstream effects on thrombosis and platelet–tumor biology)
  2. COX-2 activity modulation/inhibition → prostanoid signaling (including PGE₂) ↓ (anti-inflammatory and tumor-microenvironment effects; more dose/context dependent than platelet COX-1)
  3. Platelet-derived TXA₂ immunosuppression axis ↓ (T-cell suppression relieved; metastasis permissiveness reduced) (context-dependent; mechanistically linked to platelet COX-1/TXA₂)
  4. Immune checkpoint/inflammation coupling: PD-L1 ↓ and inflammatory mediators ↓ (model- and tissue-dependent; partly COX/prostanoid-linked and partly epigenetic/transcriptional)
  5. Pro-apoptotic balance shift in some models (BAX ↑, Bcl-2 ↓, apoptosis ↑) (secondary; model-dependent)

Bioavailability / PK relevance: Oral absorption is generally rapid (formulation-dependent). Aspirin itself is short-lived in plasma due to rapid deacetylation to salicylate, while platelet COX-1 inhibition persists for the platelet lifespan (functional persistence despite short plasma exposure). Salicylate elimination can become dose-dependent (capacity-limited) at higher doses, extending effective half-life and increasing toxicity/bleeding risk.

In-vitro vs systemic exposure relevance: Many anti-proliferative or direct tumor-cell cytotoxic effects reported in vitro occur at concentrations not typically achieved with low-dose antiplatelet regimens; clinically plausible cancer effects at low dose are more consistent with platelet/immune/microenvironment mechanisms than direct tumor cytotoxicity.

Clinical evidence status: Strong clinical use exists for antiplatelet indications (cardiovascular secondary prevention and other clinician-directed uses). For primary prevention, contemporary guidance restricts initiation due to bleeding risk (age/risk stratified). For oncology, evidence supports chemopreventive associations (strongest for colorectal cancer in long-term use) and emerging biomarker-stratified adjuvant signals (e.g., PI3K-pathway–altered CRC recurrence reduction in a large randomized setting), but this is not universal across populations and may be age- and context-dependent.

**There is debate about the reduced cancer risk effects of aspirin when used long term (10yr). The evidence is stronger for CRC especially for those with IBD. Evidence is more debatable for those 70yrs old. Also there are claims about the anti-Metastasis capabilites of aspirin for those with cancer.

Mechanistic and translation-relevant axes for aspirin (ASA) in cancer

Rank Pathway / Axis Cancer Cells Normal Cells TSF Primary Effect Notes / Interpretation
1 Platelet COX-1 → TXA₂ Indirect: platelet shielding of CTCs ↓; platelet-assisted extravasation/metastatic seeding ↓ (context-dependent) Platelet aggregation ↓; hemostasis capacity ↓ (bleeding risk ↑) P Antiplatelet state via irreversible COX-1 acetylation High mechanistic centrality at low dose because platelets cannot resynthesize COX-1; effects persist beyond plasma aspirin exposure.
2 COX-2 → PGE₂ inflammatory tumor microenvironment Inflammatory prostanoid signaling ↓; pro-tumor inflammation ↓ (dose/context dependent) GI mucosal protection ↓ (ulcer/bleeding risk ↑); renal prostaglandin effects (risk in susceptible patients) R Anti-inflammatory prostanoid suppression COX-2 modulation is less selectively targeted than platelet COX-1 at “low-dose”; relevance increases with higher systemic exposure.
3 Platelet TXA₂ → T-cell suppression axis Anti-metastatic immunity ↑ (T-cell effector function ↑; metastasis permissiveness ↓) Immune modulation ↔ (context-dependent) R Release of T-cell suppression linked to platelet TXA₂ Mechanistic bridge between antiplatelet action and metastasis control; aligns with platelet-first hypothesis for low-dose aspirin.
4 PI3K-pathway–altered CRC recurrence signal Recurrence risk ↓ in PI3K-altered localized CRC (biomarker-stratified benefit) Systemic bleeding risk ↑ remains G Genotype-linked clinical leverage (adjuvant context) Represents actionable stratification logic: benefit concentrated in molecular subsets rather than pan-CRC.
5 Immune checkpoint coupling: PD-L1 PD-L1 ↓ (model-dependent) → immune evasion ↓ (context-dependent) Immune effects ↔ G Potential immunomodulatory adjunct axis Reported in specific tumor models via transcription/epigenetic regulators; translation likely tumor-type and context dependent.
6 Apoptosis balance Apoptosis ↑; BAX ↑; Bcl-2 ↓ (model-dependent) Cell stress/irritation ↔ (context-dependent) G Secondary pro-death signaling in some models Often requires higher concentrations than antiplatelet dosing; treat as supportive rather than primary for real-world low-dose exposure.
7 Clinical Translation Constraint Benefit heterogeneity ↑ (tumor subtype, age, bleeding risk, concomitant therapy) GI bleeding ↑; hemorrhagic stroke risk ↑ (baseline-dependent); hypersensitivity in susceptible patients G Therapeutic window constrained by bleeding and population selection Major limiter for preventive use in older adults; drug–drug interactions (anticoagulants/other NSAIDs) and peri-procedural management are practical constraints.

TSF legend: P: 0–30 min   R: 30 min–3 hr   G: >3 hr
Vim, Vimentin: Click to Expand ⟱
Source:
Type:
Vimentin, a major constituent of the intermediate filament family of proteins, is ubiquitously expressed in normal mesenchymal cells and is known to maintain cellular integrity and provide resistance against stress. Vimentin is overexpressed in various epithelial cancers, including prostate cancer, gastrointestinal tumors, tumors of the central nervous system, breast cancer, malignant melanoma, and lung cancer. Vimentin’s overexpression in cancer correlates well with accelerated tumor growth, invasion, and poor prognosis; however, the role of vimentin in cancer progression remains obscure.

In many epithelial-derived tumors (carcinomas), elevated Vimentin expression is often observed in cancer cells that have undergone EMT. This upregulation is characteristic of a shift toward a mesenchymal state, which is associated with reduced cell–cell adhesion and increased motility. Vimentin expression is also noted in the tumor stroma, reflecting the presence and activation of mesenchymal cells such as cancer-associated fibroblasts (CAFs). This dual expression can contribute to the remodeling of the tumor microenvironment.
The degree of Vimentin expression may vary depending on the tumor type, grade, and stage. More aggressive and advanced tumors tend to show higher levels of Vimentin expression.

High Vimentin expression has been correlated with poor clinical outcomes in several cancers, including breast, colorectal, prostate, and lung cancers.
Elevated Vimentin levels are typically associated with higher tumor grade, increased invasiveness, enhanced metastatic potential, and a greater risk of recurrence.
As a component of the EMT signature, high Vimentin expression can serve as an indicator of a more aggressive tumor phenotype and is often associated with reduced overall survival.
- vimentin up-regulation is often used as a marker of EMT in cancer



Scientific Papers found: Click to Expand⟱
5415- ASA,    The Anti-Metastatic Role of Aspirin in Cancer: A Systematic Review
- Review, Var, NA
TumMeta↓, COX1↓, TXA2↓, AntiAg↑, EMT↓, TumCMig↓, TumCI↓, AMPK↑, cMyc↓, PGE2↓, Dose↑, RadioS↑, PD-L1↓, E-cadherin↑, EMT↓, Slug↓, Vim↓, Twist↓, MMP2↓, MMP9↓, other↑,

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:


Core Metabolism/Glycolysis ⓘ

AMPK↑, 1,   cMyc↓, 1,  

Transcription & Epigenetics ⓘ

other↑, 1,  

Proliferation, Differentiation & Cell State ⓘ

EMT↓, 2,  

Migration ⓘ

AntiAg↑, 1,   E-cadherin↑, 1,   MMP2↓, 1,   MMP9↓, 1,   Slug↓, 1,   TumCI↓, 1,   TumCMig↓, 1,   TumMeta↓, 1,   Twist↓, 1,   Vim↓, 1,  

Angiogenesis & Vasculature ⓘ

TXA2↓, 1,  

Immune & Inflammatory Signaling ⓘ

COX1↓, 1,   PD-L1↓, 1,   PGE2↓, 1,  

Drug Metabolism & Resistance ⓘ

Dose↑, 1,   RadioS↑, 1,  

Clinical Biomarkers ⓘ

PD-L1↓, 1,  
Total Targets: 21

Pathway results for Effect on Normal Cells:


Total Targets: 0

Scientific Paper Hit Count for: Vim, Vimentin
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#:1  Target#:336  State#:%  Dir#:1
  wNotes=0  sortOrder:rid,rpid

 

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