ArticleInternational journal of molecular sciences2026
Low-Molecular-Weight Salmon Collagen Peptides Promote Extracellular Matrix Gene (ECM) Expression in BJ Fibroblasts.
Article in International journal of molecular sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Salmon skin, a high-volume by-product of seafood processing, offers a circular-bioeconomy route to sustainable, value-added ingredients. This study aimed to generate low-molecular-weight collagen peptides (LMWCPs) from salmon skin using a stepwise enzymatic process and to evaluate their safety and pro-extracellular-matrix (ECM) activity in human BJ fibroblasts. LMWCPs were produced by sequential hydrolysis (alcalase/papain, then collagenase) and characterized as low-molecular-weight peptide preparations with a mean dispersed particle diameter of approximately 117 nm. LMWCPs display negatively charged peptide dispersions with a mass centered around ~1 kDa. Cytocompatibility (MTT) showed no toxicity up to 1.5 mg/mL over 48 h. Gene expression by reverse transcription-quantitative polymerase chain reaction (RT-qPCR) revealed a robust, dose-dependent ECM response: collagen type I alpha 1 chain (COL1A1) increased by approximately 7-fold, with additional rises of 5-6-fold in versican (VCAN) levels and modest increases in elastin (ELN) and transforming growth factor-β (TGF-β). These findings provide an exploratory process-to-phenotype link between the two-step hydrolysis process, physicochemical characteristics of the resulting LMWCPs, and changes in ECM-related gene expression in BJ fibroblasts. Overall, this study demonstrates that salmon skin LMWCPs were cytocompatible within the tested concentration range and modulated several ECM-related genes, providing a preliminary basis for future protein-level, functional, and translational evaluation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.