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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Patent•
03 Aug 2016
TL;DR: In this article, a chondroitin sulfate/dermatan sulfate extraction method is described, which comprises the following steps: drying the eggshell matrix and grinding to obtain eggshell mixture, separating and extracting total glycosaminoglycan from the mixture, and removing heparin/heparan sulfates, keratan sulfate, and hyaluronic acid in the total glycolycan.
Abstract: The invention discloses a chondroitin sulfate/dermatan sulfate extraction method which comprises the following steps: drying the eggshell matrix and grinding to obtain eggshell matrix powder; separating and extracting total glycosaminoglycan from the eggshell matrix powder; and removing heparin/heparan sulfate, keratan sulfate and hyaluronic acid in the total glycosaminoglycan to obtain high-purity chondroitin sulfate/dermatan sulfate.
3 citations
TL;DR: The results indicate that sulfated and unsulfated polysaccharides are able to inhibit phosphorylation of histone type IIa catalysed by cAMP‐dependent protein kinase.
Abstract: The physiological effects of the second messenger cAMP are displayed by cAMP-dependent protein kinase-medicated phosphorylation of specific target proteins which in turn control diverse cellular functions. We have determined this enzyme substrate phosphorylation in the presence of various glycosaminoglycans using a cAMP-dependent protein kinase isolated from rat liver. The results indicate that sulfated and unsulfated polysaccharides are able to inhibit phosphorylation of histone type IIa catalysed by cAMP-dependent protein kinase. Based on their impact upon substrate phosphorylation, glycosaminoglycans can be divided into three groups: group I with the highest inhibitory effect: dermatan sulfate and heparan sulfate; group II: chondroitin 4-sulfate and group III with the lowest inhibitory effect: chondroitin 6-sulfate, keratan sulfate and hyaluronic acid. Copyright © 1999 John Wiley & Sons, Ltd.
3 citations
Patent•
12 Apr 1989
TL;DR: In this paper, a hair regeneration composition containing a sulfomuco-polysaccharide mixture bearing 5-20wt.% of heparin, 13-35wt.%.
Abstract: PURPOSE: To obtain a hair regeneration composition containing a sulfomuco- polysaccharide bearing heparin, heparin sulfate, dermatan sulfate, chondroitin sulfate A+B and keratan sulfate as active ingredients. CONSTITUTION: This composition contains, as active ingredients, a sulfomuco- polysaccharide mixture bearing 5-20wt.% of heparin, 13-35wt.% of heparan sulfate, 20-32wt.% of dermatan sulfate, 24-36wt.% of chondroitin sulfate A+B, 0-5wt.% of keratan sulfate, 0-13wt.% of hyaluronic acid, <=0.5wt.% of nucleic acid and <=5wt.% of protein, in addition, an excipient and a vehicle for cosmetics. These active ingredients are obtained from extracts of organs such as small intestine, skin, lung, placenta, trachea or eyes and the composition may be prepared in any form such as lotion, gel, cream, ointment and the like.
3 citations
TL;DR: The absence of structural variation in the newly synthesized proteoglycan core proteins from cartilage of different ages suggests that the age-related changes in the structure of the intact proteoglycans result from differences in the glycosaminoglycan biosynthetic machinery rather than alterations in the acceptor molecule.
Abstract: Chondrocytes of different ages synthesize proteoglycans which have structural differences in both the chondroitin sulfate and keratan sulfate glycosaminoglycans. In order to ascertain whether age-dependent differences also occur in the core protein, the chick limb bud mesenchymal cell culture system was utilized to analyze newly synthesized proteoglycan core protein from undifferentiated mesenchymal cells (day 1 and 2), newly differentiated cartilage (day 4), mature cartilage (day 8), and senescent cartilage (day 16). The core protein synthesized at various times was identified by radiolabeling with [3H]leucine and [35S]sulfate immediately prior to extraction and purification. The sizes of the various core protein preparations were compared by electrophoresis on a 3% polyacrylamide gel after partial deglycosylation with chondroitinase AC and keratanase. The proteoglycans from day 4, 8, and 16 cultures each give rise to a single band of approximately 475,000 daltons. The proteoglycans from day 1 and 2 cult...
3 citations
TL;DR: In this paper, Bovine nasal septum aggrecan was evaluated in an inhibition ELISA using the anti-keratan sulfate (KS) monoclonal antibody 5-D-4 (5D4).
Abstract: Bovine nasal septum aggrecan and selected proteinase-digested products of aggrecan were evaluated in an inhibition ELISA using the anti-keratan sulfate (KS) monoclonal antibody 5-D-4 (5D4). Undegraded aggrecan was recognized with an IC50 of 0.27 μg/ml. When aggrecan was treated with human stromelysin (SLN), human leukocyte elastase (HLE), or papain, the degradation fragments had different hydrodynamic sizes. Treatment with SLN produced the largest fragments, HLE generated intermediate fragments, and papain the smallest fragments. Whereas degradation of aggrecan by SLN had little effect on recognition of proteoglycan in the ELISA (IC50-0.5 μg/ml), degradation by both HLE and papain significantly decreased the sensitivity for detection of KS epitope (IC50-170 and 215 μg/ml, respectively). In addition, 5D4 detected single chain costal and corneal KS with much less sensitivity (IC50-21 and 469 μg/ml, respectively) than undegraded aggrecan (IC50-0.27 μg/ml).
3 citations