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Altered fine structures of corneal and skeletal keratan sulfate and chondroitin/dermatan sulfate in macular corneal dystrophy.
J Biol Chem. 2001 Oct 26; 276(43):39788-96.JB

Abstract

The content and fine structure of keratan and chondroitin/dermatan sulfate in normal human corneas and corneas affected by macular corneal dystrophies (MCD) types I and II were examined by fluorophore-assisted carbohydrate electrophoresis. Normal tissues (n = 11) contained 15 microg of keratan sulfate and 8 microg of chondroitin/dermatan sulfate per mg dry weight. Keratan sulfates consisted of approximately 4% unsulfated, 42% monosulfated, and 54% disulfated disaccharides with number of average chain lengths of approximately 14 disaccharides. Chondroitin/dermatan sulfates were significantly longer, approximately 40 disaccharides per chain, and consisted of approximately 64% unsulfated, 28% 4-sulfated, and 8% 6-sulfated disaccharides. The fine structural parameters were altered in all diseased tissues. Keratan sulfate chain size was reduced to 3-4 disaccharides; chain sulfation was absent in MCD type I corneas and cartilages, and sulfation of both GlcNAc and Gal was significantly reduced in MCD type II. Chondroitin/dermatan sulfate chain sizes were also decreased in all diseased corneas to approximately 15 disaccharides, and the contents of 4- and 6-sulfated disaccharides were proportionally increased. Tissue concentrations (nanomole of chains per mg dry weight) of all glycosaminoglycan types were affected in the disease types. Keratan sulfate chain concentrations were reduced by approximately 24 and approximately 75% in type I corneas and cartilages, respectively, and by approximately 50% in type II corneas. Conversely, chondroitin/dermatan sulfate chain concentrations were increased by 60-70% in types I and II corneas. Such changes imply a modified tissue content of individual proteoglycans and/or an altered efficiency of chain substitution on the core proteins. Together with the finding that hyaluronan, not normally present in healthy adult corneas, was also detected in both disease subtypes, the data support the conclusion that a wide range of keratocyte-specific proteoglycan and glycosaminoglycan remodeling processes are activated during degeneration of the stromal matrix in the macular corneal dystrophies.

Authors+Show Affiliations

Shriners Hospital for Children, 12502 N. Pine Drive, Tampa, FL 33612, USA. aplaas@shctampa.usf.eduNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

11514545

Citation

Plaas, A H., et al. "Altered Fine Structures of Corneal and Skeletal Keratan Sulfate and Chondroitin/dermatan Sulfate in Macular Corneal Dystrophy." The Journal of Biological Chemistry, vol. 276, no. 43, 2001, pp. 39788-96.
Plaas AH, West LA, Thonar EJ, et al. Altered fine structures of corneal and skeletal keratan sulfate and chondroitin/dermatan sulfate in macular corneal dystrophy. J Biol Chem. 2001;276(43):39788-96.
Plaas, A. H., West, L. A., Thonar, E. J., Karcioglu, Z. A., Smith, C. J., Klintworth, G. K., & Hascall, V. C. (2001). Altered fine structures of corneal and skeletal keratan sulfate and chondroitin/dermatan sulfate in macular corneal dystrophy. The Journal of Biological Chemistry, 276(43), 39788-96.
Plaas AH, et al. Altered Fine Structures of Corneal and Skeletal Keratan Sulfate and Chondroitin/dermatan Sulfate in Macular Corneal Dystrophy. J Biol Chem. 2001 Oct 26;276(43):39788-96. PubMed PMID: 11514545.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Altered fine structures of corneal and skeletal keratan sulfate and chondroitin/dermatan sulfate in macular corneal dystrophy. AU - Plaas,A H, AU - West,L A, AU - Thonar,E J, AU - Karcioglu,Z A, AU - Smith,C J, AU - Klintworth,G K, AU - Hascall,V C, Y1 - 2001/08/20/ PY - 2001/8/22/pubmed PY - 2002/1/5/medline PY - 2001/8/22/entrez SP - 39788 EP - 96 JF - The Journal of biological chemistry JO - J Biol Chem VL - 276 IS - 43 N2 - The content and fine structure of keratan and chondroitin/dermatan sulfate in normal human corneas and corneas affected by macular corneal dystrophies (MCD) types I and II were examined by fluorophore-assisted carbohydrate electrophoresis. Normal tissues (n = 11) contained 15 microg of keratan sulfate and 8 microg of chondroitin/dermatan sulfate per mg dry weight. Keratan sulfates consisted of approximately 4% unsulfated, 42% monosulfated, and 54% disulfated disaccharides with number of average chain lengths of approximately 14 disaccharides. Chondroitin/dermatan sulfates were significantly longer, approximately 40 disaccharides per chain, and consisted of approximately 64% unsulfated, 28% 4-sulfated, and 8% 6-sulfated disaccharides. The fine structural parameters were altered in all diseased tissues. Keratan sulfate chain size was reduced to 3-4 disaccharides; chain sulfation was absent in MCD type I corneas and cartilages, and sulfation of both GlcNAc and Gal was significantly reduced in MCD type II. Chondroitin/dermatan sulfate chain sizes were also decreased in all diseased corneas to approximately 15 disaccharides, and the contents of 4- and 6-sulfated disaccharides were proportionally increased. Tissue concentrations (nanomole of chains per mg dry weight) of all glycosaminoglycan types were affected in the disease types. Keratan sulfate chain concentrations were reduced by approximately 24 and approximately 75% in type I corneas and cartilages, respectively, and by approximately 50% in type II corneas. Conversely, chondroitin/dermatan sulfate chain concentrations were increased by 60-70% in types I and II corneas. Such changes imply a modified tissue content of individual proteoglycans and/or an altered efficiency of chain substitution on the core proteins. Together with the finding that hyaluronan, not normally present in healthy adult corneas, was also detected in both disease subtypes, the data support the conclusion that a wide range of keratocyte-specific proteoglycan and glycosaminoglycan remodeling processes are activated during degeneration of the stromal matrix in the macular corneal dystrophies. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/11514545/Altered_fine_structures_of_corneal_and_skeletal_keratan_sulfate_and_chondroitin/dermatan_sulfate_in_macular_corneal_dystrophy_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0021-9258(20)60043-6 DB - PRIME DP - Unbound Medicine ER -