Results 141 to 150 of about 2,521,035 (177)

Acid ceramidase expression reduces IFNγ secretion by mouse CD4<sup>+</sup> T cells and is crucial for maintaining B-cell numbers in mice. [PDF]

open access: yesFront Immunol
Mandasari P   +8 more
europepmc   +1 more source

Sphingolipids and acid ceramidase as therapeutic targets in cancer therapy [PDF]

open access: yesCritical Reviews in Oncology/Hematology, 2019
Background: Sphingolipids have been shown to play a key part in cancer cell growth and death and have increasingly become the subject of novel anti-cancer therapies.
Dale Vimalachandran   +2 more
exaly   +4 more sources

New insights on the use of desipramine as an inhibitor for acid ceramidase [PDF]

open access: yesFEBS Letters, 2006
Treatment of different cancer cell lines with desipramine induced a time- and dose-dependent downregulation of acid ceramidase. Desipramine’s effect on acid ceramidase appeared specific for amphiphilic agents (desipramine, chlorpromazine, and chloroquine)
James Norris   +2 more
exaly   +5 more sources

Acid ceramidase and human disease

open access: yesBiochimica Et Biophysica Acta - 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).
Edward H Schuchman, Jae Ho Park
exaly   +3 more sources
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The molecular medicine of acid ceramidase

Biological Chemistry, 2015
Abstract 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 two rare inherited disorders, Farber lipogranulomatosis (Farber disease ...
Michael, Frohbergh   +2 more
openaire   +2 more sources

Properties of acid ceramidase from human spleen

Lipids and Lipid Metabolism, 1989
We have characterised ceramidase activity in extracts of human spleen from control subjects and from patients with Gaucher disease. In Triton X-100 extracts of control spleens, a broad pH optimum of pH 3.5-5.0 was found; no ceramidase activity was detectable at neutral or alkaline pH.
Joseph M Tager, A W Schram, Hugo W Moser
exaly   +3 more sources

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