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Effect of Radiosynovectomy with Holmium-166 Ferric Hydroxide Macroaggregate on Adult Equine Cartilage

OLLI T. MÄKELÄ, MIKKO J. LAMMI, HANNELE UUSITALO, MINNA VIITANEN, MIKA M. HYTTINEN, JUKKA S. JURVELIN, EERO VUORIO, HEIKKI J. HELMINEN, and RIITTA-MARI TULAMO

ABSTRACT.

Objective.
To analyze the effect of radiosynovectomy with holmium-166 ferric hydroxide macroaggregate (166Ho-FHMA) on articular cartilage in 6 adult horses.

Methods. Arthritic changes and mechanical properties of articular cartilage were evaluated with arthroscopy and postmortem microscopic analyses. Glycosaminoglycan content was measured by safranin-O staining combined with digital densitometry, uronic acid analyses, and dimethylene blue binding assay. 35S-sulfate labeling and autoradiography were used to localize proteoglycan synthesis and to characterize proteoglycan structures using SDS-agarose gel electrophoresis. Northern hybridizations were performed to measure the mRNA levels for aggrecan and pro-a1(II) collagen in cartilage samples.

Results. Histological signs of degeneration were present in the articular cartilage of both control and radiosynovectomized equine joints. Radiosynovectomy did not aggravate degenerative changes or significantly alter the matrix glycosaminoglycan content. A slightly decreased size of proteoglycan monomers was observed 2 months after 166Ho-FHMA radiosynovectomy. Tissue analysis of extracted proteoglycans revealed lower 35S incorporation after radiosynovectomy, but corresponding changes could not be observed in aggrecan mRNA levels. Transient downregulation of pro-a1(II) collagen mRNA transcription was observed 5 days after 166Ho-FHMA radiosynovectomy.

Conclusion. 166Ho-FHMA treatment did not markedly affect the composition or morphology of adult articular cartilage showing mild degeneration. However, minor degradation of proteoglycan monomers and transient downregulation of pro-a1(II) collagen mRNA were observed. (J Rheumatol 2004;31:321-8)

Key Indexing Terms:

RADIOSYNOVECTOMY
OSTEOARTHRITIS
EQUINE
ARTHROSCOPY
COLLAGEN TYPE II
PROTEOGLYCAN


From the Faculty of Veterinary Medicine, University of Helsinki, Helsinki, Finland.

Supported by MAP Medical Technologies Oy, Tikkakoski, Finland.

O.T. Mäkelä, DVM; M. Viitanen, DVM; R-M. Tulamo, DVM, PhD, Professor, Faculty of Veterinary Medicine, University of Helsinki; M.J. Lammi, PhD; M.M. Hyttinen, MD; H.J. Helminen, MD, PhD, Professor, Department of Anatomy, University of Kuopio; H. Uusitalo, MD, PhD; E. Vuorio, MD, PhD, Professor, Department of Medical Biochemistry and Molecular Biology, University of Turku; J.S. Jurvelin, PhD, Department of Applied Physics, University of Kuopio.

Address reprint requests to Dr. O.T. Mäkelä, Department of Clinical Veterinary Sciences, Faculty of Veterinary Medicine, PO Box 57, FIN-00014 University of Helsinki, Helsinki, Finland.

Submitted February 11, 2003; revision accepted July 8, 2003.




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