Purification of a lysophosphatidic acid-hydrolysing lysophospholipase from rat brain

Thomson, F. J. and Clark, M. A. (1994) Purification of a lysophosphatidic acid-hydrolysing lysophospholipase from rat brain. Biochemical Journal, 300(2), pp. 457-461. (doi: 10.1042/bj3000457) (PMID:8002951)

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A lysophosphatidic acid (LPA)-hydrolysing lysophospholipase was purified from rat brain and characterized. This membrane-bound lysophospholipase was solubilized by using n-octyl glucoside and purified by sequential cation, hydrophobic and gel-filtration chromatography. The purified protein has a mass of 80 kDa as assayed by SDS/PAGE. This lysophospholipase catalysed the hydrolysis of a variety of lysophosphatidic acids, but with different rates, depending on the length and degree of saturation of the sn-1 acyl group (1-oleoyl-LPA approximately 1-stearoyl-LPA > 1-palmitoyl-LPA > 1-myristoyl-LPA). This enzyme had no-measurable catalytic activity when other lysophospholipids, monoacylglycerol or phosphatidic acid were used as substrates. On the basis of its chromatographic properties, substrate specificity and cellular localization, we conclude that this lysophospholipase differs from those previously purified and speculate that it has an important function in terminating biological responses to LPA.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Thomson, Dr Fiona
Authors: Thomson, F. J., and Clark, M. A.
College/School:College of Medical Veterinary and Life Sciences > School of Cancer Sciences
Journal Name:Biochemical Journal
Publisher:Portland Press
ISSN (Online):1470-8728

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