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Scientific reports2025; 15(1); 18021; doi: 10.1038/s41598-025-01820-7

Integrated proteomics highlights functional activation induced by advanced-platelet rich fibrin plus (A-PRF +) in primary equine fibroblasts.

Abstract: Wounds are common in equine practice, and often lead to complications such as infections, delayed healing and hypertrophic scarring, which can be costly and difficult to manage. Developing affordable and effective treatments has become an increasingly important focus in veterinary research. Equine advanced-platelet-rich fibrin plus (A-PRF+) demonstrates regenerative properties comparable to its human counterpart, but cellular-level investigations exploring its molecular mechanisms remain limited. This study aimed to investigate the in vitro effects of equine A-PRF + on primary fibroblast cell cultures. The secretome analysis of A-PRF + revealed a complex protein profile involved in matrix remodelling, cell proliferation, and inflammation. Treatment with this platelet concentrate resulted in increased cell proliferation, enhanced migration, and significant changes in cell cycle progression compared to control groups. Reactive oxygen species production and organelles metabolism stimulation were observed, indicating active cellular responses, as well as an increase in genes and proteins associated with cell proliferation and wound regeneration. Proteomic analysis of treated fibroblasts confirmed the differential expression of key proteins associated with extracellular matrix dynamics and tissue regeneration processes. These findings provide insights into the molecular profile and functional responses of equine fibroblasts exposed to A-PRF + , contributing to our understanding of its cellular effects, supporting further exploration of this product in regenerative medicine applications.
© 2025. The Author(s).
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Publication Date: 2025-05-23 PubMed ID: 40410219PubMed Central: PMC12102165DOI: 10.1038/s41598-025-01820-7Google Scholar: Lookup
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  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article investigates the regenerative properties and molecular mechanisms of equine advanced-platelet-rich fibrin plus (A-PRF+) on primary fibroblast cell cultures to improve the treatment process for wounds in equines.

Objective of the Research

  • The study aims to explore the cellular effects of equine A-PRF+ on primary fibroblast cell cultures, a specific type of cell associated with wound healing and tissue regeneration processes. It also aims to understand the molecular mechanisms triggering these effects, thereby improving wound healing in equines.

Methodology

  • To analyze the effects of A-PRF+, the researchers conducted a secretome analysis which revealed a complex protein profile involved in various key processes such as cell proliferation, matrix remodelling and inflammation.
  • A-PRF+ was then applied to primary fibroblast cell cultures as a treatment. The progression of cell proliferation, migration and cell cycles were compared with control groups to assess the effects of the treatment.

Findings

  • The A-PRF+ treatment led to increased cell proliferation and enhanced migration, indicating its positive effects on the growth and mobility of cells. Significant alterations were observed in cell cycle progression, implicating that A-PRF+ could accelerate the cell division and growth necessary for wound healing.
  • On a cellular level, the production of reactive oxygen species and stimulation of organelles’ metabolism were notable. These processes are typically activated in response to cell damage, suggesting that A-PRF+ may potentially improve the cells’ ability to repair and recover.
  • A significant increase in the expression of genes and proteins associated with cell proliferation and wound regeneration was recorded after the treatment with A-PRF+. Proteomic analysis highlighted the varied expression of key proteins involved in maintaining the structure and function of tissues (extracellular matrix dynamics) and tissue regeneration processes.

Implications

  • The results offer valuable insights into the molecular profile and functional responses of equine cells exposed to A-PRF+, thereby contributing to a better understanding of its cellular effects. The findings support the benefits of A-PRF+ in promoting critical processes pertinent to wound healing and tissue regeneration.
  • Given the positive outcomes, this study opens avenues for further exploration of A-PRF+ in regenerative medicine applications, thereby potentially improving the treatment processes for wounds in equines.

Cite This Article

APA
Miranda MR, Montano C, Golino V, de Chiara M, Del Prete C, Pepe G, De Biase D, Ciaglia T, Bertamino A, Campiglia P, Sommella E, Vestuto V, Pasolini MP. (2025). Integrated proteomics highlights functional activation induced by advanced-platelet rich fibrin plus (A-PRF +) in primary equine fibroblasts. Sci Rep, 15(1), 18021. https://doi.org/10.1038/s41598-025-01820-7

Publication

Scientific reports
ISSN: 2045-2322
NlmUniqueID: 101563288
Country: England
Language: English
Volume: 15
Issue: 1
Pages: 18021

Researcher Affiliations

Miranda, Maria Rosaria
  • Department of Pharmacy, University of Salerno, 84084, Fisciano, SA, Italy.
  • NBFC-National Biodiversity Future Center, 90133, Palermo, Italy.
Montano, Chiara
  • Department of Veterinary Medicine and Animal Production, University of Naples Federico II, Naples, Italy.
Golino, Valentina
  • Department of Pharmacy, University of Salerno, 84084, Fisciano, SA, Italy.
  • National PhD Program in "RNA Therapeutics and Gene Therapy", Napoli, Italy.
de Chiara, Mariaelena
  • Department of Veterinary Medicine and Animal Production, University of Naples Federico II, Naples, Italy.
Del Prete, Chiara
  • Department of Veterinary Medicine and Animal Production, University of Naples Federico II, Naples, Italy.
Pepe, Giacomo
  • Department of Pharmacy, University of Salerno, 84084, Fisciano, SA, Italy.
  • NBFC-National Biodiversity Future Center, 90133, Palermo, Italy.
De Biase, Davide
  • Department of Pharmacy, University of Salerno, 84084, Fisciano, SA, Italy.
Ciaglia, Tania
  • Department of Pharmacy, University of Salerno, 84084, Fisciano, SA, Italy.
Bertamino, Alessia
  • Department of Pharmacy, University of Salerno, 84084, Fisciano, SA, Italy.
Campiglia, Pietro
  • Department of Pharmacy, University of Salerno, 84084, Fisciano, SA, Italy.
Sommella, Eduardo
  • Department of Pharmacy, University of Salerno, 84084, Fisciano, SA, Italy.
Vestuto, Vincenzo
  • Department of Pharmacy, University of Salerno, 84084, Fisciano, SA, Italy. vvestuto@unisa.it.
Pasolini, Maria Pia
  • Department of Veterinary Medicine and Animal Production, University of Naples Federico II, Naples, Italy.

MeSH Terms

  • Animals
  • Horses
  • Fibroblasts / metabolism
  • Fibroblasts / drug effects
  • Fibroblasts / cytology
  • Proteomics / methods
  • Cell Proliferation / drug effects
  • Platelet-Rich Fibrin / metabolism
  • Cells, Cultured
  • Wound Healing / drug effects
  • Reactive Oxygen Species / metabolism
  • Cell Movement / drug effects
  • Proteome

Grant Funding

  • CUP: J97G22000400006 / Project IR0000028-"Pathogen readiness platform for CERIC-ERIC Upgrade" PRP@CERIC

Conflict of Interest Statement

Declarations. Competing interests: The authors declare no competing interests.

References

This article includes 92 references
  1. Naik B, Karunakar P, Jayadev M, Marshal VR. Role of Platelet rich fibrin in wound healing: A critical review.. J. Conserv. Dent. 16, 284–293 (2013).
    pmc: PMC3740636pubmed: 23956527doi: 10.4103/0972-0707.114344google scholar: lookup
  2. Buonocore M et al. Exploiting the features of short peptides to recognize specific cell surface markers.. Int. J. Mol. Sci. 24, 15610 (2023).
    pmc: PMC10650159pubmed: 37958593doi: 10.3390/ijms242115610google scholar: lookup
  3. Song P, He D, Ren S, Fan L, Sun J. Platelet-rich fibrin in dentistry.. J. Appl. Biomater. Funct. Mater. .
    pubmed: 39588592doi: 10.1177/22808000241299588google scholar: lookup
  4. Crisci A et al. Standardized protocol proposed for clinical use of L-PRF and the use of L-PRF Wound Box®.. J. Unexplored Med. Data. 2, 77–87 (2017).
    doi: 10.20517/2572-8180.2017.17google scholar: lookup
  5. Masuki H et al. Growth factor and pro-inflammatory cytokine contents in platelet-rich plasma (PRP), plasma rich in growth factors (PRGF), advanced platelet-rich fibrin (A-PRF), and concentrated growth factors (CGF).. Int. J. Implant Dent. 2, 19 (2016).
    pmc: PMC5005757pubmed: 27747711doi: 10.1186/s40729-016-0052-4google scholar: lookup
  6. Pavlovic V, Ciric M, Jovanovic V, Trandafilovic M, Stojanovic P. Platelet-rich fibrin: Basics of biological actions and protocol modifications.. Open Med. (Wars) 16, 446–454 (2021).
    pmc: PMC7985567pubmed: 33778163doi: 10.1515/med-2021-0259google scholar: lookup
  7. Narayanaswamy R et al. Evolution and clinical advances of platelet-rich fibrin in musculoskeletal regeneration.. Bioengineering 10, 58 (2023).
    pmc: PMC9854731pubmed: 36671630doi: 10.3390/bioengineering10010058google scholar: lookup
  8. Stefanescu A et al. Assessing the effectiveness of A-PRF+ for treating periodontal defects: A prospective interventional pilot study involving smokers.. Medicina 60, 1897 (2024).
    pmc: PMC11597093pubmed: 39597082doi: 10.3390/medicina60111897google scholar: lookup
  9. Pitzurra L, Jansen IDC, de Vries TJ, Hoogenkamp MA, Loos BG. Effects of L-PRF and A-PRF+ on periodontal fibroblasts in in vitro wound healing experiments.. J. Periodontal. Res. 55, 287–295 (2020).
    pmc: PMC7154757pubmed: 31782171doi: 10.1111/jre.12714google scholar: lookup
  10. Santos Pereira VB, Barbirato DDS, Lago CAPD, Vasconcelos BCDE. The effect of advanced platelet-rich fibrin in tissue regeneration in reconstructive and graft surgery: Systematic review.. J. Craniofac. Surg. 34, 1217–1221 (2023).
    pubmed: 37143188doi: 10.1097/scs.0000000000009328google scholar: lookup
  11. Liu YH et al. Advanced platelet-rich fibrin (A-PRF) has an impact on the initial healing of gingival regeneration after tooth extraction.. J. Oral Biosci. 64, 141–147 (2022).
    pubmed: 34808363doi: 10.1016/j.job.2021.11.001google scholar: lookup
  12. Kosmidis K, Ehsan K, Pitzurra L, Loos B, Jansen I. An in vitro study into three different PRF preparations for osteogenesis potential.. J. Periodontal. Res. 58, 483–492 (2023).
    pubmed: 36942454doi: 10.1111/jre.13116google scholar: lookup
  13. Ghanaati S et al. Advanced platelet-rich fibrin: A new concept for cell-based tissue engineering by means of inflammatory cells.. J. Oral Implantol. 40, 679–689 (2014).
    pubmed: 24945603doi: 10.1563/aaid-joi-d-14-00138google scholar: lookup
  14. Caston SS. Wound care in horses.. Vet. Clin. N. Am. Equine Pract. 28, 83–100 (2012).
    pubmed: 22640581doi: 10.1016/j.cveq.2012.01.001google scholar: lookup
  15. Spink J, Moyer DC. Defining the public health threat of food fraud.. J. Food Sci. 76, R157–R163 (2011).
    pubmed: 22416717doi: 10.1111/j.1750-3841.2011.02417.xgoogle scholar: lookup
  16. Wang X, Yang Y, Zhang Y, Miron RJ. Fluid platelet-rich fibrin stimulates greater dermal skin fibroblast cell migration, proliferation, and collagen synthesis when compared to platelet-rich plasma.. J. Cosmet. Dermatol. 18, 2004–2010 (2019).
    pubmed: 30990574doi: 10.1111/jocd.12955google scholar: lookup
  17. Dachlan I et al. The effect of platelet-rich fibrin on normal dermal fibroblast proliferation after mitomycin-c treatment: An in vitro study.. Ann. Med. Surg. (Lond.) 62, 473–476 (2021).
    pmc: PMC7873574pubmed: 33604035doi: 10.1016/j.amsu.2021.01.093google scholar: lookup
  18. Marescal O, Cheeseman IM. Cellular mechanisms and regulation of quiescence.. Dev. Cell 55, 259–271 (2020).
    pmc: PMC7665062pubmed: 33171109doi: 10.1016/j.devcel.2020.09.029google scholar: lookup
  19. Pagliara V et al. Myogenesis in C2C12 cells requires phosphorylation of ATF6α by p38 MAPK.. Biomedicines 11, 1457 (2023).
    pmc: PMC10216283pubmed: 37239128doi: 10.3390/biomedicines11051457google scholar: lookup
  20. Matsuzaki S et al. Physiological ER stress mediates the differentiation of fibroblasts.. PLoS ONE 10, e0123578 (2015).
    pmc: PMC4416017pubmed: 25928708doi: 10.1371/journal.pone.0123578google scholar: lookup
  21. Miron RJ et al. Injectable platelet rich fibrin (i-PRF): Opportunities in regenerative dentistry?. Clin. Oral Investig. 21, 2619–2627 (2017).
    pubmed: 28154995doi: 10.1007/s00784-017-2063-9google scholar: lookup
  22. Farooq M, Khan AW, Kim MS, Choi S. The role of fibroblast growth factor (FGF) signaling in tissue repair and regeneration.. Cells 10, 3242 (2021).
    pmc: PMC8622657pubmed: 34831463doi: 10.3390/cells10113242google scholar: lookup
  23. Kajanne R et al. EGF-R regulates MMP function in fibroblasts through MAPK and AP-1 pathways.. J. Cell Physiol. 212, 489–497 (2007).
    pubmed: 17348021doi: 10.1002/jcp.21041google scholar: lookup
  24. Ruangpanit N et al. Gelatinase A (MMP-2) activation by skin fibroblasts: Dependence on MT1-MMP expression and fibrillar collagen form.. Matrix Biol. 20, 193–203 (2001).
    pubmed: 11420151doi: 10.1016/s0945-053x(01)00135-4google scholar: lookup
  25. Johnson BZ, Stevenson AW, Prêle CM, Fear MW, Wood FM. The role of IL-6 in skin fibrosis and cutaneous wound healing.. Biomedicines 8, 101 (2020).
    pmc: PMC7277690pubmed: 32365896doi: 10.3390/biomedicines8050101google scholar: lookup
  26. Balaji S et al. Interleukin-10-mediated regenerative postnatal tissue repair is dependent on regulation of hyaluronan metabolism via fibroblast-specific STAT3 signaling.. FASEB J. 31, 868–881 (2017).
    pmc: PMC5295728pubmed: 27903619doi: 10.1096/fj.201600856rgoogle scholar: lookup
  27. Li Y et al. HB-EGF-induced IL-8 secretion from airway epithelium leads to lung fibroblast proliferation and migration.. BMC Pulm. Med. 21, 347 (2021).
    pmc: PMC8572483pubmed: 34742261doi: 10.1186/s12890-021-01726-wgoogle scholar: lookup
  28. Hamill KJ et al. Alpha actinin-1 regulates cell-matrix adhesion organization in keratinocytes: Consequences for skin cell motility.. J. Invest. Dermatol. 135, 1043–1052 (2015).
    pmc: PMC4366307pubmed: 25431851doi: 10.1038/jid.2014.505google scholar: lookup
  29. Dias HB, de Oliveira JR, Donadio MVF, Kimura S. Fructose-1,6-bisphosphate prevents pulmonary fibrosis by regulating extracellular matrix deposition and inducing phenotype reversal of lung myofibroblasts.. PLoS ONE 14, e0222202 (2019).
    pmc: PMC6738633pubmed: 31509566doi: 10.1371/journal.pone.0222202google scholar: lookup
  30. Liang ZH et al. GLI family zinc finger protein 2 promotes skin fibroblast proliferation and DNA damage repair by targeting the miR-200/ataxia telangiectasia mutated axis in diabetic wound healing.. Kaohsiung J. Med. Sci. 40, 422–434 (2024).
    pmc: PMC11895666pubmed: 38385859doi: 10.1002/kjm2.12813google scholar: lookup
  31. Kwon Y. YAP/TAZ as molecular targets in skeletal muscle atrophy and osteoporosis.. Aging Dis. 16, 299–320 (2024).
    pmc: PMC11745433pubmed: 38502585doi: 10.14336/ad.2024.0306google scholar: lookup
  32. Manganelli V et al. Role of ERLINs in the control of cell fate through lipid rafts.. Cells 10, 2408 (2021).
    pmc: PMC8470593pubmed: 34572057doi: 10.3390/cells10092408google scholar: lookup
  33. Soares CS, Babo PS, Faria S, Pires MA, Carvalho PP. Standardized Platelet-Rich Fibrin (PRF) from canine and feline origin: An analysis on its secretome pattern and architectural structure.. Cytokine 148, 155695 (2021).
    pubmed: 34496340doi: 10.1016/j.cyto.2021.155695google scholar: lookup
  34. Al-Sharabi N et al. Proteomic analysis of mesenchymal stromal cells secretome in comparison to leukocyte- and platelet-rich fibrin.. Int. J. Mol. Sci. 24, 13057 (2023).
    pmc: PMC10487446pubmed: 37685865doi: 10.3390/ijms241713057google scholar: lookup
  35. Yaprak E, Kasap M, Akpinar G, Islek EE, Sinanoglu A. Abundant proteins in platelet-rich fibrin and their potential contribution to wound healing: An explorative proteomics study and review of the literature.. J. Dent. Sci. 13, 386–395 (2018).
    pmc: PMC6388803pubmed: 30895150doi: 10.1016/j.jds.2018.08.004google scholar: lookup
  36. Takaya K, Okabe K, Ishigami A. Actin cable formation and epidermis–dermis positional relationship during complete skin regeneration.. Sci. Rep. 12, 15913 (2022).
    pmc: PMC9508246pubmed: 36151111doi: 10.1038/s41598-022-18175-ygoogle scholar: lookup
  37. Gurtner GC, Werner S, Barrandon Y, Longaker MT. Wound repair and regeneration.. Nature 453, 314–321 (2008).
    pubmed: 18480812doi: 10.1038/nature07039google scholar: lookup
  38. Vondriska TM, Pass JM, Ping P. Scaffold proteins and assembly of multiprotein signaling complexes.. J. Mol. Cell Cardiol. 37, 391–397 (2004).
    pubmed: 15276009doi: 10.1016/j.yjmcc.2004.04.021google scholar: lookup
  39. Tracy LE, Minasian RA, Caterson EJ. Extracellular matrix and dermal fibroblast function in the healing wound.. Adv. Wound Care 5(3), 119–136 (2016).
    pmc: PMC4779293pubmed: 26989578
  40. Jolly LA et al. Fibroblast-mediated collagen remodeling within the tumor microenvironment facilitates progression of thyroid cancers driven by BrafV600E and Pten loss.. Cancer Res. 76, 1804–1813 (2016).
    pmc: PMC4873339pubmed: 26818109doi: 10.1158/0008-5472.can-15-2351google scholar: lookup
  41. Engström W, Ward A, Moorwood K. The role of scaffold proteins in JNK signalling.. Cell Prolif. 43, 56–66 (2010).
    pmc: PMC6496263pubmed: 19922489doi: 10.1111/j.1365-2184.2009.00654.xgoogle scholar: lookup
  42. Tang DD, Gerlach BD. The roles and regulation of the actin cytoskeleton, intermediate filaments and microtubules in smooth muscle cell migration.. Respir. Res. 18, 54 (2017).
    pmc: PMC5385055pubmed: 28390425doi: 10.1186/s12931-017-0544-7google scholar: lookup
  43. Etienne-Manneville S. Actin and microtubules in cell motility: Which one is in control?. Traffic 5, 470–477 (2004).
    pubmed: 15180824doi: 10.1111/j.1600-0854.2004.00196.xgoogle scholar: lookup
  44. Nobes CD, Hall A. Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia.. Cell 81, 53–62 (1995).
    pubmed: 7536630doi: 10.1016/0092-8674(95)90370-4google scholar: lookup
  45. Spiering D, Hodgson L. Dynamics of the Rho-family small GTPases in actin regulation and motility.. Cell Adh. Migr. 5, 170–180 (2011).
    pmc: PMC3084983pubmed: 21178402doi: 10.4161/cam.5.2.14403google scholar: lookup
  46. Ma Y et al. Histone demethylases in autophagy and inflammation.. Cell Commun. Signal. 23, 24 (2025).
    pmc: PMC11727796pubmed: 39806430doi: 10.1186/s12964-024-02006-wgoogle scholar: lookup
  47. Ulukan B, Sila Ozkaya Y, Zeybel M. Advances in the epigenetics of fibroblast biology and fibrotic diseases.. Curr. Opin. Pharmacol. 49, 102–109 (2019).
    pubmed: 31731224doi: 10.1016/j.coph.2019.10.001google scholar: lookup
  48. Kirk T, Ahmed A, Rognoni E. Fibroblast memory in development, homeostasis and disease.. Cells 10, 2840 (2021).
    pmc: PMC8616330pubmed: 34831065doi: 10.3390/cells10112840google scholar: lookup
  49. Liu S et al. Fetal bovine serum, an important factor affecting the reproducibility of cell experiments.. Sci. Rep. 13, 1942 (2023).
    pmc: PMC9894865pubmed: 36732616doi: 10.1038/s41598-023-29060-7google scholar: lookup
  50. Yaneselli K et al. Impact of different formulations of platelet lysate on proliferative and immune profile of equine mesenchymal stromal cells.. Front. Vet. Sci. 11, 1410855 (2024).
    pmc: PMC11330840pubmed: 39161460doi: 10.3389/fvets.2024.1410855google scholar: lookup
  51. Santos A, Sheguti TM. Platelet-rich plasma (PRP) as an alternative to fetal bovine serum (FBS) in the culture of mesenchymal stem cells in cell therapy.. J. Stem Cell Res. Ther. 7, 26–28 (2022).
    doi: 10.15406/jsrt.2022.07.00153google scholar: lookup
  52. He L, Lin Y, Hu X, Zhang Y, Wu H. A comparative study of platelet-rich fibrin (PRF) and platelet-rich plasma (PRP) on the effect of proliferation and differentiation of rat osteoblasts in vitro.. Oral Surg. Oral Med. Oral Pathol. Oral Radiol. Endod. 108, 707–713 (2009).
    pubmed: 19836723doi: 10.1016/j.tripleo.2009.06.044google scholar: lookup
  53. Atsu N, Ekinci-Aslanoglu C, Kantarci-Demirkiran B, Nuhoglu F. The comparison of platelet-rich plasma versus injectable platelet rich fibrin in facial skin rejuvenation.. Dermatol. Ther. .
    doi: 10.1155/2023/3096698google scholar: lookup
  54. Coronado M et al. Physiological mitochondrial fragmentation is a normal cardiac adaptation to increased energy demand.. Circ. Res. 122, 282–295 (2018).
    pmc: PMC5775047pubmed: 29233845doi: 10.1161/circresaha.117.310725google scholar: lookup
  55. Guo T et al. Mitochondrial fission and bioenergetics mediate human lung fibroblast durotaxis.. JCI Insight. 8, e157348 (2023).
    pmc: PMC9870082pubmed: 36422990doi: 10.1172/jci.insight.157348google scholar: lookup
  56. Yu T, Wang L, Zhang L, Deuster PA. Mitochondrial fission as a therapeutic target for metabolic diseases: Insights into antioxidant strategies.. Antioxidants (Basel) 12, 1163 (2023).
    pmc: PMC10295595pubmed: 37371893doi: 10.3390/antiox12061163google scholar: lookup
  57. Sterczała B et al. Impact of APRF+ in combination with autogenous fibroblasts on release growth factors, collagen, and proliferation and migration of gingival fibroblasts: An in vitro study.. Materials (Basel) 15, 796 (2022).
    pmc: PMC8836484pubmed: 35160741doi: 10.3390/ma15030796google scholar: lookup
  58. Bagdadi K et al. Reduction of relative centrifugal forces increases growth factor release within solid platelet-rich-fibrin (PRF)-based matrices: A proof of concept of LSCC (low speed centrifugation concept).. Eur. J. Trauma Emerg. Surg. 45, 467–479 (2019).
    pmc: PMC6579868pubmed: 28324162doi: 10.1007/s00068-017-0785-7google scholar: lookup
  59. Chen K et al. Regulation of inflammation by members of the formyl-peptide receptor family.. J. Autoimmun. 85, 64–77 (2017).
    pmc: PMC5705339pubmed: 28689639doi: 10.1016/j.jaut.2017.06.012google scholar: lookup
  60. Ding H et al. Transferrin receptor 1 ablation in satellite cells impedes skeletal muscle regeneration through activation of ferroptosis.. J. Cachexia Sarcopenia Muscle. 12, 746–768 (2021).
    pmc: PMC8200440pubmed: 33955709doi: 10.1002/jcsm.12700google scholar: lookup
  61. Czapiga M, Gao JL, Kirk A, Lekstrom-Himes J. Human platelets exhibit chemotaxis using functional N-formyl peptide receptors.. Exp. Hematol. 33, 73–84 (2005).
    pubmed: 15661400doi: 10.1016/j.exphem.2004.09.010google scholar: lookup
  62. Ward JH, Kushner JP, Kaplan J. Transferrin receptors of human fibroblasts. Analysis of receptor properties and regulation.. Biochem. J. 208, 19–26 (1982).
    pmc: PMC1153923pubmed: 6297460doi: 10.1042/bj2080019google scholar: lookup
  63. Kanaya S, Nemoto E, Ebe Y, Somerman MJ, Shimauchi H. Elevated extracellular calcium increases fibroblast growth factor-2 gene and protein expression levels via a cAMP/PKA dependent pathway in cementoblasts.. Bone 47, 564–572 (2010).
    pubmed: 20542497doi: 10.1016/j.bone.2010.05.042google scholar: lookup
  64. Izard T, Brown DT. Mechanisms and functions of vinculin interactions with phospholipids at cell adhesion sites.. J. Biol. Chem. 291, 2548–2555 (2016).
    pmc: PMC4742724pubmed: 26728462doi: 10.1074/jbc.r115.686493google scholar: lookup
  65. Giannone G. Super-resolution links vinculin localization to function in focal adhesions.. Nat. Cell Biol. 17, 845–847 (2015).
    pubmed: 26123111
  66. Bays JL, DeMali KA. Vinculin in cell–cell and cell–matrix adhesions.. Cell Mol. Life Sci. 74, 2999–3009 (2017).
    pmc: PMC5501900pubmed: 28401269doi: 10.1007/s00018-017-2511-3google scholar: lookup
  67. Tochio T, Tanaka H, Nakata S, Hosoya H. Fructose-1,6-bisphosphate aldolase A is involved in HaCaT cell migration by inducing lamellipodia formation.. J. Dermatol. Sci. 58, 123–129 (2010).
    pubmed: 20362419doi: 10.1016/j.jdermsci.2010.02.012google scholar: lookup
  68. Kusakabe T, Motoki K, Hori K. Mode of interactions of human aldolase isozymes with cytoskeletons.. Arch. Biochem. Biophys. 344, 184–193 (1997).
    pubmed: 9244396doi: 10.1006/abbi.1997.0204google scholar: lookup
  69. Harris SJ, Winzor DJ. Enzyme kinetic evidence of active-site involvement in the interaction between aldolase and muscle myofibrils.. Biochim. Biophys. Acta 91, 121–126 (1987).
    pubmed: 3790595doi: 10.1016/0167-4838(87)90279-2google scholar: lookup
  70. Geng S et al. Deletion of TECRL promotes skeletal muscle repair by up-regulating EGR2.. Proc. Natl. Acad. Sci. U. S. A. 121, e2317495121 (2024).
    pmc: PMC11126978pubmed: 38753506doi: 10.1073/pnas.2317495121google scholar: lookup
  71. Micera A et al. Toll-like receptors and tissue remodeling: The pro/cons recent findings.. J. Cell Physiol. 231, 531–544 (2016).
    pubmed: 26248215doi: 10.1002/jcp.25124google scholar: lookup
  72. Hermida-Nogueira L, Blanco J, García Á. Secretome profile of leukocyte-platelet-rich fibrin (L-PRF) membranes.. Methods Mol. Biol. 2628, 207–219 (2023).
    pubmed: 36781788doi: 10.1007/978-1-0716-2978-9_14google scholar: lookup
  73. Broeckx S et al. Allogenic mesenchymal stem cells as a treatment for equine degenerative joint disease: A pilot study.. Curr. Stem Cell Res. Ther. 9, 497–503 (2014).
    pubmed: 25175766doi: 10.2174/1574888x09666140826110601google scholar: lookup
  74. Fujioka-Kobayashi M et al. Optimized platelet-rich fibrin with the low-speed concept: Growth factor release, biocompatibility, and cellular response.. J. Periodontol. 88, 112–121 (2017).
    pubmed: 27587367doi: 10.1902/jop.2016.160443google scholar: lookup
  75. Covelli V et al. Salicylic acid release from syndiotactic polystyrene staple fibers.. Molecules 28, 5095 (2023).
    pmc: PMC10343414pubmed: 37446756doi: 10.3390/molecules28135095google scholar: lookup
  76. Ogorevc J, Lapanja T, Poklukar K, Tominšek N, Dovč P. Establishment of primary keratinocyte culture from horse tissue biopsates.. Acta Agric. Slov. 106, 87–91 (2015).
    doi: 10.14720/aas.2015.106.2.3google scholar: lookup
  77. Madelaire CB, Klink AC, Israelsen WJ, Hindle AG. Fibroblasts as an experimental model system for the study of comparative physiology.. Comp. Biochem. Physiol. Part B: Biochem. Mol. Biol. .
    pmc: PMC9215708pubmed: 35321853doi: 10.1016/j.cbpb.2022.110735google scholar: lookup
  78. Di Prima G et al. Green extraction of polyphenols from waste bentonite to produce functional antioxidant excipients for cosmetic and pharmaceutical purposes: A waste-to-market approach.. Antioxidants 11, 2493 (2022).
    pmc: PMC9774313pubmed: 36552701doi: 10.3390/antiox11122493google scholar: lookup
  79. Jung KM. Betaine enhances the cellular survival via mitochondrial fusion and fission factors, MFN2 and DRP1.. Anim. Cells Syst. (Seoul) 22, 289–298 (2018).
    pmc: PMC6171430pubmed: 30460110doi: 10.1080/19768354google scholar: lookup
  80. Carbone D et al. Metabolomics-assisted discovery of a new anticancer GLS-1 inhibitor chemotype from a nortopsentin-inspired library: From phenotype screening to target identification.. Eur. J. Med. Chem. 234, 114233 (2022).
    pubmed: 35286926doi: 10.1016/j.ejmech.2022.114233google scholar: lookup
  81. Franken NA, Rodermond HM, Stap J, Haveman J, van Bree C. Clonogenic assay of cells in vitro.. Nat. Protoc. 1, 2315–2319 (2006).
    pubmed: 17406473doi: 10.1038/nprot.2006.339google scholar: lookup
  82. Rapa SF et al. Plumericin protects against experimental inflammatory bowel disease by restoring intestinal barrier function and reducing apoptosis.. Biomedicines 9, 67 (2021).
    pmc: PMC7826791pubmed: 33445622doi: 10.3390/biomedicines9010067google scholar: lookup
  83. Ostacolo C et al. Identification of an indol-based multi-target kinase inhibitor through phenotype screening and target fishing using inverse virtual screening approach.. Eur. J. Med. Chem. 167, 61–75 (2019).
    pubmed: 30763817doi: 10.1016/j.ejmech.2019.01.066google scholar: lookup
  84. De Vita S et al. 2-Substituted 1,5-benzothiazepine-based HDAC inhibitors exert anticancer activities on human solid and acute myeloid leukemia cell lines.. Bioorg. Med. Chem. 93, 117444 (2023).
    pubmed: 37611334doi: 10.1016/j.bmc.2023.117444google scholar: lookup
  85. Aquino G et al. Optimization of microwave-assisted extraction of antioxidant compounds from spring onion leaves using Box-Behnken design.. Sci. Rep. 13, 14923 (2023).
    pmc: PMC10493223pubmed: 37691048doi: 10.1038/s41598-023-42303-xgoogle scholar: lookup
  86. Izdebska M et al. Lidocaine induces protective autophagy in rat C6 glioma cell line.. Int. J. Oncol. 54, 1099–1111 (2019).
    pmc: PMC6365045pubmed: 30569147doi: 10.3892/ijo.2018.4668google scholar: lookup
  87. Wang YY, Lee KT, Lim MC, Choi JH. TRPV1 antagonist DWP05195 induces ER stress-dependent apoptosis through the ROS-p38-CHOP pathway in human ovarian cancer cells.. Cancers 12, 1702 (2020).
    pmc: PMC7352786pubmed: 32604833doi: 10.3390/cancers12061702google scholar: lookup
  88. Amodio G et al. PERK-mediated unfolded protein response activation and oxidative stress in PARK20 fibroblasts.. Front. Neurosci. 13, 673 (2019).
    pmc: PMC6610533pubmed: 31316342doi: 10.3389/fnins.2019.00673google scholar: lookup
  89. Colarusso C et al. Activation of the AIM2 receptor in circulating cells of post-COVID-19 patients with signs of lung fibrosis is associated with the release of IL-1α, IFN-α and TGF-β.. Front. Immunol. 13, 934264 (2022).
    pmc: PMC9277546pubmed: 35844548doi: 10.3389/fimmu.2022.934264google scholar: lookup
  90. Trentini M et al. Link between organic nanovescicles from vegetable kingdom and human cell physiology: Intracellular calcium signalling.. J. Nanobiotechnol. 22, 68 (2024).
    pmc: PMC10875884pubmed: 38369472doi: 10.1186/s12951-024-02340-8google scholar: lookup
  91. Viode A et al. A simple, time- and cost-effective, high-throughput depletion strategy for deep plasma proteomics.. Sci. Adv. 9, eadf9717 (2023).
    pmc: PMC10058233pubmed: 36989362doi: 10.1126/sciadv.adf9717google scholar: lookup
  92. Capaci V et al. The deep proteomics approach identified extracellular vesicular proteins correlated to extracellular matrix in type one and two endometrial cancer.. Int. J. Mol. Sci. 25, 4650 (2024).
    pmc: PMC11083465pubmed: 38731868doi: 10.3390/ijms25094650google scholar: lookup
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