chemistry people/ interesting website

[Guest guest]

hi all I am not one to understand all this info, have no idea if its relevant!!

Was just searching around and found this info, wondered if it was of any use or

if it was a load of old rubbish and totally unhelpful

with baby Liam 4 monthc CF

Selected Abstracts

Returned: 3 citations and abstracts. Click on down arrow or scroll to see

abstracts.

M Davril , S Degroote , P Humbert , C Galabert , V Dumur , JJ Lafitte , G

Lamblin , and P Roussel

The sialylation of bronchial mucins secreted by patients suffering from cystic

fibrosis or from chronic bronchitis is related to the severity of airway

infection

Glycobiology 9: 311-321.

R. O’Riordan , Amy L. Lachapelle , Marshall , A.

Higgins , and Seng H. Cheng

Characterization of the oligosaccharide structures associated with the cystic

fibrosis transmembrane conductance regulator

Glycobiology 10: 1225-1233.

A Scharfman , S Degroote , J Beau , G Lamblin , P Roussel , and J Mazurier

Pseudomonas aeruginosa binds to neoglycoconjugates bearing mucin carbohydrate

determinants and predominantly to sialyl- x conjugates

Glycobiology 9: 757-764.

--------------------------------------------------------------------------------

Abstract 1 of 3

Glycobiology, Vol 9, 311-321, Copyright © 1999 by Oxford University Press

--------------------------------------------------------------------------

ORIGINAL ARTICLES

The sialylation of bronchial mucins secreted by patients suffering from cystic

fibrosis or from chronic bronchitis is related to the severity of airway

infection

M Davril, S Degroote, P Humbert, C Galabert, V Dumur, JJ Lafitte, G Lamblin and

P Roussel

Unite INSERM no. 377, Place de Verdun, 59045 Lille Cedex, France.

Bronchial mucins were purified from the sputum of 14 patients suffering from

cystic fibrosis and 24 patients suffering from chronic bronchitis, using two

CsBr density-gradient centrifugations. The presence of DNA in each secretion was

used as an index to estimate the severity of infection and allowed to subdivide

the mucins into four groups corresponding to infected or noninfected patients

with cystic fibrosis, and to infected or noninfected patients with chronic

bronchitis. All infected patients suffering from cystic fibrosis were colonized

by Pseudomonas aeruginosa. As already observed, the mucins from the patients

with cystic fibrosis had a higher sulfate content than the mucins from the

patients with chronic bronchitis. However, there was a striking increase in the

sialic acid content of the mucins secreted by severely infected patients as

compared to noninfected patients. Thirty- six bronchial mucins out of 38

contained the sialyl- x epitope which was even expressed by subjects

phenotyped as negative, indicating that at least one alpha1,3

fucosyltransferase different from the enzyme was involved in the

biosynthesis of this epitope. Finally, the sialyl- x determinant was also

overexpressed in the mucins from severely infected patients. Altogether these

differences in the glycosylation process of mucins from infected and noninfected

patients suggest that bacterial infection influences the expression of

sialyltransferases and alpha1,3 fucosyltransferases in the human bronchial

mucosa.

[Full Text of Davril et al.]

--------------------------------------------------------------------------------

Abstract 2 of 3 Glycobiology, 2000, Vol. 10, No. 11 1225-1233

© 2000 Oxford University Press

Characterization of the oligosaccharide structures associated with the cystic

fibrosis transmembrane conductance regulator

R. O’Riordan1, Amy L. Lachapelle, Marshall, A. Higgins

and Seng H. Cheng

Genzyme Corporation, 31 New York Avenue, Framingham, MA 01701–9322, USA

The cystic fibrosis transmembrane conductance regulator (CFTR) is a plasma

membrane-associated glycoprotein. The protein can exist in three different

molecular weight forms of approximately 127, 131, and 160 kDa, representing

either nonglycosylated, core glycosylated, or fully mature, complex glycosylated

CFTR, respectively. The most common mutation in cystic fibrosis (CF) results in

the synthesis of a variant (F508-CFTR) that is incompletely glycosylated and

defective in its trafficking to the cell surface. In this study, we have

analyzed the oligosaccharide structures associated with the different forms of

recombinant CFTR, by expressing and purifying the channel protein from either

mammalian Chinese hamster ovary (CHO) or insect Sf9 cells. Using glycosidases

and FACE analysis (fluorophore-assisted carbohydrate electrophoresis) we

determined that purified CHO-CFTR contained polylactosaminoglycan (PL)

sequences, while Sf9-CFTR had only oligomannosidic saccharides with fucosylation

on the innermost GlcNAc. The presence of PL sequences on the recombinant

CHO-CFTR is consistent with a normal feature of mammalian processing, since

endogenous CFTR isolated from T84 cells displayed a similar pattern of

glycosylation. The present study also reports on the use of FACE for the

qualitative analysis of small amounts of glycoprotein oligosaccharides released

enzymatically.

1 To whom correspondence should be addressed

[Full Text of O’Riordan et al.] [Reprint (PDF) Version of O’Riordan et al.]

--------------------------------------------------------------------------------

Abstract 3 of 3

Glycobiology, Vol 9, 757-764, Copyright © 1999 by Oxford University Press

--------------------------------------------------------------------------

ORIGINAL ARTICLES

Pseudomonas aeruginosa binds to neoglycoconjugates bearing mucin carbohydrate

determinants and predominantly to sialyl- x conjugates

A Scharfman, S Degroote, J Beau, G Lamblin, P Roussel and J Mazurier

Unite INSERM no. 377 and Universite de Lille 2, Place de Verdun, 59045 Lille

Cedex, France and UMR CNRS no. 111, USTL, 59655 Villeneuve d'Ascq Cedex, France.

Pseudomonas aeruginosa plays an important role in the colonization of the

airways of patients suffering from cystic fibrosis. It binds to the carbohydrate

part of respiratory and salivary mucins and its binding to cystic fibrosis

mucins is even higher, suggesting that qualitative or/and quantitative

modifications of the carbohydrate chains may be involved in this process. In

order to find out the best carbohydrate receptors for P.aeruginosa, a flow

cytometry technique using a panel of polyacrylamide based glycoconjugates

labeled with fluorescein was developed. The neoglycoconjugates contained

neutral, sialylated or sulfated chains analogous to carbohydrate determinants

found at the periphery of respiratory mucins (Le(a), Le(y), Le(x), sialyl- and

3'- sulfo-Le(x), and blood group A determinants). We used also

neoglycoconjugates containing Gal(alpha1-2)Galbeta and sialyl- N -

acetyllactosamine determinants. The interaction of these glycoconjugates with

the nonpiliated strain of P.aeruginosa, 1244-NP, was saturable except for the

glycoconjugates containing blood group A or sialyl- N -acetyllactosamine

epitopes. The measure of Kd indicated that strain 1244-NP had a higher affinity

for the glycoconjugate bearing the sialyl-Le(x)determinant than for all the

other glycoconjugates studied. The role of sialic acid was confirmed by

competition assay using mainly sialylated mucin glycopeptides. In order to find

out if this behavior was the same for pathological strains as for the 1244-NP

mutant, four mucoid strains of P.aeruginosa isolated from cystic fibrosis

patients were analyzed with the Le(x)neoglycoconjugate, its sialylated and its

sulfated derivatives. Individual variations in the binding of these strains to

the three glycoconjugates were observed. However, three strains out of four had

a higher affinity for the sialyl-Le(x)than for the 3'-sulfo- Le(x)derivative.

[Full Text of Scharfman et al.] [Reprint (PDF) Version of Scharfman et al.]

--------------------------------------------------------------------------------

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH SEARCH RESULT

Copyright © 2002 Oxford University Press.