Topic
Keratan sulfate
About: Keratan sulfate is a research topic. Over the lifetime, 1253 publications have been published within this topic receiving 57984 citations. The topic is also known as: keratan sulfate & KS.
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36 citations
TL;DR: Most of the PG core proteins underwent significant changes in cultured keratoconic cells and corneas, and the polymerization of the chains and their chemical modification was modified in way that depended on the specific type of GAG involved.
Abstract: PURPOSE Keratoconus is a heterogeneous disease associated with a range of pathologies, including disorders that involve proteoglycans (PGs). Some PG alterations, mainly in keratan sulfate (KS), occur in keratoconus. In this article, we studied the differential expression of the genes encoding PGs in cells isolated from keratoconus patients and healthy controls, as well as in corneal sections. METHODS Human central corneal tissue was obtained from cadaver donors and patients undergoing penetrating keratoplasty surgery. A transcriptomic approach was used, employing quantitative PCR, to analyze both the expression of the enzymes involved in glycosaminoglycan (GAG) biosynthesis and the PG core proteins. The expressions of the differentially expressed core proteins and of the GAG chains were also analyzed by immunocytochemistry in the cultured cells, as well as by immunohistochemistry in corneal sections. RESULTS The mRNA levels of most major matrix PG mRNAs in the cultured keratoconic stromal cells decreased except collagen XVIII, which increased. At keratocyte surfaces, some heparan sulfate PGs were down-regulated. With respect to GAGs, there were changes in gene expression for the polymerization of the GAG chains, mainly KS and chondroitin sulfate, and in the modification of the saccharidic chains, pointing to an alteration of the sulfation patterns of all GAG species. CONCLUSIONS Most of the PG core proteins underwent significant changes in cultured keratoconic cells and corneas. With regard to GAG chains, the polymerization of the chains and their chemical modification was modified in way that depended on the specific type of GAG involved.
36 citations
TL;DR: Bovine nucleus pulposus has been found to be a good source of a series of proteinpolysaccharides containing chondroitin 6-sulfate and keratan sulfate, and there is no evidence that in this tissue any independent kinetic component exists which contains only chondDetroitin sulfate or only keratan sulfur.
36 citations
TL;DR: The preferential distribution and marked increase in PGs from base to apex in both TM and BM supports a role for these macromolecules in regulating structural and mechanical properties of these highly specialized extracellular membranes.
35 citations
TL;DR: It is demonstrated that serum KS levels rise predictably after CN, in a manner that reflects major catabolic events of cartilage.
Abstract: Sensitive measurements of serum keratan sulfate (KS), a glycosaminoglycan found in large quantities in the proteoglycans of human cartilage, can be obtained using an enzyme-linked immunosorbent-inhibition assay. Patients who are undergoing chemonucleolysis (CN) provide a clinical opportunity to monitor the large-scale proteolytic degradation of cartilage. By measuring serum KS levels both pre- and post-CN, we have demonstrated that serum KS levels rise predictably after CN, in a manner that reflects major catabolic events of cartilage.
35 citations