Keratoconus molecular alterations revealed by Fourier-transform infrared spectroscopy.

Λεπτομέρειες βιβλιογραφικής εγγραφής
Τίτλος: Keratoconus molecular alterations revealed by Fourier-transform infrared spectroscopy.
Συγγραφείς: Oszczędłowski P; Chair and Department of General and Pediatric Ophthalmology, Medical University of Lublin, Lublin, Poland; Doctoral School, Medical University of Lublin, Chodźki 7 Street, Lublin, 20-093, Poland. Electronic address: pawelosz99@gmail.com., Dróżdż A; Faculty of Physics and Applied Computer Science, AGH University of Krakow, Krakow, Poland., Rejdak R; Chair and Department of General and Pediatric Ophthalmology, Medical University of Lublin, Lublin, Poland., Rękas K; Chair and Department of General and Pediatric Ophthalmology, Medical University of Lublin, Lublin, Poland; Doctoral School, Medical University of Lublin, Chodźki 7 Street, Lublin, 20-093, Poland., Nassasra A; Chair and Department of General and Pediatric Ophthalmology, Medical University of Lublin, Lublin, Poland., Paduch R; Department of Virology and Immunology, Maria Curie-Skłodowska University (MCSU), Lublin, Poland., Toro M; Chair and Department of General and Pediatric Ophthalmology, Medical University of Lublin, Lublin, Poland; Eye Clinic, Public Health Department, University of Naples Federico II, Naples, Italy., Roszkowska AM; Ophthalmology Clinic, Department of Biomedical Sciences, University Hospital of Messina, Messina, Italy; Ophthalmology Department, Faculty of Medicine, University Andrzej Frycz Modrzewski, Krakow, Poland., Gupanova M; Department of Ophthalmology, Military Hospital, Kharkiv, Ukraine., Denysiuk O; Shupyk National Healthcare University of Ukraine, Kyiv, Ukraine., Gagoś M; Department of Cell Biology, Maria Curie-Sklodowska University, Akademicka 19, Lublin, 20-033, Poland., Chorągiewicz T; Chair and Department of General and Pediatric Ophthalmology, Medical University of Lublin, Lublin, Poland.
Πηγή: Experimental eye research [Exp Eye Res] 2026 Oct; Vol. 271, pp. 111117. Date of Electronic Publication: 2026 Jun 09.
Τύπος έκδοσης: Journal Article
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: Academic Press Country of Publication: England NLM ID: 0370707 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1096-0007 (Electronic) Linking ISSN: 00144835 NLM ISO Abbreviation: Exp Eye Res Subsets: MEDLINE
Imprint Name(s): Publication: London : Academic Press
Original Publication: London.
Ιατρικοί όροι (MeSH): Keratoconus*/metabolism , Keratoconus*/surgery , Keratoconus*/diagnosis , Cornea*/metabolism , Cornea*/pathology , Collagen*/metabolism, Spectroscopy, Fourier Transform Infrared/methods ; Proteoglycans/metabolism ; Biomarkers/metabolism ; Humans ; Keratoplasty, Penetrating ; Female ; Adult ; Male ; Middle Aged
Περίληψη: Purpose: In this study, we aimed to identify infrared spectral markers specific to keratoconic corneas obtained during penetrating keratoplasty, based on characteristic molecular alterations associated with the disease.
Methods: Corneal tissues obtained from patients with advanced keratoconus undergoing penetrating keratoplasty (n = 7) were analysed and compared with healthy corneal tissues (n = 4). Tissues were analysed with Fourier Transform Infrared Spectroscopy with a Focal Plane Array detector (FPA-FTIR). The spectra were recorded in the range from 4000 cm-1 to 850 cm-1.
Results: In keratoconic corneas, spectrum of collagen has shown significant decrease both in its absolute (1204, p = 0.089), and relative (1204/1650, p = 0.011) contribution. Similar significant decrease could be seen in the absolute (1160, p = 0.020) and relative content of proteoglycans/polysaccharides and proteins (1160/1650, p = 0.021). We have identified non-significant decrease of relative content of phosphates compared to proteins (1238/1650, p = 0.089)). Common absorption band of collagen and proteoglycans was also increased relatively to the absorption band of phosphate group containing compounds, collagen and proteoglycans (1030/1082, p = 0.011).
Conclusions: This study demonstrates that FTIR microspectroscopy is a valuable tool for identifying spectral markers of corneal diseases. Significant differences in protein, proteoglycan and polysaccharide content were observed between keratoconic and healthy corneas. Notably, a reduced phosphate-to-protein ratio and decreased collagen and proteoglycan content were found in keratoconic samples. These changes reflect literature findings concerning ECM dysregulation driven by upregulated MMPs and altered collagen organization. Our findings highlight FTIR's potential for objective molecular characterization of corneal pathology and possibly-a tool in search of diagnostic biomarkers.
(Copyright © 2026 The Authors. Published by Elsevier Ltd.. All rights reserved.)
Competing Interests: Declaration of competing interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Tomasz Choragiewicz reports financial support was provided by National Science Centre Poland. If there are other authors, they declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
Contributed Indexing: Keywords: Cornea; Ectasia; FTIR; Fourier-transform-infrared-spectroscopy; KC; Keratoconus
Substance Nomenclature: 0 (Proteoglycans)
9007-34-5 (Collagen)
0 (Biomarkers)
Entry Date(s): Date Created: 20260609 Date Completed: 20260831 Latest Revision: 20260831
Update Code: 20260901
DOI: 10.1016/j.exer.2026.111117
PMID: 42264061
Βάση Δεδομένων: MEDLINE