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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 194 (1999), S. 265-270 
    ISSN: 1573-4919
    Keywords: calmodulin ; phosphorylation ; phospholipid ; Microsporum gypseum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The mechanism of action of Ca2+/calmodulin on phospholipid synthesis in Microsporum gypseum has been studied. These second messengers were observed to mediate their function through phosphorylation mechanism as altered protein kinase activity was seen in calcium/trifluoperazine (calmodulin antagonist) grown cells. The activity of protein kinase was dependent on calcium (200 μm) and calmodulin (1 μm). In vitro studies of phosphorylation and dephosphorylation in relation to phospholipid synthesis in Microsporum gypseum have been carried out. Addition of KN-62 (a specific inhibitor of Ca2+/calmodulin-dependent protein kinases) and polyclonal antibodies raised against purified Ca2+/calmodulin-kinase (CaMPK) of M. gypseum in the cell extract, leads to the inhibition in the incorporation of labelled acetate into total phospholipids in this fungus. These results suggest a possible involvement of Ca2+/calmodulin via Ca2+/calmodulin-dependent phosphorylation in phospholipid synthesis in M. gypseum.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 177 (1997), S. 27-31 
    ISSN: 1573-4919
    Keywords: protein kinase(s) ; phospholipid ; calcium/cAMP ; M. gypseum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Protein kinase(s) have been identified for the first time in Microsporum gypseum. It phosphorylated exogenous protein acceptors preferentially histone IIs and casein and are mainly localized in the cytosolic fraction of M. gypseum. Alterations in protein kinase activity was observed in calcium/aminophylline and atropine (cAMP modulators) grown cells which is due to the modulation in the Ca2+/cAMP levels. Alteration in the protein kinase(s) activity finally affected the total phospholipid content in these modulated cells of M. gypseum. These observations suggest a correlation between the activity of protein kinase(s) and phospholipid synthesis in M. gypseum. This protein kinase(s) has a broad substrate specificity and is a seryl-threonyl type protein kinase(s) as it phosphorylates exogenous (histone) and endogenous proteins at serine and threonine residues.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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