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The preservation of mycoplasma capricolum cell intactness after phospholipase a 2 treatment

, : The preservation of mycoplasma capricolum cell intactness after phospholipase a 2 treatment. Biochimica et Biophysica Acta 778(2): 372-378

By treating M. capricolum cells with phospholipase A2 about 80% of membrane phospholipids were rapidly hydrolyzed. The rate and extent of hydrolysis (at C) were the same in intact cells and in isolated unsealed membranes. Due to the low endogenous lysophospholipase activity detected in M. capricolum, phospholipase A2 treatment resulted in the accumulation of lysophospholipids and free fatty acids. The free fatty acids were efficiently extracted from the cells by 1% bovine serum albumin whereas the lysophospholipids were almost fully retained within the cell membrane. Following phospholipase A2 treatment in the presence of 1% bovine serum albumin, cell intactness was preserved as indicated by the constant absorbance of the cell suspension and the retention of nucleic acids and NADH dehydrogenase activity within the cells. The treated cells showed a slight decrease in K+ content and a decrease in cell viability. Viability was fully preserved after phospholipase A2 treatment of cells grown with exogenous sphingomyelin. Adapting M. capricolum to a cholesterol-poor medium resulted in a marked decrease in the cholesterol to phospholipid molar ratio (from about 1.1 to 0.3). Phospholipase A2 treatment of the cholesterol-poor cells resulted in cell lysis. Cell lysis was induced in the cholesterol-rich cells by hydrolyzing the lysophospholipids accumulated following phospholipase A2 treatment. Apparently, after phospholipase A2 treatment of M. capricolum cells, a relatively stable cell membrane is maintained and cell intactness is preserved due to the interaction of cholesterol, present in high amount in this membrane, with the lysophospholipids formed.

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