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J. Biol. Chem., Vol. 282, Issue 10, 7591-7605, March 9, 2007
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Phospholipid Biosynthesis Program Underlying Membrane Expansion during B-lymphocyte Differentiation*
12
From the
Department of Infectious Diseases, St. Jude Children's Research Hospital, Memphis, Tennessee 38105-2794 and the Department of Microbiology and Immunology, Loyola University Medical Center, Maywood, Illinois 60153
Stimulated B-lymphocytes differentiate into plasma cells committed to antibody production. Expansion of the endoplasmic reticulum and Golgi compartments is a prerequisite for high rate synthesis, assembly, and secretion of immunoglobulins. The bacterial cell wall component lipopolysaccharide (LPS) stimulates murine B-cells to proliferate and differentiate into antibody-secreting cells that morphologically resemble plasma cells. LPS activation of CH12 B-cells augmented phospholipid production and initiated a genetic program, including elevated expression of the genes for the synthesis, elongation, and desaturation of fatty acids that supply the phospholipid acyl moieties. Likewise, many of the genes in phospholipid biosynthesis were up-regulated, most notably those encoding Lipin1 and choline phosphotransferase. In contrast, CTP:phosphocholine cytidylyltransferase 
(CCT) protein, a key control point in phosphatidylcholine biosynthesis, increased because of stabilization of protein turnover rather than transcriptional activation. Furthermore, an elevation in cellular diacylglycerol and fatty acid correlated with enhanced allosteric activation of CCT by the membrane lipids. This work defines a genetic and biochemical program for membrane phospholipid biogenesis that correlates with an increase in the phospholipid components of the endoplasmic reticulum and Golgi compartments in LPS-stimulated B-cells.
Received for publication, August 25, 2006 , and in revised form, January 9, 2007.
* This work was supported by National Institutes of Health Grants GM 45737 (to S. J.) and GM 61970 (to J. B.), Cancer Center (CORE) Support Grant CA 21765, and the American Lebanese Syrian Associated Charities. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement"in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
1 Present address: Dept. of Microbiology, Chiang Mai University, Chiang Mai, 50200, Thailand.
2 To whom correspondence should be addressed. Tel.: 901-495-3494; Fax: 901-495-3099; E-mail: suzanne.jackowski{at}stjude.org.
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