Document Detail


Exposure to common food additive carrageenan leads to reduced sulfatase activity and increase in sulfated glycosaminoglycans in human epithelial cells.
MedLine Citation:
PMID:  22410212     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The commonly used food additive carrageenan, including lambda (λ), kappa (κ) and iota (ι) forms, is composed of galactose disaccharides linked in alpha-1,3 and beta-1,4 glycosidic bonds with up to three sulfate groups per disaccharide residue. Carrageenan closely resembles the endogenous galactose or N-acetylgalactosamine-containing glycosaminoglycans (GAGs), chondroitin sulfate (CS), dermatan sulfate (DS), and keratan sulfate. However, these GAGs have beta-1,3 and beta-1,4 glycosidic bonds, in contrast to the unusual alpha-1,3 glycosidic bond in carrageenan. Since sulfatase activity is inhibited by sulfate, and carrageenan is so highly sulfated, we tested the effect of carrageenan exposure on sulfatase activity in human intestinal and mammary epithelial cell lines and found that carrageenan exposure significantly reduced the activity of sulfatases, including N-acetylgalactosamine-4-sulfatase, galactose-6-sulfatase, iduronate sulfatase, steroid sulfatase, arylsulfatase A, SULF-1,2, and heparan sulfamidase. Consistent with the inhibition of sulfatase activity, following exposure to carrageenan, GAG content increased significantly and showed marked differences in disaccharide composition. Specific changes in CS disaccharides included increases in di-sulfated disaccharide components of CSD (2S6S) and CS-E (4S6S), with declines in CS-A (4S) and CS-C (6S). Specific changes in heparin-heparan sulfate disaccharides included increases in 6S disaccharides, as well as increases in NS and 2S6S disaccharides. Study results suggest that carrageenan inhibition of sulfatase activity leads to re-distribution of the cellular GAG composition with increase in di-sulfated CS and with potential consequences for cell structure and function.
Authors:
Bo Yang; Sumit Bhattacharyya; Robert Linhardt; Joanne Tobacman
Publication Detail:
Type:  Journal Article     Date:  2012-03-05
Journal Detail:
Title:  Biochimie     Volume:  94     ISSN:  1638-6183     ISO Abbreviation:  Biochimie     Publication Date:  2012 Jun 
Date Detail:
Created Date:  2012-05-04     Completed Date:  2012-08-30     Revised Date:  2013-06-26    
Medline Journal Info:
Nlm Unique ID:  1264604     Medline TA:  Biochimie     Country:  France    
Other Details:
Languages:  eng     Pagination:  1309-16     Citation Subset:  IM    
Copyright Information:
Published by Elsevier Masson SAS.
Affiliation:
Department of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, Troy, NY, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Breast / cytology
Carrageenan / adverse effects*
Cell Line
Cerebroside-Sulfatase / antagonists & inhibitors
Chondroitinsulfatases / antagonists & inhibitors
Epithelial Cells / drug effects,  enzymology
Female
Food Additives / adverse effects*
Humans
Hydrolases / antagonists & inhibitors
Iduronate Sulfatase / antagonists & inhibitors
Intestinal Mucosa / cytology
N-Acetylgalactosamine-4-Sulfatase / antagonists & inhibitors
Steryl-Sulfatase / antagonists & inhibitors
Sulfatases / antagonists & inhibitors*
Sulfotransferases / antagonists & inhibitors
Grant Support
ID/Acronym/Agency:
R01 GM038060/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Food Additives; 9000-07-1/Carrageenan; EC 2.8.2.-/SULF1 protein, human; EC 2.8.2.-/SULF2 protein, human; EC 2.8.2.-/Sulfotransferases; EC 3.-/Hydrolases; EC 3.1.6.-/Chondroitinsulfatases; EC 3.1.6.-/Sulfatases; EC 3.1.6.-/heparan sulfate sulfatase; EC 3.1.6.12/N-Acetylgalactosamine-4-Sulfatase; EC 3.1.6.13/Iduronate Sulfatase; EC 3.1.6.2/Steryl-Sulfatase; EC 3.1.6.4/GALNS protein, human; EC 3.1.6.8/Cerebroside-Sulfatase; EC 3.10.1.1/N-sulfoglucosamine sulfohydrolase
Comments/Corrections

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