Localization of lysophosphatidylcholine in bovine chromaffin granules |
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Authors: | Octávio M. De Oliveira Filgueiras Anton M.H.P. Van Den Besselaar Henk Van Den Bosch |
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Affiliation: | Laboratory of Biochemistry, State University Utrecht, Padualaan 8, 3508 TB Utrecht The Netherlands |
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Abstract: | One of the unique features of the chromaffin granule membrane is the presence of about 17 mol% lysophosphatidylcholine. Lysophosphatidylcholine isolated from the granules could be degraded by approx. 94% by lysophospholipase. This result is consistent with chemical analyses data showing that about 9% of this lysophospholipid is 1′-alkenyl glycerophosphocholine.The localization of the acylglycerophosphocholine in the chromaffin granule membrane was studied by using pure bovine liver lysophospholipases. In intact granules only about 10% of the total lysophosphatidylcholine was directly available for enzymic hydrolysis. In contrast, when granule membranes (ghosts) were treated with lysophospholipases approx. 60% of the lysophosphatidylcholine was deacylated. These values did not increase after pre-treatment of intact granules or ghosts with trypsin. Added did not mix with the endogenous lysophosphatidylcholine pool(s) and remained completely accessible to added lysophospholipases. |
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Keywords: | Chromaffin granule Lysophosphatidylcholine Transmembrane localization Lysophospholipase |
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