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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TL;DR: Proteoglycans were extracted with 4 M guanidine-HCl from the zone of maturing chondrocytes, the site of endochondral ossification of growing antlers of wapiti (Cervus elaphus) using DEAE-Sephacel chromatography and separated into three fractions.
Abstract: Proteoglycans were extracted with 4 M guanidine-HCl from the zone of maturing chondrocytes, the site of endochondral ossification of growing antlers of wapiti (Cervus elaphus). Proteoglycans were isolated by DEAE-Sephacel chromatography and separated by Sepharose CL-4B chromatography into three fractions. Fraction I contained a high molecular mass (> 1000 kDa) chondroitin sulfate proteoglycan capable of interacting with hyaluronic acid. Its amino acid composition resembled that of the cartilage proteoglycan, aggrecan. Fraction II contained proteoglycans with intermediate molecular weight which were recognized by monoclonal antibodies specific to chondroitin sulfate and keratan sulfate. Fraction III contained a low molecular mass (< 160 kDa) proteoglycan, decorin, with a glucuronate-rich glycosaminoglycan chain.
20 citations
TL;DR: Characterization of the immunogenic material by chondroitinase ABC digestion, ELISA inhibition studies, immunoblotting and HPLC analyses confirmed the presence of substantial amounts of KS, probably as a large proteoglycan (> 120 kDa).
20 citations
TL;DR: Examination of the expression of various extracellular components in the cornea of a 46-year-old man who underwent phototherapeutic keratectomy to remove a central corneal scar secondary to trauma indicated that the formation of subepithelial haze is a process of tissue remodeling, involving both corneals basal epithelial cells and keratocytes during wound repair.
Abstract: Purpose Subepithelial haze is a frequent complication and is often the cause of regression after photorefractive keratectomy (PRK). The lack of understanding of this undesirable complication following PRK is in part due to the limited availability of suitable tissues for pathological studies. Methods We examined the expression of various extracellular components in the cornea of a 46-year-old man who underwent phototherapeutic keratectomy (PTK) to remove a central corneal scar secondary to trauma. The patient subsequently underwent penetrating keratoplasty. A scar-free region containing an area of slight subepithelial haze adjacent to normal cornea was used for immunohistochemical staining with antibodies directed against cytoskeletal proteins, ie, vimentin, desmin and smooth muscle actin, and the extracellular components, laminin, heparan sulfate, keratan sulfate, and collagen types III, IV, V, and VII. Results Immunohistochemistry revealed that basal epithelial cells expressed components of basement membrane. The stromal fibroblasts within the haze tissue were labeled by anti-smooth muscle actin antibodies, a characteristic of myofibroblasts, which synthesized and secreted extracellular matrix components that contributed to the formation of the disorganized collagenous matrix and may account for subepithelial haze. Conclusions The expression patterns for the cytoskeletal proteins and extracellular components indicated that the formation of subepithelial haze is a process of tissue remodeling, involving both corneal basal epithelial cells and keratocytes during wound repair.
20 citations
TL;DR: Results indicate that most of the nonaggregating 35S-PGs in papain-treated cartilage have properties similar to those in normal cartilage and are not simple degradation products of aggregating35S- PGs; they suggest that the supplementary reaction for PG content in the cartilage during its repair process is not simple acceleration in PG turn-over but the enhancement of PG synthesis accompanied by alterations in aggregating ability and the compositions of GAG and CS isomer.
20 citations
TL;DR: Data suggest that in vertebrate corneas, the multiple KSPG core protein isoforms may arise as products of separate mRNAs, rather than from proteolytic processing of a large polypeptide precursor.
20 citations