At a glance
What is it—and why does it matter?
KPV is an endogenous tripeptide (Lysine-Proline-Valine) described as being derived from α-melanocyte-stimulating hormone. Based on the reported cellular findings, KPV was characterized as regulating lipogenic signaling with antioxidant activity.
Sources for this introduction: [1] [2]
This published profile is a reference in progress. Findings retain their source context; missing topics are marked below.
What is it?
A molecule, not a product name.
Identity
KPV is a three–amino acid peptide (Lysine–Proline–Valine) described as endogenous and derived from α-melanocyte-stimulating hormone.
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.
Exact passages, locators, and provenance
- supports · Source-backed record
“This study examined the protective role of Lysine-Proline-Valine (KPV), an endogenous tripeptide derived from α-melanocyte-stimulating hormone”
Lysine-proline-valine peptide attenuates hepatic lipid accumulation through ROS-dependent regulation of the PPARγ pathway in HepG2 cells. · UNLABELLED
pubmed:42064835:95a89fcd1956:95a89fcd1956
Identity
In this review, KPV is included under the α-MSH (alpha-melanocyte-stimulating hormone) category of host defense peptides.
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.
Exact passages, locators, and provenance
- supports · Source-backed record
“alpha-melanocyte-stimulating hormone (α-MSH) (e.g. KPV)”
Host defense peptides as a new drug lead to a strategy for inflammatory bowel disease. · Abstract
pubmed:41241376:9b214e916d89:9b214e916d89
Identity
In this source, KPV is categorized as a synthetic fragment within the broader group of peptides/peptide analogues discussed in sport and bodybuilding.
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.
Exact passages, locators, and provenance
- supports · Source-backed record
“Marketed as more selective and ostensibly safer alternatives, peptides-including growth hormone secretagogues (e.g., Ipamorelin), growth hormone-releasing hormone analogues (e.g., CJC-1295, Sermorelin), and synthetic fragments (e.g., Frag 176-191, KPV)-are promoted for muscle growth, fat metabolism, recovery, and anti-inflammatory effects.”
A new era of doping? Use of peptide and peptide-analog drugs in recreational and professional sport and bodybuilding: a critical review. · Abstract
pubmed:41880199:39c6683290a1:39c6683290a1
Identity
KPV is identified as the tripeptide lysine-proline-valine.
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.
Exact passages, locators, and provenance
- supports · Source-backed record
“lysine-proline-valine (KPV)”
NLRP3 autophagic degradation disruption in melanocytes contributes to vitiligo development. · Abstract
pubmed:40935835:eb98c3ac8765:eb98c3ac8765
Identity
KPV is described as a tripeptide derived from α-melanocyte stimulating hormone (α-MSH).
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.
Exact passages, locators, and provenance
- supports · Source-backed record
“This study investigates the mechanism by which the α-melanocyte stimulating hormone-derived tripeptide, KPV,”
Inhibition of cellular and systemic inflammation cues in human bronchial epithelial cells by melanocortin-related peptides: mechanism of KPV action and a role for MC3R agonists. · BACKGROUND/AIMS
pubmed:22837805:ee49ae914e82:ee49ae914e82
Identity
KPV is an endogenous tripeptide (Lysine-Proline-Valine) described as being derived from α-melanocyte-stimulating hormone.
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.
Exact passages, locators, and provenance
- supports · Source-backed record
“Lysine-Proline-Valine (KPV), an endogenous tripeptide derived from α-melanocyte-stimulating hormone”
KPV attenuates adipogenesis and lipid metabolism through modulation of ROS-mediated AKT/mTORC1/PPARγ signaling. · Abstract
pubmed:42585803:fa3d6f8ca000:fa3d6f8ca000
How does it work?
Target, response, and disposition.
Mechanism
Mechanistically in this model, KPV decreased reactive oxygen species (ROS) generation and was linked to prevention of extracellular signal-regulated kinase activation.
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.
Exact passages, locators, and provenance
- supports · Source-backed record
“Mechanistic analysis revealed that KPV reduced reactive oxygen species generation, thereby preventing activation of extracellular signal-regulated kinase.”
Lysine-proline-valine peptide attenuates hepatic lipid accumulation through ROS-dependent regulation of the PPARγ pathway in HepG2 cells. · UNLABELLED
pubmed:42064835:95a89fcd1956:95a89fcd1956
Mechanism
Mechanistically, KPV’s observed effect correlated with KPV entering the nucleus, stabilising IκBα, and suppressing nuclear translocation of YFP-tagged p65RelA.
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.
Exact passages, locators, and provenance
- supports · Source-backed record
“The KPV effect was associated with its nuclear import, IκBα stabilisation and suppressed nuclear translocation of YFP-tagged p65RelA.”
Inhibition of cellular and systemic inflammation cues in human bronchial epithelial cells by melanocortin-related peptides: mechanism of KPV action and a role for MC3R agonists. · RESULTS
pubmed:22837805:ee49ae914e82:ee49ae914e82
Mechanism
In the reported steatosis conditions, KPV decreased AKT phosphorylation and was linked to inhibition of mTORC1 phosphorylation.
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.
Exact passages, locators, and provenance
- supports · Source-backed record
“KPV also downregulated AKT phosphorylation, leading to inhibition of mTORC1 phosphorylation under hepatic steatosis conditions.”
Lysine-proline-valine peptide attenuates hepatic lipid accumulation through ROS-dependent regulation of the PPARγ pathway in HepG2 cells. · UNLABELLED
pubmed:42064835:95a89fcd1956:95a89fcd1956
Mechanism
In airway epithelium, KPV is stated to suppress NFκB signalling via inhibition of p65RelA nuclear import.
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.
Exact passages, locators, and provenance
- supports · Source-backed record
“KPV and γMSH respectively suppress NFκB signalling in airway epithelium by: i) inhibition of p65RelA nuclear import”
Inhibition of cellular and systemic inflammation cues in human bronchial epithelial cells by melanocortin-related peptides: mechanism of KPV action and a role for MC3R agonists. · CONCLUSION
pubmed:22837805:ee49ae914e82:ee49ae914e82
Mechanism
Based on the reported cellular findings, KPV was characterized as regulating lipogenic signaling with antioxidant activity.
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.
Exact passages, locators, and provenance
- supports · Source-backed record
“These findings suggest that KPV acts as an effective antioxidant regulator of lipogenic signaling”
Lysine-proline-valine peptide attenuates hepatic lipid accumulation through ROS-dependent regulation of the PPARγ pathway in HepG2 cells. · UNLABELLED
pubmed:42064835:95a89fcd1956:95a89fcd1956
Mechanism
The study assessed how KPV affects NFκB signaling induced by TNFα and rhino syncitial virus (RSV) in the 16HBE14o- immortalised human bronchial epithelial cell line.
1 cited source · Study independence not established
Animal or laboratory findings do not establish benefit or safety in people.
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.
Exact passages, locators, and provenance
- supports · Source-backed record
“TNFα and rhino syncitial virus (RSV)-evoked nuclear factor-κB (NFκB) signaling was measured in immortalised human bronchial epithelial cells (16HBE14o-) in response to KPV and γMSH.”
Inhibition of cellular and systemic inflammation cues in human bronchial epithelial cells by melanocortin-related peptides: mechanism of KPV action and a role for MC3R agonists. · METHODS
pubmed:22837805:ee49ae914e82:ee49ae914e82
Mechanism
The SIPPC platform is described as a prodrug-conjugate system for oral delivery that includes PEG for hydrophilicity, a ROS-responsive self-immolative hydrophobic module for inflammation-triggered behavior, and a hydrolyzable scaffold; together these components enable spontaneous micelle-like nanoparticle assembly.
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.
Exact passages, locators, and provenance
- supports · Source-backed record
“Here, we propose a self-immolative peptide prodrug conjugate (SIPPC) platform for inflammation-targeted oral delivery, integrating a hydrophilic polyethylene glycol segment, a reactive oxygen species (ROS)-responsive hydrophobic self-immolative module, and a hydrolyzable scaffold, which collectively enable spontaneous assembly into micelle-like nanoparticles.”
Inflammation-triggered self-immolative conjugates enable oral peptide delivery by overcoming gastrointestinal barriers. · Abstract
pubmed:41533788:1159f2f92387:1159f2f92387
What has been studied?
What the evidence says.
Study findings
In an in vitro HepG2 steatosis model induced by oleic acid, KPV at 100 µg/mL significantly attenuated lipid accumulation.
1 cited source · Study independence not established
Animal or laboratory findings do not establish benefit or safety in people.
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.
Exact passages, locators, and provenance
- supports · Source-backed record
“Treatment with KPV (100 µg/mL) significantly attenuated OA-induced lipid accumulation”
Lysine-proline-valine peptide attenuates hepatic lipid accumulation through ROS-dependent regulation of the PPARγ pathway in HepG2 cells. · UNLABELLED
pubmed:42064835:95a89fcd1956:95a89fcd1956
Study findings
KPV showed dose-dependent inhibitory effects on NFκB signaling, matrix metalloproteinase-9 activity, and chemokine secretion (IL8 and eotaxin).
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.
Exact passages, locators, and provenance
- supports · Source-backed record
“KPV and γMSH evoked a dose-dependent inhibition of NFκB, matrix metalloproteinase-9 activity, IL8 and eotaxin secretion.”
Inhibition of cellular and systemic inflammation cues in human bronchial epithelial cells by melanocortin-related peptides: mechanism of KPV action and a role for MC3R agonists. · RESULTS
pubmed:22837805:ee49ae914e82:ee49ae914e82
Study findings
The abstract reports that orally administered proKPV accumulated in inflamed lung tissue and produced potent anti-inflammatory effects in a mouse acute lung injury model (no quantitative values provided).
1 cited source · Study independence not established
Animal or laboratory findings do not establish benefit or safety in people.
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
Evidence boundary: Applies only to the source-defined population, formulation, dose, and assessment period.
Exact passages, locators, and provenance
- supports · Source-backed record
“Beyond therapeutic effects in the colitis model, oral proKPV substantially accumulated in inflamed lungs and exhibited potent anti-inflammatory efficacy in mice with acute lung injury.”
Inflammation-triggered self-immolative conjugates enable oral peptide delivery by overcoming gastrointestinal barriers. · Abstract
pubmed:41533788:1159f2f92387:1159f2f92387
Risks and interactions
Risks, organized for scanning.
This profile does not yet contain a published summary for this topic. This is a coverage gap, not evidence that no research exists.
Products and regulatory status
Same ingredient. Different records.
This profile does not yet contain a published summary for this topic. This is a coverage gap, not evidence that no research exists.
Administration context
The practical clinical context.
This profile does not yet contain a published summary for this topic. This is a coverage gap, not evidence that no research exists.
Additional research & classification gaps
11 archived statements are kept separate from drug-effect findings. Media studies, economic models, methods, and records with unresolved scope are not used as medical-effect evidence.
Inspect contextual research (11)
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
The authors stated that their findings suggest KPV may be a therapeutic candidate for attenuating hepatocellular steatosis (a suggestion, not a demonstrated clinical effect).
Research context only—not evidence of a treatment effect.
- Lysine-proline-valine peptide attenuates hepatic lipid accumulation through ROS-dependent regulation of the PPARγ pathway in HepG2 cells.
and may hold potential as a therapeutic candidate for attenuating hepatocellular steatosis.
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
In an oleic-acid–treated HepG2 cell model, KPV at 100 µg/mL suppressed expression of fatty acid synthase (FAS), a lipogenesis-related enzyme.
Research context only—not evidence of a treatment effect.
- Lysine-proline-valine peptide attenuates hepatic lipid accumulation through ROS-dependent regulation of the PPARγ pathway in HepG2 cells.
Treatment with KPV (100 µg/mL) significantly attenuated OA-induced lipid accumulation and suppressed FAS expression
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
KPV is reported to have anti-inflammatory activity.
Research context only—not evidence of a treatment effect.
- PepT1-mediated tripeptide KPV uptake reduces intestinal inflammation.
KPV is a tripeptide (Lys-Pro-Val), which possesses anti-inflammatory properties
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
KPV was reported to decrease the expression of key adipogenic markers, including PPARγ and FAS, during adipocyte differentiation.
Research context only—not evidence of a treatment effect.
- KPV attenuates adipogenesis and lipid metabolism through modulation of ROS-mediated AKT/mTORC1/PPARγ signaling.
KPV decreased the expression of key adipogenic markers, including peroxisome proliferator-activated receptor gamma (PPARγ) and fatty acid synthase (FAS).
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
Using anti-inflammatory peptides (including KPV), the engineered SIPPC conjugates are reported to resist GI degradation, traverse mucus, and release payload in a ROS-responsive manner at inflamed tissue sites.
Research context only—not evidence of a treatment effect.
- Inflammation-triggered self-immolative conjugates enable oral peptide delivery by overcoming gastrointestinal barriers.
Using three anti-inflammatory peptides (KPV, Ac-QAW, and IRW), we demonstrated that the engineered conjugates exhibit remarkable GI stability, efficient mucus penetration, and ROS-responsive release at inflamed sites.
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
KPV is a tripeptide composed of the amino acids Lys-Pro-Val.
Research context only—not evidence of a treatment effect.
- PepT1-mediated tripeptide KPV uptake reduces intestinal inflammation.
KPV is a tripeptide (Lys-Pro-Val)
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
In the study background, KPV’s anti-inflammatory mechanism is described as not yet known.
Research context only—not evidence of a treatment effect.
- PepT1-mediated tripeptide KPV uptake reduces intestinal inflammation.
however, its mechanisms of action still remain unknown.
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
KPV was reported to attenuate ROS production during adipocyte differentiation, consistent with modulation of oxidative signaling.
Research context only—not evidence of a treatment effect.
- KPV attenuates adipogenesis and lipid metabolism through modulation of ROS-mediated AKT/mTORC1/PPARγ signaling.
KPV attenuated reactive oxygen species (ROS) production
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
The study concludes that PepT1 functions as a transporter enabling cellular uptake of KPV.
Research context only—not evidence of a treatment effect.
- PepT1-mediated tripeptide KPV uptake reduces intestinal inflammation.
This study indicates tht KPV is transported into cells by PepT1
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
The reported regulatory effect of KPV was accompanied by suppression of fatty acid synthase (FAS) expression.
Research context only—not evidence of a treatment effect.
- KPV attenuates adipogenesis and lipid metabolism through modulation of ROS-mediated AKT/mTORC1/PPARγ signaling.
This regulatory effect was accompanied by suppression of FAS expression.
1 cited source · Study independence not established
How to read this evidence
Sources and study IDs describe provenance, not clinical strength. Several articles can report the same study; one study can support several distinct findings. No clinical strength rating has been assigned here.
1 cited passage across 1 source record. 1 publication group(s) lack a resolved study identity.
The results state that KPV’s activity is mediated through PepT1 in immune cells and intestinal epithelial cells.
Research context only—not evidence of a treatment effect.
- PepT1-mediated tripeptide KPV uptake reduces intestinal inflammation.
We found that KPV acts via PepT1 expressed in immune and intestinal epithelial cells.
Research status + gaps
What still needs better answers?
- No publishable claim yet for: administration, contraindication, interaction, regulatory, safety
- 50 compiled claim(s) withheld by automated assurance: assurance_score_below_0.58 (33), assurance_score_below_0.72 (7), current_regulatory_source_required (10), extraction_ambiguity (50), high_risk_requires_regulatory_or_two_independent_sources (12), no_direct_support (40), proposal_not_staged (2)
These are the limits of this profile, not an exhaustive list of scientific uncertainties.
References + discovery
Open the records yourself.
- PepT1-mediated tripeptide KPV uptake reduces intestinal inflammation. ↗
pubmed · published 2008-01-01 · retrieved 2026-09-04T19:34:25Z
- Inhibition of cellular and systemic inflammation cues in human bronchial epithelial cells by melanocortin-related peptides: mechanism of KPV action and a role for MC3R agonists. ↗
pubmed · published 2012-01-01 · retrieved 2026-09-09T18:02:40Z
- NLRP3 autophagic degradation disruption in melanocytes contributes to vitiligo development. ↗
pubmed · published 2026-02-01 · retrieved 2026-08-27T11:48:55Z
- Host defense peptides as a new drug lead to a strategy for inflammatory bowel disease. ↗
pubmed · published 2025-12-01 · retrieved 2026-08-27T11:48:55Z
- Inflammation-triggered self-immolative conjugates enable oral peptide delivery by overcoming gastrointestinal barriers. ↗
pubmed · published 2026-01-16 · retrieved 2026-08-27T11:48:55Z
- A new era of doping? Use of peptide and peptide-analog drugs in recreational and professional sport and bodybuilding: a critical review. ↗
pubmed · published 2026-07-01 · retrieved 2026-08-26T08:42:26Z
- Lysine-proline-valine peptide attenuates hepatic lipid accumulation through ROS-dependent regulation of the PPARγ pathway in HepG2 cells. ↗
pubmed · published 2026-06-01 · retrieved 2026-08-27T11:48:55Z
- KPV attenuates adipogenesis and lipid metabolism through modulation of ROS-mediated AKT/mTORC1/PPARγ signaling. ↗
pubmed · published 2026-08-09 · retrieved 2026-08-27T11:48:55Z
Publication history and provenance
Version 2 · Automated assessment · 2026-09-09T18:02:40Z
201e396b5bcc0eacff99dcf2f0df25b49b8b95339304f6916dd07955a4e18e12