HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Bosner, M. S. Articles by Lange, L. G. Search for Related Content PubMed PubMed Citation Articles by Bosner, M. S. Articles by Lange, L. G. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 264, Issue 34, 20261-20264, Dec, 1989

Heparin-modulated binding of pancreatic lipase and uptake of hydrolyzed triglycerides in the intestine [published erratum appears in J Biol Chem 1990 Feb 25;265(6):3585]

MS Bosner, T Gulick, DJ Riley, CA Spilburg and LG Lange
Department of Medicine, Jewish Hospital of Saint Louis, Washington University Medical Center, Missouri 63110.

Utilizing small intestine membranes that contain heparin (50 micrograms/mg protein), binding of triglyceride lipase (homogeneous 52 kDa, specific activity, 70 nmol/mg.h) to membranes was shown to be concentration dependent and saturable, and it was characterized by a single dissociation constant (KD = 86 +/- 16 nM) with a maximal binding capacity of 54 +/- 8 pmol/mg of vesicle protein. Specific binding was decreased in a concentration-dependent manner by the addition of exogenous heparin, and binding was virtually eliminated (less than 6% control values) by pretreatment of membranes with bacterial heparinase. Cultured intestinal epithelial cells (CaCo-2), shown to possess membrane-associated heparin, also bound pancreatic triglyceride lipase in a specific and saturable manner, with KD = 77 +/- 12 nM and Bmax = 13.7 +/- 6 pmol/10(6) cells. Soluble heparin not only decreased binding, but it also diminished the enzyme-mediated cellular uptake of [14C]oleate from [14C]triolein by over 75%. Therefore, intestinal heparin, a component of the brush border membrane, localizes pancreatic triglyceride lipase in a receptor-like manner to the plasma membrane to promote the subsequent absorption of fatty acids derived from hydrolyzed triglycerides.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				J. Prades, S. S. Funari, P. V. Escriba, and F. Barcelo Effects of unsaturated fatty acids and triacylglycerols on phosphatidylethanolamine membrane structure J. Lipid Res., September 1, 2003; 44(9): 1720 - 1727. [Abstract] [Full Text] [PDF]

				N Bruneau, D Lombardo, and M Bendayan Participation of GRP94-related protein in secretion of pancreatic bile salt-dependent lipase and in its internalization by the intestinal epithelium J. Cell Sci., January 9, 1998; 111(17): 2665 - 2679. [Abstract] [PDF]

				T. Tsujita, T. Miyazaki, R. Tabei, and H. Okuda Coenzyme A-independent Monoacylglycerol Acyltransferase from Rat Intestinal Mucosa J. Biol. Chem., January 26, 1996; 271(4): 2156 - 2161. [Abstract] [Full Text] [PDF]

				M. Withiam-Leitch, R. P. Rubin, S. E. Koshlukova, and J. M. Aletta Identification and Characterization of Carboxyl Ester Hydrolase as a Phospholipid Hydrolyzing Enzyme of Zymogen Granule Membranes from Rat Exocrine Pancreas J. Biol. Chem., February 24, 1995; 270(8): 3780 - 3787. [Abstract] [Full Text] [PDF]