Journal Article

Inhibition of Pancreatic Elastase by Sulfated Lipids in the Intestinal Mucosa

Nobuko Ito, Yuriko Iwamori, Kazuo Hanaoka and Masao Iwamori

in The Journal of Biochemistry

Published on behalf of The Japanese Biochemical Society

Volume 123, issue 1, pages 107-114
Published in print January 1998 | ISSN: 0021-924X
Published online January 1998 | e-ISSN: 1756-2651 | DOI: http://dx.doi.org/10.1093/oxfordjournals.jbchem.a021896
Inhibition of Pancreatic Elastase by Sulfated Lipids in the Intestinal Mucosa

Show Summary Details

Preview

Sulfated lipids, cholesterol sulfate (CS) and I3SO3-GalCer, are commonly present in the epithelia of the digestive tracts of pigs, humans, rabbits, and rats. CS was the only sulfated lipid in the esophageal epithelia of these mammals, and I3SO3-GalCer, together with CS, was detected in the epithelia of the gastrointestinal tracts, at a concentration higher than 0.05 μmol per gram of dry weight. Although no sulfated lipids were present in the pancreatic duct, they were found in relatively high concentrations in the duodenal, jejunal, and ileal epithelia. To elucidate the functional significance of sulfated lipids in the digestive tract, we determined the effect of CS and I3SO3-GalCer on the activities of pancreatic and Pseudomonas aeruginosa elastases and found that both characteristically inhibited the pancreatic elastase but not the P. aeruginosa elastase. Desulfation of CS and I3SO3-GalCer abolished their inhibitory activity, and other membrane constituents including free fatty acids, phospholipids, and gangliosides failed to inhibit pancreatic elastase. In addition, steroid sulfates, such as dehydroepiandrosterone sulfate and pregnenolone sulfate, did not exhibit any inhibitory activity toward pancreatic elastase, indicating that the sulfate group and a suitable hydrophobic side chain are required in the inhibition of elastase. Inhibition of elastase by sulfated lipids occurred in a dose-dependent manner, and the molar ratios of CS and I3SO3-GalCer to elastase at which the enzyme activity was inhibited to 50% of the maximum level were 6:1 and 9:1, respectively. CS-treated elastase had the same Km and a lower Vmax compared with the untreated enzyme, and sulfated lipids were observed to bind tightly to the enzyme, suggesting irreversible inhibition. Thus, CS and I3SO3-GalCer in the digestive tracts of mammals were shown to function as epithelial inhibitors of pancreatic elastase.

Keywords: cholesterol sulfate; gangliosides; pancreatic elastase; Pseudomonas aeruginosa elastase; sulfatide

Journal Article.  0 words. 

Subjects: Biochemistry

Full text: subscription required

How to subscribe Recommend to my Librarian

Users without a subscription are not able to see the full content. Please, subscribe or login to access all content.