Fibrillin-1 Inhibits Early Adipogenic Commitment Via αvβ3 Integrin Signaling.
Siddiqui IFS., Nelea V., Tiedemann K., Brazeau E., Agourame S., Reinhardt DP.
Animal Study, published in J Mol Biol (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
- Animal Study
- Journal
- J Mol Biol (2026)
- Country
- Netherlands
- Reported sample size
- —
- Source database
- PubMed
- PMID
- 42303090
- DOI
- 10.1016/j.jmb.2026.169912
Abstract (original English)
Extracellular fibrillin-1 is present in many tissues, including adipose tissue. Mutations in fibrillin-1 cause Marfan syndrome, paradoxically presenting with either low body fat at younger ages or frequently increased adiposity in older individuals. The latter correlated well with data obtained with the Fbn1 mgR/mgR mice, which show that global fibrillin-1 deficiency leads to sex-dependent obesity by negatively regulating early adipogenic stem cell differentiation. However, the underlying cell receptors and mechanisms remained unknown. Here, we used recombinant fibrillin-1 fragments harboring either an active RGD integrin-binding motif (rFBN1-N-RGD) or an inactive RGA motif (rFBN1-N-RGA) and tested their roles in adipogenic differentiation with primary mesenchymal progenitors isolated from bone marrow or fat tissue, as well as with adipogenic 3T3-L1 cells. rFBN1-N-RGD inhibited adipogenic differentiation in all cell models when present during the early commitment phase but not during the maturation phase, whereas the rFBN1-N-RGA control was inactive. siRNA-mediated gene silencing or pharmacologic inhibition of integrin αvβ3, but not α5β1, rescued rFBN1-N-RGD-dependent inhibition of adipogenic differentiation. Fibrillin-1 engagement of integrin αvβ3 triggered activation of the downstream focal adhesion kinase (Fak)-Src kinase (Src) signaling cascade, driving extracellular signal
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.
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