scholarly journals The structure and composition of cartilage keratan sulphate

1974 ◽  
Vol 141 (2) ◽  
pp. 517-526 ◽  
Author(s):  
John J. Hopwood ◽  
H. Clem Robinson
Keyword(s):  
Intervertebral Disc ◽  
Nasal Septum ◽  
Alkali Treatment ◽  
Neuraminic Acid ◽  
Keratan Sulphate ◽  
Molecular Parameters ◽  
Acetylneuraminic Acid ◽  
Different Types

Keratan sulphate was isolated from bovine intervertebral disc and bovine nasal septum after hydrolysis with proteinases and treatment with dilute alkali. Each preparation was found to contain, per keratan sulphate chain: (a) 1 residue of mannose; (b) 3 residues of N-acetylneuraminic acid (2 residues after alkali treatment); (c) 1 residue of N-acetylgalactosamine (lost after alkali treatment); (d) 1 residue or less of fucose. N-Acetyl-neuraminic acid residues were at non-reducing termini and were bonded to keratan sulphate through galactose residues. Evidence is presented for two different types of linkage between skeletal keratan sulphate and protein. Consideration of molecular parameters and compositions leads to a proposed structure for keratan sulphate–protein as found in skeletal proteoglycans.

scholarly journals There are two major types of skeletal keratan sulphates

1990 ◽  
Vol 271 (1) ◽  
pp. 243-245 ◽  
Author(s):  
I A Nieduszynski ◽  
T N Huckerby ◽  
J M Dickenson ◽  
G M Brown ◽  
G H Tai ◽  
...  
Keyword(s):  
Intervertebral Disc ◽  
Nasal Septum ◽  
High Field ◽  
Structural Features ◽  
Spectroscopic Studies ◽  
Neuraminic Acid ◽  
Keratan Sulphate

High-field 1H-n.m.r.-spectroscopic studies supported by chemical carbohydrate analyses show that skeletal keratan sulphates (KS-II) of bovine origin may be sub-classified into two groups. Keratan sulphate chains from articular and intervertebral-disc cartilage (KS-II-A) contain two structural features, namely alpha(1----3)-fucose and alpha(2----6)-linked N-acetyl-neuraminic acid residues, that are absent from keratan sulphates from tracheal or nasal-septum cartilage (KS-II-B).

scholarly journals The alkali-labile linkage between keratan sulphate and protein

1974 ◽  
Vol 141 (1) ◽  
pp. 57-69 ◽  
Author(s):  
John J. Hopwood ◽  
H. Clem Robinson
Keyword(s):  
Intervertebral Disc ◽  
Chondroitin Sulphate ◽  
Alkali Treatment ◽  
Glycosidic Bond ◽  
Proteus Vulgaris ◽  
Keratan Sulphate ◽  
Covalently Bonded ◽  
Sequential Digestion

Keratan sulphate was isolated from adult intervertebral disc in 90% yield by sequential digestion of the whole tissue with papain, Pronase and Proteus vulgaris chondroitin sulphate lyase. Treatment of this preparation with alkali cleaved a glycosidic bond between N-acetylgalactosamine and threonine and produced, by an alkali-catalysed ‘peeling’ reaction, an unsaturated derivative of N-acetylgalactosamine which reacted as a chromogen in the Morgan–Elson reaction, but remained covalently bonded to the keratan sulphate chain. This derivative was reduced and labelled by alkaline NaB3H4. The substituent at position 3 of N-acetylgalactosamine in the keratan sulphate–protein linkage was identified as a disaccharide, N-acetylneuraminylgalactose, which was isolated from the reaction mixture after alkali treatment.

scholarly journals Skeletal keratan sulphate chains isolated from bovine intervertebral disc may terminate in α(2----6)-linked N-acetylneuraminic acid

1992 ◽  
Vol 282 (1) ◽  
pp. 267-271 ◽  
Author(s):  
J M Dickenson ◽  
T N Huckerby ◽  
I A Nieduszynski
Keyword(s):  
Intervertebral Disc ◽  
Anion Exchange ◽  
Gel Permeation Chromatography ◽  
Intervertebral Discs ◽  
Borohydride Reduction ◽  
Anion Exchange Column ◽  
Keratan Sulphate ◽  
Acetylneuraminic Acid ◽  
Sialidase Inhibitor ◽  
Gel Permeation

Peptido-keratan sulphate fragments were isolated from the nucleus pulposus of bovine intervertebral discs (2-year-old animals) after digestion with chondroitin ABC lyase followed by digestion with diphenylcarbamoyl chloride-treated trypsin of A1D1 proteoglycans and gel-permeation chromatography on Sepharose CL-6B. The peptido-keratan sulphate fragments were subjected to alkaline borohydride reduction. The reduced chains were treated with keratanase in the presence of the sialidase inhibitor 2,3-dehydro-2-deoxy-N-acetylneuraminic acid, and the digest was subjected to alkaline borohydride reduction. This produced oligosaccharides with galactitol at their reducing ends. This reduced digest was chromatographed on a Nucleosil 5 SB anion-exchange column and individual oligosaccharides were isolated. One of these was shown by 600 MHz 1H-n.m.r. spectroscopy to have the following structure: NeuAc alpha 2-6Gal beta 1-4GlcNAc(6-SO4)beta 1-3Gal-ol The structure of this oligosaccharide shows that keratan sulphate chains from bovine intervertebral disc have non-reducing termini with N-acetylneuraminic acid linked alpha(2----6) as well as alpha(2----3) to an unsulphated galactose.

scholarly journals Caspase-3 knockout inhibits intervertebral disc degeneration related to injury but accelerates degeneration related to aging

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Takashi Ohnishi ◽  
Katsuhisa Yamada ◽  
Koji Iwasaki ◽  
Takeru Tsujimoto ◽  
Hideaki Higashi ◽  
...  
Keyword(s):  
Intervertebral Disc ◽  
Intervertebral Disc Degeneration ◽  
Caspase 3 ◽  
Treatment Target ◽  
Age Related ◽  
Different Types ◽  
New Treatments ◽  
Surgical Treatments ◽  
Ivd Degeneration ◽  
Primary Effector

AbstractApproximately 40% of people under 30 and over 90% of people 55 or older suffer from moderate-to-severe levels of degenerative intervertebral disc (IVD) disease in their lumbar spines. Surgical treatments are sometimes effective; however, the treatment of back pain related to IVD degeneration is still a challenge; therefore, new treatments are necessary. Apoptosis may be important in IVD degeneration because suppressing cell apoptosis inside the IVD inhibits degeneration. Caspase-3, the primary effector of apoptosis, may be a key treatment target. We analyzed caspase-3’s role in two different types of IVD degeneration using caspase-3 knockout (Casp-3 KO) mice. Casp-3 KO delayed IVD degeneration in the injury-induced model but accelerated it in the age-induced model. Our results suggest that this is due to different pathological mechanisms of these two types of IVD degeneration. Apoptosis was suppressed in the IVD cells of Casp-3 KO mice, but cellular senescence was enhanced. This would explain why the Casp-3 KO was effective against injury-induced, but not age-related, IVD degeneration. Our results suggest that short-term caspase-3 inhibition could be used to treat injury-induced IVD degeneration.

scholarly journals Kinetic studies on the acid hydrolysis of the methyl ketoside of unsubstituted and O-acetylated N-acetylneuraminic acid

1973 ◽  
Vol 133 (4) ◽  
pp. 623-628 ◽  
Author(s):  
A. Neuberger ◽  
Wendy A. Ratcliffe
Keyword(s):  
Sialic Acid ◽  
Acid Hydrolysis ◽  
Model Compound ◽  
Kinetic Studies ◽  
Order Rate Constant ◽  
Neuraminic Acid ◽  
Acetylneuraminic Acid ◽  
Rate Of Hydrolysis ◽  
Ph Range ◽  
Hydrolysis Of

The hydrolysis of the model compound 2-O-methyl-4,7,8,9-tetra-O-acetyl-N-acetyl-α-d-neuraminic acid and neuraminidase (Vibrio cholerae) closely resembled that of the O-acetylated sialic acid residues of rabbit Tamm–Horsfall glycoprotein. This confirmed that O-acetylation was responsible for the unusually slow rate of acid hydrolysis of O-acetylated sialic acid residues observed in rabbit Tamm–Horsfall glycoprotein and their resistance to hydrolysis by neuraminidase. The first-order rate constant of hydrolysis of 2-methyl-N-acetyl-α-d-neuraminic acid by 0.05m-H2SO4 was 56-fold greater than that of 2-O-methyl-4,7,8,9-tetra-O-acetyl-N-acetyl -α-d-neuraminic acid. Kinetic studies have shown that in the pH range 1.00–3.30, the observed rate of hydrolysis of 2-methyl-N-acetyl-α-d-neuraminic acid can be attributed to acid-catalysed hydrolysis of the negatively charged CO2− form of the methyl ketoside.

A synthesis of N-acetylneuraminic acid and [6-2H]-N-acetyl-neuraminic acid from N-acetyl-d-glucosamine

1987 ◽  
Vol 164 ◽  
pp. 415-432 ◽  
Author(s):  
Radomir Julina ◽  
Ingrid Müller ◽  
Andrea Vasella ◽  
René Wyler
Keyword(s):  
Neuraminic Acid ◽  
Acetylneuraminic Acid

scholarly journals Facile Anomer-oriented Syntheses of 4-Methylumbelliferyl Sialic Acid Glycosides

2021 ◽  
Author(s):  
Abdullah Hassan ◽  
Stefan Oscarson
Keyword(s):  
Catalytic Activity ◽  
Sialic Acid ◽  
Substrate Specificity ◽  
Enzymatic Activity ◽  
Addition Reaction ◽  
Neuraminic Acid ◽  
Acetylneuraminic Acid ◽  
Diastereoselective Addition ◽  
High Yields ◽  
Stereoselective Syntheses

<p>As part of a program to find new sialidases and determine their enzymatic specificity and catalytic activity, a library of 4-methylumbelliferyl sialic acid glycosides derivatised at the C-5 position were prepared from <i>N</i>-acetylneuraminic acid. Both α- and β-4-methylumbelliferyl sialic acid glycosides were prepared in high yields and excellent stereoselectivity. Alpha anomers were accessed via reagent control by utilising additive CH<sub>3</sub>CN and TBAI, whereas the beta anomers were synthesised through a diastereoselective addition reaction of iodine and the aglycone to the corresponding glycal followed by reduction of the resulting 3-iodo compounds. Both anomer-oriented synthetic pathways allow for gram-scale stereoselective syntheses of the desired C-5 modified neuraminic acid derivatives for use as tools to quantify the enzymatic activity and substrate specificity of known<b> </b>sialidases, and potential detection and investigation of<b> </b>novel sialidases.</p>

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