High-yield cell-derived extracellular matrix bioink via macromolecular crowding for versatile 3D bioprinting
Utami SS., Park H., Kim J., Sung A., Choi MJ., Ryoo GH.
Laboratory Study, published in Mater Today Bio (2026) — summary generated from the PubMed abstract.
Evidence from laboratory and animal studies provides groundwork for understanding mechanisms and potential before human studies continue.
- Level A · Stronger Clinical Evidence
- Level B · Emerging clinical evidence with positive signals
- Level C · Early human research exploring benefits
- Level D · Scientific groundwork from lab and animal studies
- Emerging · Emerging topic under active research
This page is generated from the PubMed record. The Thai description is an automated summary of bibliographic fields and the abstract, not a full translation, and is not medical advice.
- Study type
- Laboratory Study
- Journal
- Mater Today Bio (2026)
- Reported sample size
- —
- Source database
- Europe PMC
- PMID
- 42058963
- PMCID
- PMC13123329
- DOI
- 10.1016/j.mtbio.2026.103135
Abstract (original English)
Decellularized extracellular matrix (dECM) is a promising bioink because it replicates the biochemical and structural features of native tissues. However, tissue-derived dECM is limited by restricted availability and potential immunogenicity. To overcome these challenges, we developed a macromolecular crowding (MMC)-enhanced cell-derived extracellular matrix (CD-ECM) bioink with improved yield and biofunctionality. MC3T3-E1 pre-osteoblasts were cultured under MMC conditions, followed by decellularization and enzymatic processing to generate a printable CD-ECM bioink. The MMC strategy markedly increased extracellular matrix (ECM) yield, collagen and glycosaminoglycan (GAG) content, and mechanical stability compared to conventional cultures. The optimized CD-ECM bioink exhibited reliable printability in both extrusion-based and digital light processing (DLP) 3D bioprinting, enabling fabrication of constructs with high shape fidelity and cell viability. Incorporation of α-tricalcium phosphate (α-TCP) further enhanced osteogenic performance, resulting in elevated alkaline phosphatase (ALP) activity, increased calcium deposition, and upregulation of osteogenic markers, including runt-related transcription factor 2 (RUNX2), collagen type I alpha 1(COL1A1), ALP, and osteocalcin (OCN). These findings highlight the synergistic interaction between ECM-derived biochemical cues and α-TCP-m
What this study does not prove
- • This study does not prove SVF is an approved treatment or a replacement for standard care.
- • This is preclinical work; animal or laboratory results cannot be applied to humans.
Evidence level
Evidence from laboratory and animal studies provides groundwork for understanding mechanisms and potential before human studies continue.
How we grade evidenceBrowse all related research
Filter the research library by this study's title keywords, author, or publication year.