Characterization of corneal proteoglycans under vitamin A deficiency. Biochim Biophys Acta 1989 Aug 18;992(2):181-90
Date
08/18/1989Pubmed ID
2758064DOI
10.1016/0304-4165(89)90008-1Scopus ID
2-s2.0-0024362452 (requires institutional sign-in at Scopus site) 4 CitationsAbstract
Comparison of in vivo radiolabeled corneal proteoglycans from vitamin A deficient, pair-fed control and normal rabbits by chromatographic and enzymatic methods, reveals subtle but reproducible changes in the proteoglycans present in the vitamin A deficient corneas relative to those of pair-fed and normal control corneas. Although the total amounts of [3H]leucine and [35S]sulfate incorporated in vivo into the proteoglycans per cornea are similar in the three types of cornea, the proteoglycan affinity for DEAE-Sepharose is different, with more of the vitamin A deficient proteoglycans requiring a higher NaCl concentration for elution. Analysis of in vivo labeled rabbit corneal proteoglycans reveals that in vitamin A deficient animals, relative to pair-fed controls, there is (1) an increase in the proteoglycans digested by chondroitinase AC indicative of decreased epimerization of glucuronic acid to iduronic acid; (2) an increase in the amount of keratan sulfate proteoglycan with high affinity for an anion exchange resin, consistent with a greater negative charge; (3) differences in proteoglycan affinities for octyl-Sepharose, reflecting differences in hydrophobicity; (4) increased susceptibility to proteolysis by trypsin; (5) no significant difference in sulfation.
Author List
Twining SS, Wilson PM, Hatchell DLAuthor
Sally S. Twining PhD Assistant Dean, Professor in the Biochemistry department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsChromatography, Ion Exchange
Corneal Diseases
Eye Proteins
Glycosaminoglycans
Glycoside Hydrolases
Hydrolysis
Male
Proteoglycans
Rabbits
Trypsin
Vitamin A Deficiency
