#PAGE_PARAMS# #ADS_HEAD_SCRIPTS# #MICRODATA#

Histochemical quantification of collagen content in articular cartilage


Autoři: Lassi Rieppo aff001;  Lauriane Janssen aff001;  Krista Rahunen aff001;  Petri Lehenkari aff003;  Mikko A. J. Finnilä aff001;  Simo Saarakkala aff001
Působiště autorů: Research Unit of Medical Imaging, Physics and Technology, Faculty of Medicine, University of Oulu, Oulu, Finland aff001;  Microelectronics Research Unit, Faculty of Information Technology and Electrical Engineering, University of Oulu, Oulu, Finland aff002;  Department of Surgery and Intensive Care, Oulu University Hospital, Oulu, Finland aff003;  Cancer and Translational Medicine Research Unit, Faculty of Medicine, University of Oulu, Oulu, Finland aff004;  Infotech Oulu, University of Oulu, Oulu, Finland aff005;  Department of Diagnostic Radiology, Oulu University Hospital, Oulu, Finland aff006
Vyšlo v časopise: PLoS ONE 14(11)
Kategorie: Research Article
doi: https://doi.org/10.1371/journal.pone.0224839

Souhrn

Background

Articular cartilage (AC) is mainly composed of water, type II collagen, proteoglycans (PGs) and chondrocytes. The amount of PGs in AC is routinely quantified with digital densitometry (DD) from Safranin O-stained sections, but it is unclear whether similar method could be used for collagens.

Objective

The aim of this study was to clarify whether collagens can be quantified from histological AC sections using DD.

Material and methods

Sixteen human AC samples were stained with Masson’s trichrome or Picrosirius red. Optical densities of histological stains were compared to two commonly used collagen parameters (amide I and collagen CH2 side chain peak at 1338cm-1) measured using Fourier Transform Infrared (FTIR) spectroscopic imaging.

Results

Optical density of Modified Masson’s trichrome staining, which included enzymatic removal of PGs before staining, correlated significantly with FTIR-derived collagen parameters at almost all depths of cartilage. The other studied staining protocols displayed significant correlations with the reference parameters at only few depth layers.

Conclusions

Based on our findings, modified Masson’s trichrome staining protocol is suitable for quantification of AC collagen content. Enzymatic removal of PGs prior to staining is critical as us allows better staining of the collagen. Further optimization of staining protocols may improve the results in the future studies.

Klíčová slova:

Amides – Cartilage – Collagens – Fourier transform infrared spectroscopy – Histology – Staining – Safranin staining – Densitometry


Zdroje

1. Buckwalter JA, Mankin HJ. Articular cartilage: tissue design and chondrocyte-matrix interactions. Instr Course Lect. 1998;47: 477–86. 9571449

2. Wall A, Board T. A direct spectrophotometric microassay for sulphated glycosaminoglycans in cartilage cultures. Classic Papers in Orthopaedics. 2014. pp. 431–432. doi: 10.1007/978-1-4471-5451-8_109

3. Brama PAJ, Tekoppele JM, Bank RA, van Weeren PR, Barneveld A. Influence of different exercise levels and age on the biochemical characteristics of immature equine articular cartilage. Equine Vet J Suppl. 1999;31: 55–61. doi: 10.1111/j.2042-3306.1999.tb05314.x

4. Edwards CA, O’Brien WD. Modified assay for determination of hydroxyproline in a tissue hydrolyzate. Clin Chim Acta. 1980;104: 161–167. doi: 10.1016/0009-8981(80)90192-8 7389130

5. Bank RA, Krikken M, Beekman B, Stoop R, Maroudas A, Lafebers FPJG, et al. A simplified measurement of degraded collagen in tissues: Application in healthy, fibrillated and osteoarthritic cartilage. Matrix Biol. 1997;16: 233–243. doi: 10.1016/S0945-053X(97)90012-3 9501324

6. Kiviranta I, Jurvelin J, Säämänen A-M, Helminen HJ. Microspectrophotometric quantitation of glycosaminoglycans in articular cartilage sections stained with Safranin O. Histochemistry. 1985;82: 249–255. doi: 10.1007/bf00501401 2581923

7. Hyllested JL, Veje K, Ostergaard K. Histochemical studies of the extracellular matrix of human articular cartilage-A review. Osteoarthr Cartil. 2002;10: 333–343. doi: 10.1053/joca.2002.0519 12027534

8. Schmitz N, Laverty S, Kraus VB, Aigner T. Basic methods in histopathology of joint tissues. Osteoarthr Cartil. 2010;18: S113–S116. doi: 10.1016/j.joca.2010.05.026 20864017

9. Király K, Lapveteläinen T, Arokoski J, Törrönen K, Módis L, Kiviranta I, et al. Application of selected cationic dyes for the semiquantitative estimation of glycosaminoglycans in histological sections of articular cartilage by microspectrophotometry. Histochem J. 1996;28: 577–90. doi: 10.1007/bf02331378 8894661

10. Junqueira LCU, Bignolas G, Brentani RR. Picrosirius staining plus polarization microscopy, a specific method for collagen detection in tissue sections. Histochem J. 1979;11: 447–455. doi: 10.1007/bf01002772 91593

11. Cheheltani R, Rosano JM, Wang B, Sabri AK, Pleshko N, Kiani MF. Fourier transform infrared spectroscopic imaging of cardiac tissue to detect collagen deposition after myocardial infarction. J Biomed Opt. 2012;17: 056014. doi: 10.1117/1.JBO.17.5.056014 22612137

12. Rich L, Whittaker P. Collagen and picrosirius red staining: a polarized light assessment of fibrillar hue and spatial distribution [Internet]. Braz J Morphol Sci 2005 pp. 97–104. https://www.semanticscholar.org/paper/Collagen-and-picrosirius-red-staining%3A-a-polarized-Rich-Whittaker/81282ace6a9024d0bd96b46dcc47aabc6e669a30

13. Whittaker P, Kloner RA, Boughner DR, Pickering JG. Quantitative assessment of myocardial collagen with picrosirius red staining and circularly polarized light. Basic Res Cardiol. 1994;89: 397–410. doi: 10.1007/bf00788278 7535519

14. Wolman M, Kasten FH. Polarized light microscopy in the study of the molecular structure of collagen and reticulin. Histochemistry. 1986;85: 41–49. doi: 10.1007/bf00508652 3733471

15. Nieminen MT, Rieppo J, Töyräs J, Hakumäki JM, Silvennoinen J, Hyttinen MM, et al. T2 relaxation reveals spatial collagen architecture in articular cartilage: A comparative quantitative MRI and polarized light microscopic study. Magn Reson Med. 2001;46: 487–493. doi: 10.1002/mrm.1218 11550240

16. Puchtler H, Isler H. the Effect of Phosphomolybdic Acid on the Stainability of Connective Tissues By Various Dyes. J Histochem Cytochem. 1958;6: 265–270. doi: 10.1177/6.4.265 13563844

17. Constantine VS, Mowry RW. Selective staining of human dermal collagen. II. The use of picrosirius red F3BA with polarization microscopy. J Invest Dermatol. 1968;50: 419–423. doi: 10.1038/jid.1968.68 4172462

18. Rieppo L, Saarakkala S, Närhi T, Helminen HJ, Jurvelin JS, Rieppo J. Application of second derivative spectroscopy for increasing molecular specificity of fourier transform infrared spectroscopic imaging of articular cartilage. Osteoarthr Cartil. 2012;20: 451–459. doi: 10.1016/j.joca.2012.01.010 22321720

19. Rieppo J, Hallikainen J, Jurvelin JS, Kiviranta I, Helminen HJ, Hyttinen MM. Practical Considerations in the Use of Polarized Light Microscopy in the Analysis of the Collagen Network in Articular Cartilage. 2008;287: 279–287. doi: 10.1002/jemt.20551 18072283


Článek vyšel v časopise

PLOS One


2019 Číslo 11
Nejčtenější tento týden
Nejčtenější v tomto čísle
Kurzy

Zvyšte si kvalifikaci online z pohodlí domova

Svět praktické medicíny 3/2024 (znalostní test z časopisu)
nový kurz

Kardiologické projevy hypereozinofilií
Autoři: prof. MUDr. Petr Němec, Ph.D.

Střevní příprava před kolonoskopií
Autoři: MUDr. Klára Kmochová, Ph.D.

Aktuální možnosti diagnostiky a léčby litiáz
Autoři: MUDr. Tomáš Ürge, PhD.

Závislosti moderní doby – digitální závislosti a hypnotika
Autoři: MUDr. Vladimír Kmoch

Všechny kurzy
Kurzy Podcasty Doporučená témata Časopisy
Přihlášení
Zapomenuté heslo

Zadejte e-mailovou adresu, se kterou jste vytvářel(a) účet, budou Vám na ni zaslány informace k nastavení nového hesla.

Přihlášení

Nemáte účet?  Registrujte se

#ADS_BOTTOM_SCRIPTS#