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Nuclear lipidome is altered in amyotrophic lateral sclerosis: A pilot study.
J Neurochem
July 2021
Department of Experimental Medicine, School of Medicine, IRBLleida-UdL, Lleida, Spain.
Nucleocytosolic transport, a membrane process, is impaired in motor neurons in amyotrophic lateral sclerosis (ALS). This study analyzes the nuclear lipidome in motor neurons in ALS and examines molecular pathways linked to the major lipid alterations. Nuclei were obtained from the frozen anterior horn of the lumbar spinal cord of ALS patients and age-matched controls.
View Article and Find Full Text PDFPlasmalogen mediates integration of adherens junction.
J Biochem
November 2019
Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka, Japan.
Ether glycerolipids, plasmalogens are found in various mammalian cells and tissues. However, physiological role of plasmalogens in epithelial cells remains unknown. We herein show that synthesis of ethanolamine-containing plasmalogens, plasmenylethanolamine (PlsEtn), is deficient in MCF7 cells, an epithelial cell line, with severely reduced expression of alkyl-dihydroxyacetonephosphate synthase (ADAPS), the second enzyme in the PlsEtn biosynthesis.
View Article and Find Full Text PDFThe glycosomal alkyl-dihydroxyacetonephosphate synthase TbADS is essential for the synthesis of ether glycerophospholipids in procyclic trypanosomes.
Exp Parasitol
February 2018
Department of Biological Sciences, St John's University, 8000 Utopia Parkway, Jamaica, NY 11439, USA. Electronic address:
Glycerophospholipids are the main constituents of the biological membranes in Trypanosoma brucei, which causes sleeping sickness in humans. The present work reports the characterization of the alkyl-dihydroxyacetonephosphate synthase TbADS that catalyzes the committed step in ether glycerophospholipid biosynthesis. TbADS localizes to the glycosomal lumen.
View Article and Find Full Text PDFIsolation and characterization of mutant animal cell line defective in alkyl-dihydroxyacetonephosphate synthase: localization and transport of plasmalogens to post-Golgi compartments.
Biochim Biophys Acta
October 2008
Graduate School of Systems Life Sciences, Kyushu University, Fukuoka 812-8581, Japan.
We herein isolated plasmalogen-deficient Chinese hamster ovary (CHO) mutant, ZPEG251, with a phenotype of normal import of peroxisomal matrix and membrane proteins. In ZPEG251, plasmenylethanolamine (PlsEtn) was severely reduced. Complementation analysis by expression of genes responsible for the plasmalogen biogenesis suggested that alkyl-dihydroxyacetonephosphate synthase (ADAPS), catalyzing the second step of plasmalogen biogenesis, was deficient in ZPEG251.
View Article and Find Full Text PDFIdentifying a recombinant alkyldihydroxyacetonephosphate synthase suited for crystallographic studies.
Protein Expr Purif
October 2007
Dipartimento di Genetica e Microbiologia, Università di Pavia, via Ferrata 1, 27100 Pavia, Italy.
Alkyldihydroxyacetonephosphate is the building block for the biosynthesis of ether phospholipids, which are essential components of eukaryotic cell membranes and are involved in a variety of signaling processes. The metabolite is synthesized by alkyldihydroxyacetonephosphate synthase (ADPS), a peroxisomal flavoenzyme. Deficiency in ADPS activity causes rhizomelic chondrodysplasia punctata type 3, a very severe genetic disease.
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