Log in

Relevant bibliographies by topics / Keratane sulfate

Contents

Journal articles
Dissertations / Theses
Book chapters
Conference papers

Academic literature on the topic 'Keratane sulfate'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Keratane sulfate.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Keratane sulfate"

1

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

2

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

3

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

4

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.

Full text

Abstract:

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).

APA, Harvard, Vancouver, ISO, and other styles

5

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

7

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.

Full text

Abstract:

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.

APA, Harvard, Vancouver, ISO, and other styles

8

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

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.

Full text

APA, Harvard, Vancouver, ISO, and other styles

More sources

Dissertations / Theses on the topic "Keratane sulfate"

1

BON, EMMANUEL. "Dosage serique des keratanes sulfates : application a la polyarthrite rhumatoide ; influence des corticoides." Toulouse 3, 1993. http://www.theses.fr/1993TOU31554.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Camelier, Marli Teresinha Viapiana. "Diagnóstico de mucopolissacaridose tipo IVA em amostras de sangue impregnado em papel filtro." reponame:Biblioteca Digital de Teses e Dissertações da UFRGS, 2011. http://hdl.handle.net/10183/30961.

Full text

Abstract:

INTRODUÇÃO: As mucopolissacaridoses (MPS) são doenças de depósito lisossômico, caracterizadas pela deficiência de enzimas lisossômicas envolvidas na degradação dos glicosaminoglicanos (GAGs). O acúmulo anormal dessas macromoléculas no interior dos lisossomos provoca alterações estruturais e funcionais, de caráter multissistêmico e progressivo. Os GAGs acumulados também são excretados na urina, onde podem ser identificados através de diversos métodos bioquímicos. Estas doenças estão presentes em todos os grupos étnicos e a incidência conjunta das MPS, é estimada entre 1:10.000 a 1:25.000 nascidos vivos. (Baehner, 2005). A causa das MPS é a deficiência de uma enzima específica na rota de degradação dos GAGs. As MPS são classificadas segundo o tipo de substrato (GAGs) acumulado e a enzima específica deficiente. Na síndrome de Morquio A, ou mucopolissacaridose tipo IVA (MPS IVA), o substrato acumulado é o queratan sulfato e a enzima deficiente é a N-acetilgalactosamina-6-sulfatase. (GALNS). Os pacientes afetados por MPS IVA apresentam baixa estatura, disostose múltipla, opacidade de córnea, entre outros sinais e sintomas. O desenvolvimento psicomotor e mental é normal. O método de detecção inicial das MPS baseia-se na identificação dos GAGs, que são excretados em excesso na urina destes pacientes. A presença de queratan sulfato na eletroforese ou a detecção de níveis aumentados na dosagem quantitativa, direciona a investigação laboratorial para a MPS IV. O diagnóstico definitivo se estabelece através da medida da atividade enzimática em leucócitos ou fibroblastos, onde se constata a deficiência enzimática. OBJETIVOS: Este estudo teve como objetivo principal, tornar disponível um novo método, mais simples, rápido e acessível, para o diagnóstico bioquímico de mucopolissacaridose tipo IVA, utilizando amostras de sangue impregnadas em papel filtro (SIPF). MATERIAIS E MÉTODOS: Amostras de SIPF e leucócitos de 35 pacientes de ambos os sexos, com idade entre 3 e 47 anos, com diagnóstico previamente estabelecido de MPS IVA, pelo método convencional, em leucócitos e /ou fibroblastos, foram analisadas. Para o estabelecimento dos valores de referência, foram estudadas amostras de leucócitos e de SIPF de 54 indivíduos saudáveis (18-50 anos), de ambos os sexos. Após assinatura do termo de consentimento, amostras de sangue periférico de pacientes e controles, foram coletadas, para a obtenção de leucócitos e sangue impregnado em papel filtro.(SIPF). Os ensaios enzimáticos foram realizados nas amostras de leucócitos e SIPF, simultaneamente, para comparar os resultados. RESULTADOS: Os resultados obtidos nos ensaios enzimáticos de todos os pacientes apresentando MPS IVA, confirmaram a deficiência da atividade enzimática em ambos materiais (leucócitos e SIPF) com uma diferença estatisticamente significativa em relação ao grupo controle. (Mann-Witney U test, p< 0,001). Neste estudo, a medida de GALNS em amostras de SIPF permitiu a identificação dos pacientes com MPS IVA, com sensibilidade de 100 %. Os testes de estabilidade realizados nas amostras de SIPF indicaram que amostras coletadas para a medida da atividade de GALNS devem ser mantidas a 4ºC sempre que possível, sendo estáveis nesta temperatura por mais de 30 dias. CONCLUSÕES: Nas condições utilizadas, amostras de SIPF se mostraram adequadas para a identificação segura de pacientes com MPS tipo IVA. O método que utiliza amostras de SIPF é mais acessível e rápido, simplificando a etapa de coleta e transporte, podendo ser utilizado para detectar pacientes afetados, especialmente em áreas de difícil acesso para a coleta e transporte de amostras líquidas.
INTRODUCTION: Mucopolysaccharidosis (MPS) are lysosomal deposit diseases characterized by lysosomal enzymes deficiency involved in the degradation of glycosaminoglycans (GAGs). The abnormal accumulation of these macromolecules inside the lysosomes provokes structural and functional alterations multi-systemically and progressively. The accumulated GAGs are also excreted in the urine, where they may be identified through many different biochemical methods. These diseases occur among all ethnical groups and the combined incidence of MPS is estimated at 1:10.000 to 1:25.000 live births. (Baehner, 2005). The MPS’ cause is the deficiency of a specific enzyme in the GAGs degradation route. The MPS are classified according to a type of substrate accumulated (GAGs) and the deficiency of a specific enzyme. In Morquio syndrome A or Mucopolysaccharidosis type IVA (MPS IVA), the accumulated substrate is the keratan sulfate and the deficient enzyme is the N-acetylgalactosamine-6-sulfatase (GALNS). The patients affected by MPS IVA present short stature, dysostosis multiplex, corneal opacity, among others signs and symptoms. The cognitive and mental developments are normal. The MPS initial detection method is based on the identification of the GAGs which are excreted in the patients’ urine. The presence of the keratan sulphate in the electrophoresis or the detection of the increased levels in the quantitative dosage directs the laboratory investigation to MPS IV. The definitive diagnosis is established through measuring the enzymatic activity in leukocytes or fibroblasts, in which the enzymatic deficiency is proved. OBJECTIVE: This study’s main purpose is to offer an original, simpler, faster and more accessible method for biochemical diagnosis of Mucopolysaccharidosis type IVA using dried blood samples (DBS). MATERIALS AND METHODS: DBS and leukocytes from 35 patients from both sexes between 3 and 47 years of age with previously established diagnosis of MPS IVA through the conventional method in leukocytes and/or fibroblasts were analyzed. In order to establish reference values DBS and leukocytes samples from 54 healthy people (18-50 years of age) from both sexes were studied. After signing a paper consent form, peripheral blood samples from patients and controls were collected for obtaining leukocytes and dried blood samples (DBS). To validate the method, we made a simultaneous GALNS assay in leukocytes and DBS. RESULTS: The results obtained in the enzymatic assays from all patients presenting MPS IVA confirmed the deficiency of enzymatic activity in both materials (leukocytes and DBS) with a significant statistical difference in relation to the control group. (Mann-Witney U tes, p< 0,001). In this study, the quantity of GALNS in DBS allowed the identification of patients with MPS IVA with sensibility of 100%. The stability tests indicate that DBS samples collected for measuring the activity of GALNS must be kept at 4ºC whenever possible, being stable in this temperature for more than 30 days. CONCLUSION: In the used conditions, DBS were adequate for a safe identification of patients with MPS type IVA. The method which utilizes DBS is cheaper and faster, what simplifies the collection and transportation stage and can be used to detect affected patients especially in difficult access areas for the collection and transportation of liquid samples.

APA, Harvard, Vancouver, ISO, and other styles

3

"Catabolism of glycoconjugates (keratan sulfate)." Tulane University, 1986.

Find full text

Abstract:

This dissertation is based on published and unpublished results related to the catabolism of various type of glycoconjugates The catabolism of GM$\sb{2}$ ganglioside was studied in the roe of striped mullet (Mugil cephalus). This tissue was selected since it contains GM$\sb{2}$ as a major ganglioside. Mullet roe GM$\sb{2}$ was isolated in pure form and fully characterized in its saccharide and ceramide portion. It was found that mullet roe $\beta$-hexosaminidase A required the assistance of a specific activator protein in order to cleave GM$\sb{2}$. This protein was purified and its properties and specificity were studied. During these studies it was also found that mullet roe contains a protein capable of inhibiting the hydrolysis of GM$\sb{2}$. These results indicated that mullet roe could be used as a model system to study the catabolism of GM$\sb{2}$ and its regulation since from the same tissue one can isolate GM$\sb{2}$, $\beta$-hexosaminidase A activator protein and inhibitor protein The role of the endoglycosidases in the catabolism of glycoconjugates in human tissues was the other topic examined. From human urine two different forms of this enzyme (Endo-U1 and Endo-U2) were separated. Endo-U1 was found to cleave only high mannose type asparaginyl-glycopeptides while Endo-U2 on the other hand could cleave both complex type and high mannose type asparaginyl-glycopeptides. Endo-U1 but not U2 was found to cleave glycopeptides acetylated at the amino group of asparagine. Urine were also found to contain an endo-$\beta$-galactosidase activity. This enzyme had been previously isolated from bacteria but its presence in human fluid or tissues had never been reported before. The interest in the catabolism of polylactosaminoglycans was partly aroused by the finding that brain and liver of GM$\sb{1}$-gangliosidosis patients accumulate glycoproteins containing N-acetyllactosamine repeating units Human endo-$\beta$-galactosidase could cleave both sulfated and non-sulfated polylactosaminoglycan with the release of oligosaccharides containing galactose at the reducing end. The discovery of this enzyme indicates the existence of an alternative catabolic pathway for polylactosamininoglycans beside the proposed sequential exoglycosidase digestion. (Abstract shortened with permission of author.)
acase@tulane.edu

APA, Harvard, Vancouver, ISO, and other styles

4

平野, 健一, and Kenichi Hirano. "Ablation of Keratan Sulfate Accelerates Early Phase Pathogenesis of ALS." Thesis, 2013. http://hdl.handle.net/2237/18980.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

松井, 寛樹, and Hiroki Matsui. "Keratan Sulfate Expression in Microglia Is Diminished in the Spinal Cord in Experimental Autoimmune Neuritis." Thesis, 2014. http://hdl.handle.net/2237/20036.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

LOCEY, BETTY J. "IMPACT OF BIS-(BETA-CHLOROETHYL) SULFIDE ON KERATIN PROTEIN AND INTERMEDIATE FILAMENTS IN CULTURED KERATINOCYTES AS INDICATED BY MONOCLONAL ANTIBODY BINDING." 1988. http://books.google.com/books?id=iBg-AAAAMAAJ.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Book chapters on the topic "Keratane sulfate"

1

Fukuta, Masakazu, and Osami Habuchi. "Keratan Sulfate Gal-6-Sulfotransferase." In Handbook of Glycosyltransferases and Related Genes, 418–22. Tokyo: Springer Japan, 2002. http://dx.doi.org/10.1007/978-4-431-67877-9_59.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Schomburg, Dietmar, and Margit Salzmann. "Keratan-sulfate endo-1, 4-beta-galactosidase." In Enzyme Handbook 4, 531–34. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-84437-9_92.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Uchimura, Kenji. "Keratan Sulfate: Biosynthesis, Structures, and Biological Functions." In Methods in Molecular Biology, 389–400. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-1714-3_30.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Shimada, Tsutomu, Shunji Tomatsu, Robert W. Mason, Eriko Yasuda, William G. Mackenzie, Jobayer Hossain, Yuniko Shibata, et al. "Di-sulfated Keratan Sulfate as a Novel Biomarker for Mucopolysaccharidosis II, IVA, and IVB." In JIMD Reports, 1–13. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/8904_2014_330.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Habuchi, Osami. "Carbohydrate (Keratan Sulfate Gal-6) Sulfotransferase 1 (CHST1)." In Handbook of Glycosyltransferases and Related Genes, 989–96. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54240-7_42.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Greiling, H. "Structure and biological functions of keratan sulfate proteoglycans." In Proteoglycans, 101–22. Basel: Birkhäuser Basel, 1994. http://dx.doi.org/10.1007/978-3-0348-7545-5_7.

Full text

APA, Harvard, Vancouver, ISO, and other styles

7

Huckerby, Thomas N., Gavin M. Brown, Robert M. Lauder, and Ian A. Nieduszynski. "Keratan Sulfates: Structural Investigations Using NMR Spectroscopy." In ACS Symposium Series, 289–97. Washington, DC: American Chemical Society, 2002. http://dx.doi.org/10.1021/bk-2003-0834.ch022.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Bedini, Emiliano, Maria Michela Corsaro, Alfonso Fernández-Mayoralas, and Alfonso Iadonisi. "Chondroitin, Dermatan, Heparan, and Keratan Sulfate: Structure and Functions." In Biologically-Inspired Systems, 187–233. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-12919-4_5.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Imagama, Shiro, Zenya Ito, Kei Ando, Yukihiro Matsuyama, Yoshihiro Nishida, and Naoki Ishiguro. "The Proteoglycan-Degrading Enzymes Promote Functional Recovery After Spinal Cord Injury: Keratan Sulfate and Chondroitin Sulfate." In Neuroprotection and Regeneration of the Spinal Cord, 169–91. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54502-6_15.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Kawasaki, Toshisuke, Nobuko Kawasaki, Hiromi Nakao, and Hidenao Toyoda. "Novel Antibody for Keratan Sulfate Expressed on Human iPS/ES Cells." In Glycoscience: Biology and Medicine, 1457–64. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54841-6_94.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Keratane sulfate"

1

Yoshida, Takayuki, Cong-xiao Gao, Tomoko Betsuyaku, Fumi Ota, Akio Matsumoto, Masaharu Nishimura, and Naoyuki Taniguchi. "Glycan X, A Keratan Sulfate Oligosaccharide, Attenuates Elastase-induced Lung Inflammation And Emphysema In Mice." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a4978.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Hatami-Marbini, Hamed, and Ebitimi Etebu. "Influence of Ionic Concentration on Swelling Behavior and Shear Properties of the Bovine Cornea." In ASME 2012 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/sbc2012-80896.

Full text

Abstract:

The mechanical properties and structure of connective tissues such as the cornea and the cartilage are derived from the functions and properties of their extracellular matrix, a polyelectrolyte gel composed of collagenous fibers embedded in an aqueous matrix. The collagen fibers in the extracellular matrix of the corneal stroma are arranged in regular lattice structures, which is necessary for corneal transparency and transmitting the incident light to the back of the eye. This regular pseudo hexagonal arrangement is attributed to the interaction of collagen fibers with the proteoglycans as these regularities are lost in knock-out mice [i]. Proteoglycans (PGs) are heavily glycosylated glycoproteins. They consist of a core protein to which is glycosaminoglycan chains are covalently attached. The main PG in the corneal stroma is the proteoglycan decorin. Decorin is the simplest small leucine-rich PG and only has a single glycosaminoglycan side chain. It has a horse shape core protein and binds collagen fibrils at regular sites. Chondroitin sulfate (CS), dermatan sulfate (DS), keratan sulfate (KS) are among the prevalent glycosaminoglycans found in the cornea. Under physiological conditions, these linear carbohydrate polymers are ionized and carry negative charges due to the presence of negatively charged carboxylate and sulfate groups. Therefore, a hydrated gel is formed in the empty space between collagen fibrils by attracting water. The interaction of negatively charged glycosaminoglycans with themselves and their interaction with the free ions contribute to the corneal swelling pressure and subsequently to its compressive stiffness. From structural view point, the corneal stroma is a composite polyelectrolyte system in which the observed regular spacings of the collagens are suggested to exist because of the structural interaction of collagens, negatively charged glycosaminoglycans, and the free ions in the interfibrillar space.

APA, Harvard, Vancouver, ISO, and other styles

3

Tomaslni, B. R., and D. F. Mosher. "PREFERENTIAL RECOGNITION OF VITRONECTIN (S-PR0TEIN) BY A MONOCLONAL ANTIBODY UPON INTERACTION WITH THROMBIN, ANTITHROMBIN AND GLYCOSAMINOGLYCANS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643634.

Full text

Abstract:

V1tronect1n/S-Prote1n (VN/SP) is a glycoprotein present at a concentration of 200-400 ug/ml 1n plasma and serum. It has been shown to promote cel 1-substratum adhesion and to act as an Inhibitor of the membrane attack complex of complement and of the inactivation of thrombin by antithrombin III in the presence of low levels of heparin. We have previously shown that VN/SP binds more avidly to heparln-agarose and to a monoclonal antibody (MaVN/SP)-Sepharose column when present 1n serum rather than 1n plasma. In order to examine the possibility of a serum-induced conformational change, we utilized, 1n this study, an Indirect enzyme-linked Immunosorbent system to test for the exposure of new antigenic determinants. When MaVN/SP was Incubated with plasma or serum, recognition of VN/SP 1n serum was approximately 50 fold greater than recognition of VN/SP in plasma. Since VN/SP has been shown to Interact strongly with the thromb1n-ant1thrombin complex, we examined the antigenicity of VN/SP when Incubated with thrombin and antithrombin 1n the presence and absence of heparin. Incubation of VN/SP with heparin promoted a 2.5-fold Increase 1n recognition by MaVN/SP. When MaVN/SP was Incubated with thromb1n-ant1thrombin but not thrombin or antithrombin alone, recognition was Increased by 7-fold 1n the absence of heparin and by 32-fold 1n the presence of heparin. This differential recognition of VN/SP was not observed with a second monoclonal antibody raised originally against S-Prote1n. Treatment of VN/SP with various glycosaminoglycans and polysaccharides demonstrated the following relative potencies for Induction of the partial antigenic change: dextran sulfate>fucoidan>heparin> dermatan suIfate>hyaluronic acid. No effect was detected upon Incubation of VN/SP with keratan sulfate, heparan sulfate or chondroltln sulfate. These data suggest a conformational change Induced by thrombin-antlthrombin which may allow VN/SP to Interact more avidly with other molecules such as heparin. The physiological role of this putative conformational change is under investigation.

APA, Harvard, Vancouver, ISO, and other styles

4

Rahimi, Abdolrasol, and Hamed Hatami-Marbini. "Hydration Effects on Tensile Properties of the Corneal Stroma." In ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14788.

Full text

Abstract:

The mechanical behavior of the cornea is mainly governed by the microstructure and composition of the stroma. The stroma is a highly ordered extracellular matrix and constitutes about 90% of the corneal thickness. From the mechanics point of view, the corneal stroma can be considered as a polyelectrolyte gel which is composed of collagen fibrils embedded in an aqueous matrix. The collagen fibrils compose about 70% of cornea’s dry mass and are arranged in a regular lattice structure [2]. Previous studies have shown that while the collagen fibrils are primarily located parallel to the surface, they are not distributed uniformly in all directions and their preferred orientation is not same in different species. For example, collagen fibrils are almost equally distributed in the nasal-temporal and inferior-superior directions in healthy human corneas [4] and they are mainly aligned in the inferior-superior direction in bovine corneas[2]. The differences in the orientations of the collagen fibrils have seen to have important implications on the mechanical properties of the cornea. In addition to this observation, the relative distance between the collagen fibrils is expected to play a role in defining the mechanics of the tissue. It is well-documented that the proteoglycans bind collagen fibrils at regular sites and control their relative position. The main proteoglycan in the corneal stroma is decorin. Decorin is the simplest small leucine-rich proteoglycan with a single glycosaminoglycan side chain. Chondroitin sulfate, dermatan sulfate, and keratan sulfate are among the prevalent glycosaminoglycans found in the cornea. Under physiological conditions, these linear carbohydrate polymers are ionized and carry negative charges. Therefore, a hydrated gel is formed in the empty space between collagen fibrils by attracting water. It is known that the interaction of these negatively charged glycosaminoglycans with themselves and with the free ions contribute to the corneal swelling pressure and subsequently to its compressive stiffness. Nevertheless, their possible influence on the corneal tensile properties is yet to be determined. In this work, we experimentally characterized the tensile properties of the bovine corneal stroma in different bathing solutions. Furthermore, a quasi-linear viscoelastic (QLV) model was used to examine the effect of bathing fluids and corneal hydration on mechanical parameter of the cornea.

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!