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Role of cyclic adenosine monophosphate in phospholipid synthesis in Mycobacterium smegmatis ATCC 607
Author(s) -
Kaur Harpinder,
Khuller G. K.
Publication year - 1995
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02536043
Subject(s) - phospholipid , forskolin , biochemistry , adenylate kinase , intracellular , protein kinase c , protein kinase a , chemistry , cyclase , enzyme , biology , membrane , receptor
The present study was undertaken to examine the influence of intracellular levels of cyclic AMP on phospholipid synthesis in Mycobacterium smegmatis ATCC 607. The cyclic AMP levels were modulated by growing cells in the presence of activator (forskolin) and inhibitor (atropine) of adenylate cyclase, the synthesizing enzyme of cyclic AMP. Forskolin‐grown cells exhibited a 1.4‐fold increase in the level of cAMP while a similar decrease (1.8‐fold) was seen with atropine‐grown cells. These altered levels of cAMP in turn affected the total content, composition and synthesis of phospholipids. Total phospholipid content increased and decreased in cells grown in the presence of forskolin and atropine, respectively. These observations were further supported by alterations in [ 14 C]acetate incorporation as well as in activities of glycerol kinase and glycerol‐3‐phosphate acyltransferase, the key enzymes of phospholipid synthesis. Protein phosphorylation mechanism seems to be involved in phospholipid metabolism as the activities of protein kinase increased and decreased in cells grown in forskolin or atropine cells. Our results demonstrate a correlation between phospholipid synthesis and intracellular levels of cAMP in M. smegmatis .