Results 31 to 40 of about 2,263 (197)
Substrate specificity of rat brain ceramidase [PDF]
Journal of Lipid Research, 2002 In this study, the substrate specificity of a newly identified rat brain ceramidase (CDase) was investigated. To this end, the major functional groups and stereochemistry of ceramide (Cer) were evaluated for their influence on the hydrolysis of substrate by this CDase. The results showed that, of the four possible stereoisomers of Cer, only the natural
Samer El Bawab +5 more
openaire +3 more sources
Role of the cell-wall structure in the retention of bacteria by microfiltration membranes [PDF]
, 2009 This experimental study investigates the retention of bacteria by porous membranes. The transfer of bacteria larger than the nominal pore size of microfiltration track-etched membranes has been studied for several kinds of bacterial strains.
Aimar, Pierre +3 more
core +2 more sources
Acid ceramidase promotes senescent cell survival
Aging, 2021 Cellular senescence is linked to chronic age-related diseases including atherosclerosis, diabetes, and neurodegeneration. Compared to proliferating cells, senescent cells express distinct subsets of proteins. In this study, we used cultured human diploid fibroblasts rendered senescent through replicative exhaustion or ionizing radiation to identify ...
Munk, Rachel +12 more
openaire +2 more sources
Presence of Ceramidase Activity in Electronegative LDL [PDF]
International Journal of Molecular Sciences, 2022 Electronegative low-density lipoprotein (LDL(−)) is a minor modified fraction of human plasma LDL with several atherogenic properties. Among them is increased bioactive lipid mediator content, such as lysophosphatidylcholine (LPC), non-esterified fatty acids (NEFA), ceramide (Cer), and sphingosine (Sph), which are related to the presence of some ...
Núria Puig +9 more
openaire +6 more sources
Journal of Lipid Research, 2007 Ceramidases (CDases) hydrolyze ceramide to sphingosine (SPH) and fatty acid. Pseudomonas CDase (pCDase) is a homolog of mammalian neutral ceramidases and may play roles in disease pathogenesis.
Bill X Wu +4 more
doaj +1 more source
Acid ceramidase and human disease
Biochimica et Biophysica Acta (BBA) - Biomembranes, 2006 Acid ceramidase (N-acylsphingosine deacylase, EC 3.5.1.23; AC) is the lipid hydrolase responsible for the degradation of ceramide into sphingosine and free fatty acids within lysosomes. The enzymatic activity was first identified over four decades ago, and is deficient in the inherited lipid storage disorder, Farber Lipogranulomatosis (Farber disease).
Park, Jae-Ho, Schuchman, Edward H.
openaire +2 more sources
Gene cloning of a neutral ceramidase from the sphingolipid metabolic pathway based on transcriptome analysis of Amorphophallus muelleri. [PDF]
PLoS ONE, 2018 Amorphophallus is a perennial herbaceous plant species mainly distributed in the tropics or subtropics of Asia and Africa. It has been used as a traditional medicine for a long time and now is utilized for the pharmaceutical, chemical and agriculture ...
Lin Zhong +7 more
doaj +1 more source
Frontiers in Plant Science, 2023 Brown rot, caused by the Monilinia spp., is the disease that causes the greatest losses in stone fruit worldwide. Currently, M. fructicola has become the dominant species in the main peach production area in Spain.
Pedro J. Martínez-García +4 more
doaj +1 more source
Scientific Opinion on the substantiation of a health claim related to Wheat Polar Lipid Extract and protection of the skin against dehydration pursuant to Article 13(5) of Regulation (EC) No 1924/2006 [PDF]
, 2012 <p>Following an application from Extraction Purification Innovation France, submitted pursuant to Article 13(5) of Regulation (EC) No 1924/2006 via the Competent Authority of France, the Panel on Dietetic Products, Nutrition and Allergies (NDA) was
EFSA Panel on Dietetic Products, Nutrition and Allergies
core +1 more source
Structure of a human intramembrane ceramidase explains enzymatic dysfunction found in leukodystrophy
Nature Communications, 2018 Alkaline ceramidases (ACERs) are a class of poorly understood transmembrane enzymes controlling the homeostasis of ceramides. Here authors solve the Xray structure of human ACER3 and uncover a Ca2+ binding site providing an explanation for the known ...
Ieva Vasiliauskaité-Brooks +13 more
doaj +1 more source