These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Phospholipase D activity is altered in X-linked adrenoleukodystrophy heterozygous carriers, but not in hemizygous patients.
    Author: Logan HE, Byers DM, Ridgway ND, Cook HW.
    Journal: Biochim Biophys Acta; 1998 Jul 01; 1407(1):7-20. PubMed ID: 9639664.
    Abstract:
    Abnormalities in levels of choline and its metabolites have been reported in the lesions of brains of X-linked adrenoleukodystrophy (X-ALD) patients. We have examined the turnover of the major choline-containing phospholipid, phosphatidylcholine (PtdCho), in fibroblasts from hemizygous X-ALD, heterozygous X-ALD, Zellweger syndrome (ZW), and male and female control individuals to assess possible alterations in PtdCho metabolism mediated by activation of protein kinase C (PKC). Hydrolysis of PtdCho by phospholipase D (PLD) and resynthesis of PtdCho from labeled choline were stimulated 2- to 4-fold by PKC activation with the phorbol ester, 4beta-12-O-tetradecanoylphorbol-13-acetate (beta-TPA), in all cells except those from heterozygous X-ALD individuals. No differences in quantity or intracellular distribution of PKC activity, PKC isoforms by Western blot analysis, or of the PKC substrate, myristoylated alanine-rich C kinase substrate (MARCKS), were apparent in any of the cells. Thus, altered PtdCho metabolism was not directly linked to either of these inherited defects that result in abnormal peroxisomal functions. Further, altered responsiveness of PLD in X-ALD heterozygotes was independent of changes in PKC and MARCKS.
    [Abstract] [Full Text] [Related] [New Search]