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Phospholipid Metabolism of Rat Gastric Mucosa

  • Chapter
Membrane Fluidity

Part of the book series: Experimental Biology and Medicine ((EBAM,volume 1))

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Abstract

Phospholipids of rat gastric mucosa comprised about 30% of the total extractable lipidsl phosphatidylcholine (PC) constitutes about half of the phospholipids. Disaturated (dipalmitoyl)-PC made up about 31% of the PC species, a concentration comparable to that reported for lung tissue. Gastric mucosa exhibited three distinguishable phospholipid deacylating enzyme activites; lysophospholipase, phospholipase A1 and phospholipase A2 and an acylase activity owing to a lysophospholipase-transacylase enzyme complex. The lysophospholipase hydrolyzed 1-palmitoyl lyso-PC to free fatty acid and glycerophosphorylcholine (GPC). This enzyme had an optimum pH of 8.0, was heat labile, did not require Ca2+ for maximum activity and was not inhibited by bile salts or buffers of high ionic strength. Phospholipase A2 and phospholipase A1 deacylated dipalmitoy1-PC to the corresponding lyso compound and free fatty acid. The specific activity of phospholipase A2 was 2-4-fold higher than that of phospholipase A1 under all the conditions tested. Both activities were enhanced 4-7.5-fold in the presence of bile salts at alkaline pH and 11-18-fold at acidic pH. Phospholipase A2 hydrolyzed diarachidonyl-PC>PC-18:2>>PC-18:1>PC-16:0. No phospholipase C or D activities were detected with dipalmitoyl1-PC as substrate. The lysophospholipase-transacylase enzyme comples displayed both a lysophospholipase and a transacylase activity. The transacylase converted, stoichiometrically, 2 moles of 1-palmitoyl1 lyso-PC to one mole each of dipalmitoyl-PC and GPC in the absence of ATP, CoA, fatty acids, bile salts or detergents. The transacylase-lyso-phospholipase activities were both located in the cytosol fraction and were associated at a constant ratio through-out several purification steps, including the isoelectrofocusing procedure.

The high levels of dipalmitoyl-PC and the presence of deacylating enzymes and of a lysophospholipase-transacylase enzyme complex in gastric mucosa and the lung suggest similarities between gastric and lung phospholipid metabolism. Dipalmitoyl-PC is generally accepted as the major active component of pulmonary surfactant, but the exact role of dipalmitoyl-PC in gastric mucosa awaits furthere documentation.

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Authors and Affiliations

  1. Department of Biochemistry, New York Medical College, Valhalla, NY, 10595, USA

    Momtaz K. Wassef, Y. N. Lin & M. I. Horowitz

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  1. Momtaz K. Wassef
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  2. Y. N. Lin
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  3. M. I. Horowitz
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Editors and Affiliations

  1. University of Ottawa, Canada

    Morris Kates

  2. University of Toronto, Canada

    Arnis Kuksis

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Wassef, M.K., Lin, Y.N., Horowitz, M.I. (1980). Phospholipid Metabolism of Rat Gastric Mucosa. In: Kates, M., Kuksis, A. (eds) Membrane Fluidity. Experimental Biology and Medicine, vol 1. Humana Press. https://doi.org/10.1007/978-1-4612-6120-9_22

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  • DOI: https://doi.org/10.1007/978-1-4612-6120-9_22

  • Publisher Name: Humana Press

  • Print ISBN: 978-1-4612-6122-3

  • Online ISBN: 978-1-4612-6120-9

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