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Previous Volume 335:1029-1033 October 3, 1996 Number 14 Next

	Since this article has no abstract, we have provided an extract of the first 100 words of the full text and any section headings.

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The mucopolysaccharidoses are lysosomal storage disorders caused by a genetic deficiency of enzymes that catalyze the degradation of glycosaminoglycans (mucopolysaccharides). These disorders are clinically variable and commonly associated with mental retardation, short stature, coarse facial features, organomegaly, and an accumulation of glycosaminoglycans in tissues.

Hyaluronan (hyaluronic acid) is one of the major glycosaminoglycans and has a vital role in many physiologic processes.^1,2,3,4 Genetic deficiencies of most of the lysosomal enzymes that catalyze the degradation of glycosaminoglycans have been identified, with the exception of hyaluronidase, a lysosomal endoglycosidase that catalyzes the degradation of hyaluronan.^5,6,7 We describe the clinical, pathological, and biochemical . . . [Full Text of this Article]

Case Report

Radiographic Findings

Methods

Histochemical and Electron-Microscopical Analyses

Biochemical Studies

Results

Histologic and Electron-Microscopical Findings

Biochemical Findings

Discussion

Source Information

From the Division of Medical Genetics, Shriver Center for Mental Retardation, Waltham, Mass. (M.R.N., Y.W.); and the Departments of Neurology (M.R.N., M.P.S., K.B.S.), Pathology (M.R.N., M.P.S., G.R.D., A.E.R.), Radiology (D.I.R.), and Orthopedic Surgery (M.C.G.), Massachusetts General Hospital, Boston.

Address reprint requests to Dr. Natowicz at the Division of Medical Genetics, Shriver Center for Mental Retardation, 200 Trapelo Rd., Waltham, MA 02254.

References

This article has been cited by other articles:

• Martin, D. C., Atmuri, V., Hemming, R. J., Farley, J., Mort, J. S., Byers, S., Hombach-Klonisch, S., Stern, R., Triggs-Raine, B. L. (2008). A mouse model of human mucopolysaccharidosis IX exhibits osteoarthritis. Hum Mol Genet 17: 1904-1915 [Abstract] [Full Text]  
• Hemming, R., Martin, D. C., Slominski, E., Nagy, J. I., Halayko, A. J., Pind, S., Triggs-Raine, B. (2008). Mouse Hyal3 encodes a 45- to 56-kDa glycoprotein whose overexpression increases hyaluronidase 1 activity in cultured cells. Glycobiology 18: 280-289 [Abstract] [Full Text]  
• Stern, R. (2003). Devising a pathway for hyaluronan catabolism: are we there yet?. Glycobiology 13: 105R-115R [Abstract] [Full Text]  
• Shuttleworth, T. L., Wilson, M. D., Wicklow, B. A., Wilkins, J. A., Triggs-Raine, B. L. (2002). Characterization of the Murine Hyaluronidase Gene Region Reveals Complex Organization and Cotranscription of Hyal1 with Downstream Genes, Fus2 and Hyal3. J. Biol. Chem. 277: 23008-23018 [Abstract] [Full Text]  
• Triggs-Raine, B., Salo, T. J., Zhang, H., Wicklow, B. A., Natowicz, M. R. (1999). Mutations in HYAL1, a member of a tandemly distributed multigene family encoding disparate hyaluronidase activities, cause a newly described lysosomal disorder, mucopolysaccharidosis IX. Proc. Natl. Acad. Sci. USA 96: 6296-6300 [Abstract] [Full Text]  
• Fischer, T A, Lehr, H-A, Nixdorff, U, Meyer, J (1999). Combined aortic and mitral stenosis in mucopolysaccharidosis type I-S (Ullrich-Scheie syndrome). Heart 81: 97-99 [Abstract] [Full Text]