Journal articles: 'Keratane sulfate'

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Ley, K., M. Cerrito, and K. E. Arfors. "Sulfated polysaccharides inhibit leukocyte rolling in rabbit mesentery venules." American Journal of Physiology-Heart and Circulatory Physiology 260, no. 5 (May 1, 1991): H1667—H1673. http://dx.doi.org/10.1152/ajpheart.1991.260.5.h1667.

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Before firm adhesion, leukocytes roll slowly along the walls of small venules at velocities ranging from 0.7 to 36% of mean blood flow velocity. To investigate the nature of the adhesive process underlying leukocyte rolling, synthetic (dextran sulfate) and naturally occurring sulfated polysaccharides (heparin, chondroitin sulfates, keratan sulfate, and heparan sulfate) were infused via glass micropipettes into the lumen of small venules (20–60 microns diam) of the rabbit mesentery. Leukocyte rolling was observed and quantified using both transmitted light and incident fluorescence intravital microscopy. Rolling leukocytes accounted for 27–80% of total leukocyte flux, exhibiting a wide range of individual velocities (0.01–0.84 mm/s) with a mean value of 4% of centerline velocity. Dextran sulfate (Mr 500,000) inhibited leukocyte rolling very effectively [half-effective concentration (ED50) approximately 10 micrograms/ml] and was able to almost completely abolish rolling at 500 micrograms/ml. Heparin (ED50 approximately 50 micrograms/ml), chondroitin 6-sulfate C (ED50 approximately 500 micrograms/ml), and heparan sulfate (ED50 approximately 5 mg/ml) also reduced leukocyte rolling. At 5 mg/ml, chondroitin 4-sulfate B (dermatan sulfate) was marginally effective, but chondroitin 4-sulfate A and keratan sulfate were ineffective. The present data suggest that an adhesion receptor-ligand system distinct from the leukocyte integrins may be underlying transient leukocyte adhesion (rolling). Endothelial glycoproteins or proteoglycans containing sulfated side chains may be involved in mediating this adhesive process.

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Nagai, Yuko, Hiromi Nakao, Aya Kojima, Yuka Komatsubara, Yuki Ohta, Nana Kawasaki, Nobuko Kawasaki, Hidenao Toyoda, and Toshisuke Kawasaki. "Glycan Epitopes on 201B7 Human-Induced Pluripotent Stem Cells Using R-10G and R-17F Marker Antibodies." Biomolecules 11, no. 4 (March 29, 2021): 508. http://dx.doi.org/10.3390/biom11040508.

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We developed two human-induced pluripotent stem cell (hiPSC)/human embryonic stem cell (hESC)-specific glycan-recognizing mouse antibodies, R-10G and R-17F, using the Tic (JCRB1331) hiPSC line as an antigen. R-10G recognizes a low-sulfate keratan sulfate, and R-17F recognizes lacto-N-fucopentaose-1. To evaluate the general characteristics of stem cell glycans, we investigated the hiPSC line 201B7 (HPS0063), a prototype iPSC line. Using an R-10G affinity column, an R-10G-binding protein was isolated from 201B7 cells. The protein yielded a single but very broad band from 480 to 1236 kDa by blue native gel electrophoresis. After trypsin digestion, the protein was identified as podocalyxin by liquid chromatography/mass spectrometry. According to Western blotting, the protein reacted with R-10G and R-17F. The R-10G-positive band was resistant to digestion with glycan-degrading enzymes, including peptide N-glycanase, but the intensity of the band was decreased significantly by digestion with keratanase, keratanase II, and endo-β-galactosidase, suggesting the R-10G epitope to be a keratan sulfate. These results suggest that keratan sulfate-type epitopes are shared by hiPSCs. However, the keratan sulfate from 201B7 cells contained a polylactosamine disaccharide unit (Galβ1-4GlcNAc) at a significant frequency, whereas that from Tic cells consisted mostly of keratan sulfate disaccharide units (Galβ1-4GlcNAc(6S)). In addition, the abundance of the R-10G epitope was significantly lower in 201B7 cells than in Tic cells.

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Sorrell, J. M., and B. Caterson. "Detection of age-related changes in the distributions of keratan sulfates and chondroitin sulfates in developing chick limbs: an immunocytochemical study." Development 106, no. 4 (August 1, 1989): 657–63. http://dx.doi.org/10.1242/dev.106.4.657.

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A panel of four separate monoclonal antibodies, all known to specifically recognize epitopes on keratan sulfate glycosaminoglycans, were employed in an immunocytochemical study of developing chick hind limbs. In addition, two monoclonal antibodies specific for epitopes on chondroitin/dermatan sulfate glycosaminoglycans were employed on equivalent sections to determine the degree of colocalization of keratan and chondroitin/dermatan sulfates. The spatial distributions of keratan sulfate and chondroitin/dermatan sulfate differed to some extent. In younger embryos, high extracellular concentrations of keratan sulfate occurred in joints and articular cartilages, with diminishing amounts being present in epiphyseal and diaphyseal regions. The high concentration of keratan sulfate in joints and articular cartilage corresponded to equally high concentration of chondroitin-6 sulfate. With advancing age, the above mentioned distribution was modified, most notably by increased amounts of keratan sulfate within diaphyseal regions. Finally, the use of four different anti-keratan sulfate monoclonal antibodies made it possible to compare keratan sulfate epitope expression. Differences in keratan sulfate epitopes were noted in some regions of bones, mostly in diaphyseal regions of younger bones and epiphyseal regions of older bones. This pattern of keratan sulfate expression suggests that different types of keratan sulfate may be present and their expression may be developmentally regulated.

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Panin, G., S. Naia, R. Dall'Amico, L. Chiandetti, F. Zachello, C. Catassi, L. Felici, and G. V. Coppa. "Simple spectrophotometric quantification of urinary excretion of glycosaminoglycan sulfates." Clinical Chemistry 32, no. 11 (November 1, 1986): 2073–76. http://dx.doi.org/10.1093/clinchem/32.11.2073.

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Abstract We describe a simple, rapid, precise, and sensitive spectrophotometric method for measuring urinary glycosaminoglycan (GAG) sulfate excretion. The GAG sulfates are precipitated with cetylpyridinium chloride, resuspended in water, and mixed with the basic dye 1,9-dimethylmethylene blue to produce a complex with the polyanionic molecule of sulfated GAGs. Absorbance is read at 535 nm. The standard curve for reaction was linear up to 12 micrograms of the different GAGs: dermatan sulfate, heparan sulfate, keratan sulfate, chondroitin 4-sulfate, and chondroitin 6-sulfate. Within- and between-run precision (CV), measured at three different GAG concentrations (normal and pathological), varied from 1.6% to 2.5% and from 1.8% to 4.5%, respectively. Analytical recovery ranged from 71% to 107%. Urinary GAG excretion, measured by this procedure, correlates (r = 0.837; p less than 0.001) with the values obtained with the borate-carbazole reaction (Anal Biochem 1962;4:330-4).

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Brown, Gavin M., Thomas N. Huckerby, Haydn G. Morris, Beverley L. Abram, and Ian A. Nieduszynski. "Oligosaccharides Derived from Bovine Articular Cartilage Keratan Sulfates after Keratanase II Digestion: Implications for Keratan Sulfate Structural Fingerprinting." Biochemistry 33, no. 16 (April 1994): 4836–46. http://dx.doi.org/10.1021/bi00182a012.

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Sawamoto, Kazuki, and Shunji Tomatsu. "Development of Substrate Degradation Enzyme Therapy for Mucopolysaccharidosis IVA Murine Model." International Journal of Molecular Sciences 20, no. 17 (August 24, 2019): 4139. http://dx.doi.org/10.3390/ijms20174139.

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Mucopolysaccharidosis IVA (MPS IVA) is caused by a deficiency of the lysosomal enzyme N-acetylgalactosamine-6-sulfate sulfatase (GALNS). Conventional enzyme replacement therapy (ERT) is approved for MPS IVA. However, the fact that the infused enzyme cannot penetrate avascular lesions in cartilage leads to minimal impact on the bone lesion. Moreover, short half-life, high cost, instability, and narrow optimal pH range remain unmet challenges in ERT. Thermostable keratanase, endo-β-N-acetylglucosaminidase, has a unique character of a wide optimal pH range of pH 5.0–7.0. We hypothesized that this endoglycosidase degrades keratan sulfate (KS) polymer in circulating blood and, therefore, ameliorates the accumulation of KS in multiple tissues. We propose a novel approach, Substrate Degradation Enzyme Therapy (SDET), to treat bone lesion of MPS IVA. We assessed the effect of thermostable keratanase on blood KS level and bone pathology using Galns knock-out MPS IVA mice. After a single administration of 2 U/kg (= 0.2 mg/kg) of the enzyme at 8 weeks of age via intravenous injection, the level of serum KS was significantly decreased to normal range level, and this suppression was maintained for at least 4 weeks. We administered 2 U/kg of the enzyme to MPS IVA mice every fourth week for 12 weeks (total of 3 times) at newborns or 8 weeks of age. After a third injection, serum mono-sulfated KS levels were kept low for 4 weeks, similar to that in control mice, and at 12 weeks, bone pathology was markedly improved when SDET started at newborns, compared with untreated MPS IVA mice. Overall, thermostable keratanase reduces the level of KS in blood and provides a positive impact on cartilage lesions, demonstrating that SDET is a novel therapeutic approach to MPS IVA.

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Perris, R., D. Krotoski, T. Lallier, C. Domingo, J. M. Sorrell, and M. Bronner-Fraser. "Spatial and temporal changes in the distribution of proteoglycans during avian neural crest development." Development 111, no. 2 (February 1, 1991): 583–99. http://dx.doi.org/10.1242/dev.111.2.583.

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In this study, we describe the distribution of various classes of proteoglycans and their potential matrix ligand, hyaluronan, during neural crest development in the trunk region of the chicken embryo. Different types of chondroitin and keratan sulfate proteoglycans were recognized using a panel of monoclonal antibodies produced against specific epitopes on their glycosaminoglycan chains. A heparan sulfate proteoglycan was identified by an antibody against its core protein. The distribution of hyaluronan was mapped using a biotinylated fragment that corresponds to the hyaluronan-binding region of cartilage proteoglycans. Four major patterns of proteoglycan immunoreactivity were observed. (1) Chondroitin-6-sulfate-rich proteoglycans and certain keratin sulfate proteoglycans were absent from regions containing migrating neural crest cells, but were present in interstitial matrices and basement membranes along prospective migratory pathways such as the ventral portion of the sclerotome. Although initially distributed uniformly along the rostrocaudal extent of the sclerotome, these proteoglycans became rearranged to the caudal portion of the sclerotome with progressive migration of neural crest cells through the rostral sclerotome and their aggregation into peripheral ganglia. (2) A subset of chondroitin/keratan sulfate proteoglycans bearing primarily unsulfated chondroitin chains was observed exclusively in regions where neural crest cells were absent or delayed from entering, such as the perinotochordal and subepidermal spaces. (3) A subset of chondroitin/keratan sulfate proteoglycans was restricted to the perinotochordal region and, following gangliogenesis, was arranged in a metameric pattern corresponding to the sites where presumptive vertebral arches form. (4) Certain keratan sulfate proteoglycans and a heparan sulfate proteoglycan were observed in basement membranes and in an interstitial matrix uniformly distributed along the rostrocaudal extent of the sclerotome. After gangliogenesis, the neural crest-derived dorsal root and sympathetic ganglia contained both these proteoglycan types, but were essentially free of other chondroitin/keratan-proteoglycan subsets. Hyaluronan generally colocalized with the first set of proteoglycans, but also was concentrated around migrating neural crest cells and was reduced in neural crest-derived ganglia. These observations demonstrate that proteoglycans have diverse and dynamic distributions during times of neural crest development and chondrogenesis of the presumptive vertebrae. In general, chondroitin/keratan sulfate proteoglycans are abundant in regions where neural crest cells are absent, and their segmental distribution inversely correlates with that of neural crest-derived ganglia.

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Kerr, B. C., C. E. Hughes, and B. Caterson. "A novel keratanase-generated keratan sulfate antibody and its application to structural analysis of skeletal and corneal keratan sulfate." International Journal of Experimental Pathology 85, no. 4 (August 12, 2004): A67—A68. http://dx.doi.org/10.1111/j.0959-9673.2004.390ad.x.

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Bhaduri, Sayantan, and Nicola L. B. Pohl. "Fluorous-Tag Assisted Syntheses of Sulfated Keratan Sulfate Oligosaccharide Fragments." Organic Letters 18, no. 6 (March 9, 2016): 1414–17. http://dx.doi.org/10.1021/acs.orglett.6b00344.

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10

Schafer, Irwin A., and J. Michael Sorrell. "Human Keratinocytes Contain Keratin Filaments That Are Glycosylated with Keratan Sulfate." Experimental Cell Research 207, no. 2 (August 1993): 213–19. http://dx.doi.org/10.1006/excr.1993.1185.

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11

Zanetti, M., A. Ratcliffe, and F. M. Watt. "Two subpopulations of differentiated chondrocytes identified with a monoclonal antibody to keratan sulfate." Journal of Cell Biology 101, no. 1 (July 1, 1985): 53–59. http://dx.doi.org/10.1083/jcb.101.1.53.

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We have prepared a monoclonal antibody, named MZ15, that specifically binds keratan sulfate. Immunofluorescence studies showed that the distribution of keratan sulfate in articular cartilage was not uniform: the amount of keratan sulfate increased with distance from the articular surface. Two subpopulations of chondrocytes could be distinguished after isolation from cartilage by the presence or absence of cell surface keratan sulfate. Keratan sulfate-negative chondrocytes were shown to come from the upper cartilage layers. There was therefore a direct correlation between biochemical heterogeneity of cartilage matrix and heterogeneity within the chondrocyte population. During growth in monolayer culture, superficial chondrocytes began to synthesize keratan sulfate, but the cells could still be distinguished from cultures of deep or unfractionated chondrocytes by their reduced substrate adhesiveness and tendency to remain rounded.

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Funderburgh, James L. "Keratan Sulfate Biosynthesis." IUBMB Life (International Union of Biochemistry and Molecular Biology: Life) 54, no. 4 (October 1, 2002): 187–94. http://dx.doi.org/10.1080/15216540214932.

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13

Kubaski, Francyne, Tsutomu Shimada, Shunji Tomatsu, Robert W. Mason, Eriko Yasuda, William G. Mackenzie, Jobayer Hossain, et al. "Di-sulfated keratan sulfate as a novel biomarker for mucopolysaccharidosis IVA." Molecular Genetics and Metabolism 114, no. 2 (February 2015): S66—S67. http://dx.doi.org/10.1016/j.ymgme.2014.12.142.

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Hayatsu, Norihito, Satoshi Ogasawara, Mika Kato Kaneko, Yukinari Kato, and Hisashi Narimatsu. "Expression of highly sulfated keratan sulfate synthesized in human glioblastoma cells." Biochemical and Biophysical Research Communications 368, no. 2 (April 2008): 217–22. http://dx.doi.org/10.1016/j.bbrc.2008.01.058.

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Byers, S., B. Caterson, J. J. Hopwood, and B. K. Foster. "Immunolocation analysis of glycosaminoglycans in the human growth plate." Journal of Histochemistry & Cytochemistry 40, no. 2 (February 1992): 275–82. http://dx.doi.org/10.1177/40.2.1372629.

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Monoclonal antibodies were used in this study to immunolocate glycosaminoglycans throughout the human growth plate. Chondroitin-4-sulfate, chondroitin-6-sulfate, and keratan sulfate were observed in the extracellular matrix of all zones of the growth plate and persisted into the cartilage trabeculae of newly formed metaphyseal bone. Also present in the extracellular matrix was an oversulfated chondroitin/dermatan sulfate glycosaminoglycan which appeared to be specific to the proliferative and hypertrophic zones of the growth plate. As with the other extracellular matrix molecules, this epitope persisted into the cartilage trabeculae of the metaphyseal bone. Zonal differences between the extracellular and pericellular or lacunae matrix were also observed. The hypertrophic chondrocytes appeared to synthesize chondroitin sulfate chains containing a non-reducing terminal 6-sulfated disaccharide, which were located in areas immediately adjacent to the cells. This epitope was not found to any significant extent in the other zones. The pericellular region around hypertrophic chondrocytes also contained a keratan sulfate epitope which was also observed in the resting zone but not in the proliferative zone. These cell-associated glycosaminoglycans were not found in the cartilage trabeculae of metaphyseal bone, indicating their removal as the terminal hypertrophic chondrocytes and their lacunae are removed by invading blood vessels. These changes in matrix glycosaminoglycan content, both in the different zones and within zones, indicate constant subtle alterations in chondrocyte metabolic products as they proceed through their life cycle of proliferation, maturation, and hypertrophy.

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Arunkumar, Nivethitha, Dung Chi Vu, Shaukat Khan, Hironori Kobayashi, Thi Bich Ngoc Can, Tsubasa Oguni, Jun Watanabe, et al. "Diagnosis of Mucopolysaccharidoses and Mucolipidosis by Assaying Multiplex Enzymes and Glycosaminoglycans." Diagnostics 11, no. 8 (July 27, 2021): 1347. http://dx.doi.org/10.3390/diagnostics11081347.

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Mucopolysaccharidoses (MPS) and mucolipidosis (ML II/III) are a group of lysosomal storage disorders (LSDs) that occur due to a dysfunction of the lysosomal hydrolases responsible for the catabolism of glycosaminoglycans (GAGs). However, ML is caused by a deficiency of the enzyme uridine-diphosphate N-acetylglucosamine:lysosomal-enzyme-N-acetylglucosamine-1-phosphotransferase (GlcNAc-1-phosphotransferase, EC2.7.8.17), which tags lysosomal enzymes with a mannose 6-phosphate (M6P) marker for transport to the lysosome. A timely diagnosis of MPS and ML can lead to appropriate therapeutic options for patients. To improve the accuracy of diagnosis for MPS and ML in a high-risk population, we propose a combination method based on known biomarkers, enzyme activities, and specific GAGs. We measured five lysosomal enzymes (α-L-iduronidase (MPS I), iduronate-2-sulfatase (MPS II), α-N-acetylglucosaminidase (MPS IIIB), N-acetylglucosamine-6-sulfatase (MPS IVA), and N-acetylglucosamine-4-sulfatase (MPS VI)) and five GAGs (two kinds of heparan sulfate (HS), dermatan sulfate (DS), and two kinds of keratan sulfate (KS)) in dried blood samples (DBS) to diagnose suspected MPS patients by five-plex enzyme and simultaneous five GAGs assays. We used liquid chromatography-tandem mass spectrometry (LC-MS/MS) for both assays. These combined assays were tested for 43 patients with suspected MPS and 103 normal control subjects. We diagnosed two MPS I, thirteen MPS II, one MPS IIIB, three MPS IVA, two MPS VI, and six ML patients with this combined method, where enzymes, GAGs, and clinical manifestations were compatible. The remaining 16 patients were not diagnosed with MPS or ML. The five-plex enzyme assay successfully identified MPS patients from controls. Patients with MPS I, MPS II, and MPS IIIB had significantly elevated HS and DS levels in DBS. Compared to age-matched controls, patients with ML and MPS had significantly elevated mono-sulfated KS and di-sulfated KS levels. The results indicated that the combination method could distinguish these affected patients with MPS or ML from healthy controls. Overall, this study has shown that this combined method is effective and can be implemented in larger populations, including newborn screening.

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Pawlak, Agnieszka S., Elizabeth Hammond, Thomas Hammond, and Steven D. Gray. "Immunocytochemical Study of Proteoglycans in Vocal Folds." Annals of Otology, Rhinology & Laryngology 105, no. 1 (January 1996): 6–11. http://dx.doi.org/10.1177/000348949610500102.

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We evaluated the proteoglycan composition of normal vocal folds using immunocytochemical techniques. Frozen sections of 14 normal cadaveric vocal folds were obtained within 12 hours of death and sectioned immediately. Vocal fold sections were stained with antibodies against keratan sulfate, chondroitin sulfate, heparan sulfate proteoglycan (HSPG), decorin, and hyaluronate receptor. We found that the lamina propria has diffuse staining of fibrillar components with keratan sulfate and decorin. Intense staining was observed in the vocal ligament area with keratan sulfate. The HSPG was localized to the basement membrane zone. Chondroitin sulfate, HSPG, and hyaluronate receptor were detected in the cytoplasm of interstitial cells with immunocytochemical characteristics of macrophages. The keratan sulfate distribution suggests that fibromodulin may be significant in normal vocal folds. Production of HSPG and probably versican occurs in macrophages and fibroblasts in the lamina propria.

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Fukuda, K., F. Matsumura, and S. Tanaka. "Histamine H2 receptor mediates keratan sulfate secretion in rabbit chondrocytes: role of cAMP." American Journal of Physiology-Cell Physiology 265, no. 6 (December 1, 1993): C1653—C1657. http://dx.doi.org/10.1152/ajpcell.1993.265.6.c1653.

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We obtained evidence for the presence of a single class of histamine H2 receptor on rabbit chondrocytes. Stimulation of these receptors with specific H2 agonists led to an inhibition of keratan sulfate secretion and rapid (15 min) accumulation of intracellular adenosine 3',5'-cyclic monophosphate (cAMP). Factors such as prostaglandin E2 and parathyroid hormone, which stimulate short-term increases in cAMP, also caused a reduction in keratan sulfate secretion. Conversely, cholera toxin and forskolin, which enhance cAMP accumulation over 48 and 4 h, respectively, as well as a continuous exposure to dibutyryl cAMP, stimulated keratan sulfate secretion. These data suggest that intracellular cAMP must be kept above a certain level for a prolonged period to stimulate keratan sulfate secretion. We conclude that inhibition of keratan sulfate secretion is coupled with activation of the H2 histamine receptor.

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Mutoji, Kazadi N., Mingxia Sun, Garrett Elliott, Isabel Y. Moreno, Clare Hughes, Tarsis F. Gesteira, and Vivien J. Coulson-Thomas. "Extracellular Matrix Deposition and Remodeling after Corneal Alkali Burn in Mice." International Journal of Molecular Sciences 22, no. 11 (May 27, 2021): 5708. http://dx.doi.org/10.3390/ijms22115708.

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Corneal transparency relies on the precise arrangement and orientation of collagen fibrils, made of mostly Type I and V collagen fibrils and proteoglycans (PGs). PGs are essential for correct collagen fibrillogenesis and maintaining corneal homeostasis. We investigated the spatial and temporal distribution of glycosaminoglycans (GAGs) and PGs after a chemical injury. The chemical composition of chondroitin sulfate (CS)/dermatan sulfate (DS) and heparan sulfate (HS) were characterized in mouse corneas 5 and 14 days after alkali burn (AB), and compared to uninjured corneas. The expression profile and corneal distribution of CS/DSPGs and keratan sulfate (KS) PGs were also analyzed. We found a significant overall increase in CS after AB, with an increase in sulfated forms of CS and a decrease in lesser sulfated forms of CS. Expression of the CSPGs biglycan and versican was increased after AB, while decorin expression was decreased. We also found an increase in KS expression 14 days after AB, with an increase in lumican and mimecan expression, and a decrease in keratocan expression. No significant changes in HS composition were noted after AB. Taken together, our study reveals significant changes in the composition of the extracellular matrix following a corneal chemical injury.

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Kato, Yukinari, Norihito Hayatsu, Mika Kato Kaneko, Satoshi Ogasawara, Tetsutaro Hamano, Satoru Takahashi, Ryo Nishikawa, Masao Matsutani, Kazuhiko Mishima, and Hisashi Narimatsu. "Increased expression of highly sulfated keratan sulfate synthesized in malignant astrocytic tumors." Biochemical and Biophysical Research Communications 369, no. 4 (May 2008): 1041–46. http://dx.doi.org/10.1016/j.bbrc.2008.02.130.

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BAMBINO-MEDEIROS, R., F. O. R. OLIVEIRA, C. M. CALVET, D. VICENTE, L. TOMA, M. A. KRIEGER, M. N. MEIRELLES, and M. C. S. PEREIRA. "Involvement of host cell heparan sulfate proteoglycan inTrypanosoma cruziamastigote attachment and invasion." Parasitology 138, no. 5 (January 27, 2011): 593–601. http://dx.doi.org/10.1017/s0031182010001678.

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SUMMARYCell surface glycosaminoglycans (GAGs) play an important role in the attachment and invasion process of a variety of intracellular pathogens. We have previously demonstrated that heparan sulfate proteoglycans (HSPG) mediate the invasion of trypomastigote forms ofTrypanosoma cruziin cardiomyocytes. Herein, we analysed whether GAGs are also implicated in amastigote invasion. Competition assays with soluble GAGs revealed that treatment ofT. cruziamastigotes with heparin and heparan sulfate leads to a reduction in the infection ratio, achieving 82% and 65% inhibition of invasion, respectively. Other sulfated GAGs, such as chondroitin sulfate, dermatan sulfate and keratan sulfate, had no effect on the invasion process. In addition, a significant decrease in infection occurred after interaction of amastigotes with GAG-deficient Chinese Hamster Ovary (CHO) cells, decreasing from 20% and 28% in wild-type CHO cells to 5% and 9% in the mutant cells after 2 h and 4 h of infection, respectively. These findings suggest that amastigote invasion also involves host cell surface heparan sulfate proteoglycans. The knowledge of the mechanism triggered by heparan sulfate-bindingT. cruziproteins may provide new potential candidates for Chagas disease therapy.

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Higashi, Kyohei, Keita Takeda, Ann Mukuno, Yusuke Okamoto, Sayaka Masuko, Robert J. Linhardt, and Toshihiko Toida. "Identification of keratan sulfate disaccharide at C-3 position of glucuronate of chondroitin sulfate from Mactra chinensis." Biochemical Journal 473, no. 22 (November 10, 2016): 4145–58. http://dx.doi.org/10.1042/bcj20160655.

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Glycosaminoglycans (GAGs), including chondroitin sulfate (CS), dermatan sulfate, heparin, heparan sulfate and keratan sulfate (KS) are linear sulfated repeating disaccharide sequences containing hexosamine and uronic acid [or galactose (Gal) in the case of KS]. Among the GAGs, CS shows structural variations, such as sulfation patterns and fucosylation, which are responsible for their physiological functions through CS interaction with CS-binding proteins. Here, we solved the structure of KS-branched CS-E derived from a clam, Mactra chinensis. KS disaccharide [d-GlcNAc6S-(1→3)-β-d-Gal-(1→] was attached to the C-3 position of GlcA, and consecutive KS-branched disaccharide sequences were found in a CS chain. KS-branched polysaccharides clearly exhibited resistance to degradation by chondroitinase ABC or ACII (at low concentrations) compared with typical CS structures. Furthermore, KS-branched polysaccharides stimulated neurite outgrowth of hippocampal neurons. These results strongly suggest that M. chinensis is a rich source of KS-branched CS, and it has important biological activities.

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Fukuda, K., H. Yamasaki, Y. Nagata, H. Motoyoshi, F. Matsumura, T. Kuno, and S. Tanaka. "Histamine H1-receptor-mediated keratan sulfate production in rabbit chondrocytes: involvement of protein kinase C." American Journal of Physiology-Cell Physiology 261, no. 3 (September 1, 1991): C413—C416. http://dx.doi.org/10.1152/ajpcell.1991.261.3.c413.

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We investigated the characteristics of the histamine H1-receptor in cultured rabbit chondrocytes. Scatchard analysis of [3H]pyrilamine, an H1-antagonist, binding to the chondrocytes revealed a single class of binding sites with KD and Bmax values of 90 +/- 12 nM and 56 +/- 11 fmol/10(4) cells, respectively. H1-agonists stimulated the production of keratan sulfate in a dose-dependent manner. Stimulation of keratan sulfate production was inhibited by pyrilamine. Protein kinase C inhibitors (sphingosine and H-7) also had inhibitory effects. Phorbol 12,13-dibutyrate, a direct activator of protein kinase C, activated the production. When protein kinase C in the chondrocytes was down-regulated by preincubation with phorbol ester, the effect of the H1-agonist on keratan sulfate production was abolished. These results indicate that the histamine H1-receptor on chondrocytes mediates the accumulation of keratan sulfate production and that protein kinase C is involved in these events.

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Viana, Gustavo M., David A. Priestman, Frances M. Platt, Shaukat Khan, Shunji Tomatsu, and Alexey V. Pshezhetsky. "Brain Pathology in Mucopolysaccharidoses (MPS) Patients with Neurological Forms." Journal of Clinical Medicine 9, no. 2 (February 1, 2020): 396. http://dx.doi.org/10.3390/jcm9020396.

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Mucopolysaccharidoses (MPS) are the group of lysosomal storage disorders caused by deficiencies of enzymes involved in the stepwise degradation of glycosaminoglycans. To identify brain pathology common for neurological MPS, we conducted a comprehensive analysis of brain cortex tissues from post-mortem autopsy materials of eight patients affected with MPS I, II, IIIA, IIIC, and IIID, and age-matched controls. Frozen brain tissues were analyzed for the abundance of glycosaminoglycans (heparan, dermatan, and keratan sulfates) by LC-MS/MS, glycosphingolipids by normal phase HPLC, and presence of inflammatory cytokines interleukin-6 (IL-6) and tumor necrosis factor superfamily member 10 (TNFSF10) by Western blotting. Fixed tissues were stained for the markers for microgliosis, astrogliosis, misfolded proteins, impaired autophagy, and GM2 ganglioside. Our results demonstrate that increase of heparan sulfate, decrease of keratan sulfate, and storage of simple monosialogangliosides 2 and 3 (GM2 and GM3) as well as the neutral glycosphingolipid, LacCer, together with neuroinflammation and neuronal accumulation of misfolded proteins are the hallmarks of brain pathology in MPS patients. These biomarkers are similar to those reported in the corresponding mouse models, suggesting that the pathological mechanism is common for all neurological MPS in humans and mice.

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Helenius, Terhi O., Julia O. Misiorek, Joel H. Nyström, Lina E. Fortelius, Aida Habtezion, Jian Liao, M. Nadeem Asghar, et al. "Keratin 8 absence down-regulates colonocyte HMGCS2 and modulates colonic ketogenesis and energy metabolism." Molecular Biology of the Cell 26, no. 12 (June 15, 2015): 2298–310. http://dx.doi.org/10.1091/mbc.e14-02-0736.

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Simple-type epithelial keratins are intermediate filament proteins important for mechanical stability and stress protection. Keratin mutations predispose to human liver disorders, whereas their roles in intestinal diseases are unclear. Absence of keratin 8 (K8) in mice leads to colitis, decreased Na/Cl uptake, protein mistargeting, and longer crypts, suggesting that keratins contribute to intestinal homeostasis. We describe the rate-limiting enzyme of the ketogenic energy metabolism pathway, mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase 2 (HMGCS2), as a major down-regulated protein in the K8-knockout (K8−/−) colon. K8 absence leads to decreased quantity and activity of HMGCS2, and the down-regulation is not dependent on the inflammatory state, since HMGCS2 is not decreased in dextran sulfate sodium-induced colitis. Peroxisome proliferator–activated receptor α, a transcriptional activator of HMGCS2, is similarly down-regulated. Ketogenic conditions—starvation or ketogenic diet—increase K8+/+ HMGCS2, whereas this response is blunted in the K8−/− colon. Microbiota-produced short-chain fatty acids (SCFAs), substrates in the colonic ketone body pathway, are increased in stool, which correlates with decreased levels of their main transporter, monocarboxylate transporter 1 (MCT1). Microbial populations, including the main SCFA-butyrate producers in the colon, were not altered in the K8−/−. In summary, the regulation of the SCFA-MCT1-HMGCS2 axis is disrupted in K8−/− colonocytes, suggesting a role for keratins in colonocyte energy metabolism and homeostasis.

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Gupta, Saloni, Kangana Sengar, Arulselvi Subramanian, and Gurudatta Satyarthee. "Morquio Syndrome Presenting with Dural Band Pathology: A Case Report." Journal of Laboratory Physicians 12, no. 04 (December 2020): 285–88. http://dx.doi.org/10.1055/s-0040-1722548.

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AbstractMorquio syndrome is caused by the deficiency of N-acetylgalactosamine-6-sulfate sulfatase (GALNS) enzyme, which is required for the catabolism of glycosaminoglycans (namely, chondroitin-6-sulfate and keratan sulfate). Pathogenic accumulation of these glycosaminoglycans occurs throughout the body. The various organs and tissues affected are bones, cartilage, tendon, teeth, trachea and lungs, heart, cornea, skin and connective tissues.Here, we present a case of Morquio syndrome. A 16-year-old boy presented with multiple skeletal abnormalities, including cervicomedullary compression by dorsal dural band in foramen magnum. The dural band was resected during the surgery to relieve compression and sent for histopathological examination. This case report not only reviews the clinical features and shows rare dural band histopathological findings but also mentions a note on the future therapies of this syndrome.

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Yoon, Jung Hae, Randolph Brooks, and Jaroslava Halper. "Immunoblotting Assays for Keratan Sulfate." Analytical Biochemistry 306, no. 2 (July 2002): 298–304. http://dx.doi.org/10.1006/abio.2002.5711.

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Mykhaliuk, V. V., and V. V. Havryliak. "Obtaining human hair keratin-based films and their characteristics." Studia Biologica 15, no. 1 (2021): 27–36. http://dx.doi.org/10.30970/sbi.1501.643.

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Background. Keratins are natural biopolymers with a wide range of applications in the field of biotechnology. Materials and Methods. Extraction of keratins was performed by a modified Nakamura method using 250 mM DTT. The protein concentration in the supernatant was determined by Bradford method. The protein composition was studied by their electrophoretic separation in a polyacrylamide gel in the presence of sodium dodecyl sulfate. The films were made by casting. The surface characteristics of the films were determined using a scanning electron microscope REMMA-102. The elemental composition of the films was determined using an X-ray microanalyzer. Results. The protein concentration in the supernatant was 3.75 mg/mL. After using dithiothreitol in the extraction mixture, we obtained proteins of intermediate filaments with a molecular weight of 40–60 kDa and a low Sulfur content. In the low molecular weight region, we obtained keratin-associated proteins with a molecular weight of 10–30 kDa and a high content of Sulfur. These proteins belong to fibrillar proteins, which can be used as a matrix for the creation of new keratin-containing biocomposites with a wide range of applications in reparative medicine and tissue engineering. Based on the obtained keratin extract, polymer films with and without the addition of glycerol were made. Scanning electron microscopy revealed that glycerol provided the film structure with homogeneity and plasticity due to the accumulation of moisture after the fixation by water vapor. The X-ray microanalysis of films revealed such elements as Sodium, Silicon, Sulfur, Potassium. Among the detected elements, Sulfur has the largest share that is due to the large number of disulfide bonds in the keratin molecule. Conclusions. The polymer keratin films with the addition of glycerol demonstrated better mechanical properties and can be used in biomedicine.

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Asari, A., S. Miyauchi, K. Miyazaki, A. Hamai, K. Horie, T. Takahashi, T. Sekiguchi, A. Machida, K. Kohno, and Y. Uchiyama. "Intra- and extracellular localization of hyaluronic acid and proteoglycan constituents (chondroitin sulfate, keratan sulfate, and protein core) in articular cartilage of rabbit tibia." Journal of Histochemistry & Cytochemistry 40, no. 11 (November 1992): 1693–704. http://dx.doi.org/10.1177/40.11.1431058.

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To demonstrate the intra- and extracellular localization of hyaluronic acid (HA) in articular cartilage of the rabbit tibia, biotinylated HA binding region, which specifically binds to the HA molecule, was applied to the tissue. In comparison with the localization of HA, that of chondroitin sulfate (CS), keratan sulfate (KS), and the protein core (PC) of the proteoglycan was examined by immunohistochemistry. Strong positive staining for HA was detected in chondrocytes located in the transition between the superficial and middle zones of the tissue. Pre-treatment with chondroitinase ABC, keratanase II, or trypsin enhanced the stainability for HA in peri- and intercellular matrices. Immunohistochemistry with or without enzymatic pre-treatment demonstrated that immunoreactivity for CS, KS, and PC was distinctly discerned in chondrocytes and in the extracellular matrix located in the middle and deep zones. In particular, the immunoreactivity for KS and PC was augmented by pre-treatment with chondroitinase ABC not only in chondrocytes but in the extracellular matrix located in the middle and deep zones. Microbiochemical analysis corresponded well with histochemical and immunohistochemical results. These results suggest that HA is abundantly synthesized and secreted in chondrocytes located in the transition between the superficial and middle zones.

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Day, Christopher J., Katharina Röltgen, Gerd Pluschke, and Michael P. Jennings. "The cell surface protein MUL_3720 confers binding of the skin pathogen Mycobacterium ulcerans to sulfated glycans and keratin." PLOS Neglected Tropical Diseases 15, no. 2 (February 25, 2021): e0009136. http://dx.doi.org/10.1371/journal.pntd.0009136.

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Mycobacterium ulceransis the causative agent of the chronic, necrotizing skin disease Buruli ulcer. Modes of transmission and molecular mechanisms involved in the establishment ofM.ulceransinfections are poorly understood. Interactions with host glycans are often crucial in bacterial pathogenesis and the 22 kDaM.ulceransprotein MUL_3720 has a putative role in host cell attachment. It has a predictedN-terminal lectin domain and aC-terminal peptidoglycan-binding domain and is highly expressed on the surface of the bacilli. Here we report the glycan-binding repertoire of whole, fixedM.ulceransbacteria and of purified, recombinant MUL_3720. On an array comprising 368 diverse biologically relevant glycan structures,M.ulceranscells showed binding to 64 glycan structures, representing several distinct classes of glycans, including sulfated structures. MUL_3720 bound only to glycans containing sulfated galactose and GalNAc, such as glycans known to be associated with keratins isolated from human skin. Surface plasmon resonance studies demonstrated that both whole, fixedM.ulceranscells and MUL_3720 show high affinity interactions with both glycans and human skin keratin extracts. This MUL_3720-mediated interaction with glycans associated with human skin keratin may contribute to the pathobiology of Buruli ulcer.

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Tai, Gui-Hua, Ian A. Nieduszynski, Nigel J. Fullwood, and Thomas N. Huckerby. "Human Corneal Keratan Sulfates." Journal of Biological Chemistry 272, no. 45 (November 7, 1997): 28227–31. http://dx.doi.org/10.1074/jbc.272.45.28227.

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Plaas, A. H. K., L. A. West, and R. J. Midura. "Keratan sulfate disaccharide composition determined by FACE analysis of keratanase II and endo- -galactosidase digestion products." Glycobiology 11, no. 10 (October 1, 2001): 779–90. http://dx.doi.org/10.1093/glycob/11.10.779.

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Hahn, R. A., and D. E. Birk. "beta-D xyloside alters dermatan sulfate proteoglycan synthesis and the organization of the developing avian corneal stroma." Development 115, no. 2 (June 1, 1992): 383–93. http://dx.doi.org/10.1242/dev.115.2.383.

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Corneal transparency is dependent upon the development of an organized extracellular matrix containing small diameter collagen fibrils with regular spacing, organized as orthogonal lamellae. Proteoglycan-collagen interactions have been implicated in the regulation of collagen fibrillogenesis and matrix assembly. To determine the role of dermatan sulfate proteoglycan in the development and organization of the secondary corneal stroma, its synthesis was disrupted using beta-D xyloside. The secondary corneal stroma contains two different proteoglycans, dermatan sulfate and keratan sulfate proteoglycan. beta-D xyloside interferes with xylose-mediated O-linked proteoglycan synthesis, and thus disrupts dermatan sulfate proteoglycan synthesis. Corneal keratan sulfate proteoglycan, a mannose-mediated N-linked proteoglycan, should not be altered. Biochemical analysis of corneas treated both in vitro and in ovo revealed a reduced synthesis of normally glycosylated dermatan sulfate proteoglycans and an increased synthesis of free xyloside-dermatan sulfate glycosaminoglycans. Keratan sulfate proteoglycan synthesis was unaltered in both cases. Corneal stromas were studied using histochemistry and electron microscopy after in ovo treatment with beta-D xyloside. The observed biochemical alterations in dermatan sulfate proteoglycans translated into disruptions in the organization of beta-D xyloside-treated stromas. There was a reduction in the histochemical staining of proteoglycans, but no alteration in collagen fibril diameter. In addition, focal alterations in collagen fibril packing, and a disruption of lamellar organization were observed in beta-D xyloside-treated corneas. These data suggest that dermatan sulfate proteoglycans are not involved in the regulation of corneal collagen fibril diameter, but are important in the fibril-fibril spacing as well as in lamellar organization, and cohesiveness.

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Klauser, Rainer J. "Induction of Fibrinolysis by Polyanions in Human Plasma." Thrombosis and Haemostasis 60, no. 02 (1988): 324–27. http://dx.doi.org/10.1055/s-0038-1647054.

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SummaryThe fibrinolytic potency of several polyanions was comparatively investigated. Fibrinolytic activity was measured in a whole plasma assay using H-D-Val-Leu-Lys-pNA (S-2251) as chromogenic substrate and by a fibrin plate assay using plasminogen rich fibrin plates.In the chromogenic substrate assay potent fibrinolytic polyanions comprised dextran sulfate, GAGPS, pentosan polysulfate, polyanethol sulfate, 1-carrageenan and i-carrageenan. Chon- droitin sulfates A, B, ‘C, keratan sulfate, ribonucleic acid, k-carrageenan and heparin were weakly fibrinolytic. Hyaluronic acid and lipopolysaccharide from E. coli were inactive.Similar results were obtained when fibrinolytic activity was measured by a fibrin plate assay. All polyanions except lipopolysaccharide produced lysis zones.Induction of fibrinolytic activity in human plasma was shown to be at least partially dependent on Hageman factor. In factor XII deficient plasma no fibrinolysis was induced by any of the polyanions when measured in the fibrin plate assay.In the. chromogenic substrate assay corn Hageman factor inhibitor (CHFI) inhibited the activation of S-2251 cleaving enzyme by GAGPS, pentosan poly sulfate, polyanethol sulfate, heparin, and ribonucleic acid near completely. The activation by dextran sulfate was inhibited by 45%.Heparin, pentosan polysulfate and GAGPS, three poly anions of therapeutic interest were separately compared. In both assays GAGPS proved the most potent activator, while pentosan poly sulfate exhibited 83% and 44% and heparin 32% and 14% of GAGPS fibrinolytic activity in the chromogenic substrate test and the fibrin plate assay, respectively.

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Sakamoto, Kazuma, and Kenji Kadomatsu. "Keratan Sulfate in Neuronal Network Reconstruction." Trends in Glycoscience and Glycotechnology 23, no. 133 (2011): 212–20. http://dx.doi.org/10.4052/tigg.23.212.

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Funderburgh, J. L., and G. W. Conrad. "Isoforms of corneal keratan sulfate proteoglycan." Journal of Biological Chemistry 265, no. 14 (June 1990): 8297–303. http://dx.doi.org/10.1016/s0021-9258(19)39071-4.

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Ueno, Rino, Katsuichi Miyamoto, Noriko Tanaka, Kota Moriguchi, Kenji Kadomatsu, and Susumu Kusunoki. "Keratan sulfate exacerbates experimental autoimmune encephalomyelitis." Journal of Neuroscience Research 93, no. 12 (September 5, 2015): 1874–80. http://dx.doi.org/10.1002/jnr.23640.

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Ying, Q. L., M. Kemme, D. Saunders, and S. R. Simon. "Glycosaminoglycans regulate elastase inhibition by oxidized secretory leukoprotease inhibitor." American Journal of Physiology-Lung Cellular and Molecular Physiology 272, no. 3 (March 1, 1997): L533—L541. http://dx.doi.org/10.1152/ajplung.1997.272.3.l533.

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Secretory leukoprotease inhibitor (SLPI) is one of the major physiological inhibitors protecting respiratory epithelium from attack by excess human leukocyte elastase (HLE), a serine protease released by neutrophils upon activation in response to inflammatory stimuli. Reaction with N-chlorotaurine, a major long-lived oxidant generated by activated neutrophils, oxidized all four methionine residues, but no other amino acids, in SLPI, resulting in substantial diminution of its elastase inhibitory activity. Oxidation of the P1' residue, Met73, accounted for most of the diminution in activity since a site-directed mutant of SLPI with leucine at the P1' position retained much higher residual activity after reaction with N-chlorotaurine. The diminished activity of oxidized SLPI could be almost completely restored when an iduronate-containing glycosaminoglycan, such as heparin, heparan sulfate, or dermatan sulfate, was added to the reaction medium. Addition of a sulfated glucuronate-containing glycosaminoglycan, chondroitin 4- or 6-sulfate, to the medium resulted in smaller but significant restoration of the lost activity, whereas the effects of hyaluronic acid and keratan sulfate were negligible. Kinetic analysis revealed that glycosaminoglycans greatly accelerated the association of oxidized SLPI and HLE, whereas iduronate-containing glycosaminoglycans also stabilized the enzyme-inhibitor complex formed. Based on these findings, we suggest that oxidized SLPI is a functionally active form of the inhibitor but that expression of its elastase inhibitory activity is regulated by sulfated uronate-containing glycosaminoglycans. Because its methionine residues have already been oxidized, this form of SLPI is resistant to the oxidant species that selectively attacks methionine residues in proteins. These findings indicate that SLPI may play a previously unexpected role in elastase inhibitory function in the lungs when significant inflammation is present.

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Powell, Adam W., Michael D. Taylor, T. Andrew Burrow, Robert J. Hopkin, Carlos E. Prada, and John L. Jefferies. "Widespread Vasculopathy in a Patient with Morquio A Syndrome." Texas Heart Institute Journal 44, no. 6 (December 1, 2017): 420–23. http://dx.doi.org/10.14503/thij-16-6121.

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Morquio A syndrome (mucopolysaccharidosis IV type A), an autosomal recessive lysosomal storage disorder caused by a defective N-acetylgalactosamine 6-sulfatase gene, leads to lysosomal accumulation of keratan sulfate and chondroitin 6-sulfate. This accumulation affects multiple systems and causes notable cardiovascular manifestations, such as thickening of the left-sided valves, ventricular hypertrophy, and intimal stenosis of the coronary arteries. There have been few reports of vasculopathy in this population. We present the case of a 58-year-old woman with Morquio A syndrome who was found to have aortic dilation on a routine screening echocardiogram. Magnetic resonance images revealed multiple tortuous, dilated arteries in her head, neck, and abdomen. The diffuse vasculopathy seen in this patient should prompt further study to determine whether this is an underreported phenomenon of clinical significance or an unusual finding in this rare disorder.

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Pomin, Vitor H., Adriana A. Piquet, Mariana S. Pereira, and Paulo A. S. Mourão. "Residual keratan sulfate in chondroitin sulfate formulations for oral administration." Carbohydrate Polymers 90, no. 2 (October 2012): 839–46. http://dx.doi.org/10.1016/j.carbpol.2012.06.009.

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Lawrence, Roger, Heather Prill, Preejith P. Vachali, Evan G. Adintori, Greg de Hart, Raymond Y. Wang, Barbara K. Burton, Marzia Pasquali, and Brett E. Crawford. "Characterization of disease-specific chondroitin sulfate nonreducing end accumulation in mucopolysaccharidosis IVA." Glycobiology 30, no. 7 (January 2, 2020): 433–45. http://dx.doi.org/10.1093/glycob/cwz109.

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Abstract Morquio syndrome type A, also known as MPS IVA, is a rare autosomal recessive disorder caused by deficiency of N-acetylgalactosamine-6-sulfatase, a lysosomal hydrolase critical in the degradation of keratan sulfate (KS) and chondroitin sulfate (CS). The CS that accumulates in MPS IVA patients has a disease-specific nonreducing end (NRE) terminating with N-acetyl-D-galactosamine 6-sulfate, which can be specifically quantified after enzymatic depolymerization of CS polysaccharide chains. The abundance of N-acetyl-D-galactosamine 6-sulfate over other possible NRE structures is diagnostic for MPS IVA. Here, we describe an assay for the liberation and measurement of N-acetyl-D-galactosamine 6-sulfate and explore its application to MPS IVA patient samples in pilot studies examining disease detection, effects of age and treatment with enzyme-replacement therapy. This assay complements the existing urinary KS assay by quantifying CS-derived substrates, which represent a distinct biochemical aspect of MPS IVA. A more complete understanding of the disease could help to more definitively detect disease across age ranges and more completely measure the pharmacodynamic efficacy of therapies. Larger studies will be needed to clarify the potential value of this CS-derived substrate to manage disease in MPS IVA patients.

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Peña, Michael, Clarrisa Williams, and Edward Pfeiler. "Structure of keratan sulfate from bonefish (Albula sp.) larvae deduced from NMR spectroscopy of keratanase-derived oligosaccharides." Carbohydrate Research 309, no. 1 (May 1998): 117–24. http://dx.doi.org/10.1016/s0008-6215(98)00128-1.

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Yamazaki, Yuji, Shunsaku Kimura, and Masashi Ohmae. "Reaction specificity of keratanase II in the transglycosylation using the sugar oxazolines having keratan sulfate repeating units." Carbohydrate Research 456 (February 2018): 61–68. http://dx.doi.org/10.1016/j.carres.2017.12.003.

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Zhang, Yuntao, Abigail H. Conrad, Elena S. Tasheva, Ke An, Lolita M. Corpuz, Yutaka Kariya, Kiyoshi Suzuki, and Gary W. Conrad. "Detection and Quantification of Sulfated Disaccharides from Keratan Sulfate and Chondroitin/Dermatan Sulfate during Chick Corneal Development by ESI-MS/MS." Investigative Opthalmology & Visual Science 46, no. 5 (May 1, 2005): 1604. http://dx.doi.org/10.1167/iovs.04-1453.

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Bayraktar, Halil, Evren Akal, Orkan Sarper, and Tereza Varnali. "Modeling glycosaminoglycans—hyaluronan, chondroitin, chondroitin sulfate A, chondroitin sulfate C and keratan sulfate." Journal of Molecular Structure: THEOCHEM 683, no. 1-3 (September 2004): 121–32. http://dx.doi.org/10.1016/j.theochem.2004.07.001.

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Lewis, D., Y. Davies, I. A. Nieduszynski, F. Lawrence, A. J. Quantock, R. Bonshek, and N. J. Fullwood. "Ultrastructural localization of sulfated and unsulfated keratan sulfate in normal and macular corneal dystrophy type I." Glycobiology 10, no. 3 (March 1, 2000): 305–12. http://dx.doi.org/10.1093/glycob/10.3.305.

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Sorrell, J. Michael, Fatemeh Mahmoodian, and Bruce Caterson. "Immunochemical characterization and ultrastructural localization of chondroitin sulfates and keratan sulfate in embryonic chick bone marrow." Cell and Tissue Research 252, no. 3 (June 1988): 523–31. http://dx.doi.org/10.1007/bf00216639.

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Kubota, Masayuki, Keiichi Yoshida, Akira Tawada, and Mamoru Ohashi. "Characterization of Oligosaccharides of the Lactosamine Series Derived from Keratan Sulfates by Tandem Mass Spectrometry." European Journal of Mass Spectrometry 6, no. 2 (April 2000): 193–203. http://dx.doi.org/10.1255/ejms.338.

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Positive- and negative-ion fast-atom bombardment tandem mass spectrometry with collision-induced dissociation (FAB-CID-MS/MS) has been used in the characterization of di-and tetra-saccharides of the lactosamine series from keratan sulfates. FAB-CID-MS/MS of Galβ1-4GlcNAc (L1) exhibited strong fragment ions originating from ring cleavage at the reducing-terminal sugar moiety together with glycosidic bond-cleavage ions, whereas GlcNAcβ1-3Gal (K1) showed strong glycosidic bond-cleavage ions but no ring-cleavage ions. A series of ring-cleavage fragment ions was observed with members of the L-series which have free hydroxyl groups at the C1 and C3 positions. CID-MS/MS spectra of the [M + Na – SO3]+ ion ( m/z 406) from L2 and the [M + Na − 2SO3]+ ion ( m/z 406) from L4 were almost identical with the CID-MS/MS spectrum of the [M + Na]+ ion ( m/z 406) from L1, which indicated that the sugar skeletons of L2 and L4 are the same as that of L1. On the other hand, the CID-MS/MS spectrum of the [M + Na – SO3]+ ion ( m/z 508) from L4 did not resemble that of the [M + Na]+ ion ( m/z 508) from L2. The former showed peaks that were additional to the peaks in the latter. Since these extra peaks were accounted for on the basis of the structure of L3 [Galβ1(6S)-4GlcNAc, S = sulfate], the in-source loss of sulfate groups by ester exchange upon FAB ionization takes place in a dual manner; one reaction at the non-reducing terminal sugar to give L2 and the other at the reducing-terminal sugar to give L3. The CID-MS/MS spectra were characteristic for the tetrasaccharides L1-L1, L2-L2 and L4-L4 while in-source fragmentation confirms the component disaccharides of each tetrasaccharide. The structure of a tetrasaccharide trisulfate was confirmed as L2–L4 and not L4–L2 by CID-MS/MS. Negative-ion FAB-CID-MS/MS spectra of the sulfated di-and tetra-saccharides showed a pattern similar to that of the positive-ion spectra. Subtraction of the CID-MS/MS spectrum of the [M – H]− ion of L2 [Galβ1-4GlcNAc(6S)] from that of the [M – H – SO3]− ion of L4 [Gal(6S)β1-4GlcNAc(6S)] gave several specific ions whose origins were nicely explained on the basis of the structure of L3. The structure of a pentasaccharide consisting of N-acetylneuraminic acid and a tetrasaccharide trisulfate was confirmed, on the basis of FAB-CID-MS/MS, as NeuNAcα2-6L2-L4.

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Ren, Qiang, Jian Wang, Chao Liu, Ling-xin Meng, Rui-kun Qian, Hui-jie Gao, Wei Qin, et al. "Exploring the sulfate patterns of chondroitin sulfate/dermatan sulfate and keratan sulfate in human pancreatic cancer." Journal of Pharmaceutical and Biomedical Analysis 205 (October 2021): 114339. http://dx.doi.org/10.1016/j.jpba.2021.114339.

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Kavanagh, Emma, Anne C. Osborne, Doreen E. Ashhurst, and Andrew A. Pitsillides. "Keratan Sulfate Epitopes Exhibit a Conserved Distribution During Joint Development That Remains Undisclosed on the Basis of Glycosaminoglycan Charge Density." Journal of Histochemistry & Cytochemistry 50, no. 8 (August 2002): 1039–47. http://dx.doi.org/10.1177/002215540205000806.

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Changes in glycosaminoglycan (GAG) content and distribution are vital for joint development. However, their precise character has not been established. We have used immunohistochemistry (IHC) and “critical electrolyte” Alcian blue staining to assess such changes in developing chick and rabbit joints. IHC showed chondroitin sulfate labeling in chick epiphyseal cartilage but not in interzones. In contrast, prominent labeling for keratan sulfate (KS) was restricted to chick cartilage–interzone interfaces. In rabbit knees, KS labeling was also prominent at presumptive cavity borders, but weak in interzone and cartilage. Selective pre-digestion produced appropriate loss of label and undersulfated KS was undetectable. Quantification of Alcian blue staining by scanning and integrating microdensitometry showed prominent hyaluronan-like (HA-like) interzone staining, with chondroitin sulfate and weaker KS staining restricted to epiphyseal cartilage. Hyaluronidase decreased HA-like staining in the interzone. Surprisingly, keratanases also reduced HA-like but not sulfated GAG (sGAG-like) staining in the interzone. Chondroitinase ABC had little effect on HA-like staining but decreased sGAG staining in all regions. Rabbit joints also showed HA-like but not KS staining in the interzone and strong chondroitin sulfate-like staining in epiphyseal cartilage. Our findings show restricted KS distribution in the region close to the presumptive joint cavity of developing chick and rabbit joints. Alcian blue staining does not detect this moiety. Therefore, it appears that although histochemistry allows relatively insensitive quantitative assessment of GAGs, IHC increases these detection limits. This is particularly evident for KS, which exhibits immunolabeling patterns in joints from different species that is consistent with a conserved functional role in chondrogenesis.

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Journal articles on the topic 'Keratane sulfate'

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