Sterol regulatory element-binding protein 1 / SREBP-1

duration

Not stated here

evidence_access

Primary PubMed abstract and indexed metadata reviewed. Full-text method details not stated here remain unresolved.

experimental_model

Endothelial cells

exposure

Nattokinase

limitations

A measured null from the confirmation step of a screen, recorded because it bounds which transcripts the screen actually supports.

organism

Endothelial cells

plain_language

SREBF1 messenger RNA appeared in the sequencing screen but was unaffected on Q-PCR confirmation.

primary_references

Nattokinase attenuates endothelial inflammation through the activation of SRF and THBS1. (2024) https://pubmed.ncbi.nlm.nih.gov/38679250/ DOI: 10.1016/j.ijbiomac.2024.131779

route

In vitro

tissue

Cultured endothelium, transcriptional profiling

Nattokinase: what the purified enzyme cleaves, what survives being eaten, and the gap between the two (2026-09-23) · lines 609–609

Original AI-assisted curation built from a supplied entity-first document of 105 entities and 129 claims. Every reference in that document was resolved against live PubMed with its abstract read and its DOI cross-checked on 2026-09-23, and the EFSA novel-food opinion was retrieved and read in full. That check corrected two PMIDs that pointed at unrelated papers, two DOIs, and two papers recorded as carrying no erratum that do carry one; it also reversed three findings the supplied document had stated backwards. Two papers carry a published correction, recorded as such and not as a retraction. Three sources are not indexed in PubMed and are cited by what they have. Laboratory lineages are recorded, so the four papers from one group, the three from another and the two readings of a single applicant dossier cannot be counted as separate lines of support. Study-specific doses, units, populations and limitations retained; activity units are never converted between systems. Not publisher full text. · supports · Endothelial cells · source_derived_draft · unverified_draft

SREBF1 messenger RNA appeared in the sequencing screen but was unaffected on Q-PCR confirmation.

evidence_span

{"source_cache": "artifacts/metformin-research/11602624.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "86e283289def8a6e3e3098d49f321dbcca9a6cd4677ba84f26daf17467179237", "start_char": 0, "end_char": 1390, "text_sha256": "86e283289def8a6e3e3098d49f321dbcca9a6cd4677ba84f26daf17467179237"}

experimental_model

Rat hepatocytes, isolated rat skeletal muscle and metformin-treated rats with an AMPK inhibitor

exposure

Metformin in hepatocytes and in vivo; compound C AMPK inhibition

limitations

The inhibitor experiment supports a requirement for AMPK in these hepatocytes; later work in AMPK-deficient mice reached a different conclusion, recorded separately.

nutrient_topic

Metformin research collection; topical membership is not evidence of a direct clinical effect, and pharmacological exposure is not dietary intake. · Metformin

organism

Rat

plain_language

The switch reaches the transcription factor that drives fat synthesis.

primary_references

[metformin-p11602624] Role of AMP-activated protein kinase in mechanism of metformin action. (2001). https://pubmed.ncbi.nlm.nih.gov/11602624/ DOI: 10.1172/jci13505

tissue_or_cell_type

Liver and skeletal muscle

Metformin: transport, molecular targets, gut mechanisms and nutrient interactions (2026-09-19) · lines 541–552

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rat hepatocytes, isolated rat skeletal muscle and metformin-treated rats with an AMPK inhibitor · source_derived_draft · unverified_draft

### metformin-ampk-srebp1 Activation of AMPK by metformin suppressed expression of SREBP-1, and hepatic lipogenic mRNA and protein were reduced in metformin-treated rats. Condition category: normal nutrient_topic: Metformin research collection; topical membership is not evidence of a direct clinical effect, and pharmacological exposure is not dietary intake. plain_language: The switch reaches the transcription factor that drives fat synthesis. organism: Rat tissue_or_cell_type: Liver and skeletal muscle experimental_model: Rat hepatocytes, isolated rat skeletal muscle and metformin-treated rats with an AMPK inhibitor limitations: The inhibitor experiment supports a requirement for AMPK in these hepatocytes; later work in AMPK-deficient mice reached a different conclusion, recorded separately. exposure: Metformin in hepatocytes and in vivo; compound C AMPK inhibition evidence_span: {"source_cache": "artifacts/metformin-research/11602624.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "86e283289def8a6e3e3098d49f321dbcca9a6cd4677ba84f26daf17467179237", "start_char": 0, "end_char": 1390, "text_sha256": "86e283289def8a6e3e3098d49f321dbcca9a6cd4677ba84f26daf17467179237"} [metformin-p11602624] Role of AMP-activated protein kinase in mechanism of metformin action. (2001). https://pubmed.ncbi.nlm.nih.gov/11602624/ DOI: 10.1172/jci13505

acting_entity

s-allylcysteine

dose

Not specified in accessed abstract

duration

Not specified in accessed abstract

evidence_access

Primary abstract

experimental_comparison

SAC addition; pathway inhibitor comparisons

experimental_model

Free-fatty-acid-treated HepG2 cells

interpretation_status

Source-derived research curation; not independent primary verification

limitations

SREBP-1 isoform and direct molecular target are unresolved in the accessed abstract.

nutrient_topic

S-allylcysteine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · S-allyl-L-cysteine / SAC

organism

Homo sapiens

plain_language

The lipid-production program changed as well as kinase activity.

primary_references

[23465592] S-allyl cysteine attenuates free fatty acid-induced lipogenesis in human HepG2 cells through activation of the AMP-activated protein kinase-dependent pathway. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23465592/ · DOI 10.1016/j.jnutbio.2012.12.006

route

Cell culture

tissue_or_cell_type

Free-fatty-acid-treated HepG2 cells

S-allylcysteine: sulfur signaling, redox responses and cross-nutrient mechanisms (2026-09-20) · lines 203–210

AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Free-fatty-acid-treated HepG2 cells · source_derived_draft · unverified_draft

## s-allylcysteine-srebp The lipid-production program changed as well as kinase activity. SAC reduced SREBP-1 levels and expression of lipogenic targets including ACC and FAS in HepG2 cells. Model: Free-fatty-acid-treated HepG2 cells Limitations: SREBP-1 isoform and direct molecular target are unresolved in the accessed abstract. Evidence access: Primary abstract [23465592] S-allyl cysteine attenuates free fatty acid-induced lipogenesis in human HepG2 cells through activation of the AMP-activated protein kinase-dependent pathway. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23465592/ · DOI 10.1016/j.jnutbio.2012.12.006 Structured context: {"organism": "Homo sapiens", "tissue_or_cell_type": "Free-fatty-acid-treated HepG2 cells", "dose": "Not specified in accessed abstract", "duration": "Not specified in accessed abstract", "route": "Cell culture", "experimental_comparison": "SAC addition; pathway inhibitor comparisons", "acting_entity": "s-allylcysteine", "interpretation_status": "Source-derived research curation; not independent primary verification"}

evidence_span

{"source_cache": "artifacts/acetate-research/16630552.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8e99fe94e17c850602d0da9607212293dfc8d773e356b73ef37c4b071bbeabea", "start_char": 0, "end_char": 914, "text_sha256": "8e99fe94e17c850602d0da9607212293dfc8d773e356b73ef37c4b071bbeabea"}

experimental_model

KK-Ay diabetic mice fed for 8 weeks, with rat hepatocyte experiments

exposure

0.3% dietary acetic acid for 8 weeks; sodium acetate as neutralised acetic acid applied to rat hepatocytes

limitations

The hepatocyte arm used the neutralised salt and still activated AMPK, which does not sit easily beside the human finding that the acid rather than the salt lowered glucose. Both are recorded.

nutrient_topic

Acetic acid research collection; topical membership is not evidence of a direct clinical effect, and the ingested acid is recorded separately from the circulating acetate anion. · Acetic acid

organism

Mouse and rat cells

plain_language

The neutralised salt switched on the liver cell energy sensor directly.

primary_references

[acetate-p16630552] Acetic acid activates hepatic AMPK and reduces hyperglycemia in diabetic KK-A(y) mice. (2006). https://pubmed.ncbi.nlm.nih.gov/16630552/ DOI: 10.1016/j.bbrc.2006.03.176

tissue_or_cell_type

Liver

Acetic acid: the ingested acid, the receptors acetate binds, the acetyl-CoA it becomes, and the acetyl groups that reach histones (2026-09-21) · lines 420–431

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · KK-Ay diabetic mice fed for 8 weeks, with rat hepatocyte experiments · source_derived_draft · unverified_draft

### acetate-sodium-acetate-hepatocyte Sodium acetate, in the form of neutralised acetic acid, directly activated AMPK and lowered the expression of genes such as glucose-6-phosphatase and sterol regulatory element binding protein 1 in rat hepatocytes, leading the authors to conclude that the hypoglycaemic effect might be due to activation of AMPK in the liver. Condition category: normal nutrient_topic: Acetic acid research collection; topical membership is not evidence of a direct clinical effect, and the ingested acid is recorded separately from the circulating acetate anion. plain_language: The neutralised salt switched on the liver cell energy sensor directly. organism: Mouse and rat cells tissue_or_cell_type: Liver experimental_model: KK-Ay diabetic mice fed for 8 weeks, with rat hepatocyte experiments limitations: The hepatocyte arm used the neutralised salt and still activated AMPK, which does not sit easily beside the human finding that the acid rather than the salt lowered glucose. Both are recorded. exposure: 0.3% dietary acetic acid for 8 weeks; sodium acetate as neutralised acetic acid applied to rat hepatocytes evidence_span: {"source_cache": "artifacts/acetate-research/16630552.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "8e99fe94e17c850602d0da9607212293dfc8d773e356b73ef37c4b071bbeabea", "start_char": 0, "end_char": 914, "text_sha256": "8e99fe94e17c850602d0da9607212293dfc8d773e356b73ef37c4b071bbeabea"} [acetate-p16630552] Acetic acid activates hepatic AMPK and reduces hyperglycemia in diabetic KK-A(y) mice. (2006). https://pubmed.ncbi.nlm.nih.gov/16630552/ DOI: 10.1016/j.bbrc.2006.03.176

evidence_span

{"source_cache": "artifacts/alcohol-research/21953514.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "acfcd2656e45aab9abcf367ed27e447001ddaa55ac143e9cc2f24b0958ea15a7", "start_char": 0, "end_char": 1626, "text_sha256": "acfcd2656e45aab9abcf367ed27e447001ddaa55ac143e9cc2f24b0958ea15a7"}

experimental_model

Ethanol-fed mice with hepatic AMPK and SREBP-1 measurement

exposure

Chronic ethanol feeding

limitations

A signalling route to steatosis measured in mice. It sits alongside, not instead of, the redox explanation for fatty liver.

nutrient_topic

Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. · Ethanol

organism

Mouse

plain_language

Alcohol rewires the liver’s fat-building programme through the energy sensor.

primary_references

[alcohol-p21953514] Regulation of hepatic lipin-1 by ethanol: role of AMP-activated protein kinase/sterol regulatory element-binding protein 1 signaling in mice. (2012). https://pubmed.ncbi.nlm.nih.gov/21953514/ DOI: 10.1002/hep.24708

tissue_or_cell_type

Liver

Alcohol: ethanol clearance, acetaldehyde, the channels it binds, organ injury and nutrient collisions (2026-09-21) · lines 436–447

AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Ethanol-fed mice with hepatic AMPK and SREBP-1 measurement · source_derived_draft · unverified_draft

### alcohol-lipin1-srebp Ethanol regulated hepatic lipin-1 through AMP-activated protein kinase and sterol regulatory element-binding protein 1 signalling in mice. Condition category: normal nutrient_topic: Alcohol research collection; topical membership is not evidence of a direct clinical effect, and ethanol is recorded separately from the acetaldehyde it becomes. plain_language: Alcohol rewires the liver’s fat-building programme through the energy sensor. organism: Mouse tissue_or_cell_type: Liver experimental_model: Ethanol-fed mice with hepatic AMPK and SREBP-1 measurement limitations: A signalling route to steatosis measured in mice. It sits alongside, not instead of, the redox explanation for fatty liver. exposure: Chronic ethanol feeding evidence_span: {"source_cache": "artifacts/alcohol-research/21953514.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "acfcd2656e45aab9abcf367ed27e447001ddaa55ac143e9cc2f24b0958ea15a7", "start_char": 0, "end_char": 1626, "text_sha256": "acfcd2656e45aab9abcf367ed27e447001ddaa55ac143e9cc2f24b0958ea15a7"} [alcohol-p21953514] Regulation of hepatic lipin-1 by ethanol: role of AMP-activated protein kinase/sterol regulatory element-binding protein 1 signaling in mice. (2012). https://pubmed.ncbi.nlm.nih.gov/21953514/ DOI: 10.1002/hep.24708