| Autor: |
Parveen F; Department of Medical Laboratory Science and Biotechnology, College of Health Sciences, Kaohsiung Medical University, Kaohsiung 80708, Taiwan., Bender D; Institute of Biochemistry, Department of Chemistry, University of Cologne, 50674 Köln, Germany., Law SH; Department of Medical Laboratory Science and Biotechnology, College of Health Sciences, Kaohsiung Medical University, Kaohsiung 80708, Taiwan., Mishra VK; Department of Medical Laboratory Science and Biotechnology, College of Health Sciences, Kaohsiung Medical University, Kaohsiung 80708, Taiwan., Chen CC; Institute of Medical Science and Technology, National Sun Yat-sen University, Kaohsiung 80424, Taiwan., Ke LY; Department of Medical Laboratory Science and Biotechnology, College of Health Sciences, Kaohsiung Medical University, Kaohsiung 80708, Taiwan.; Center for Lipid Biosciences, Kaohsiung Medical University Hospital, Kaohsiung 80708, Taiwan.; Graduate Institute of Medicine, College of Medicine & Drug Development and Value Creation Research Center, Kaohsiung Medical University, Kaohsiung 80708, Taiwan. |
| Abstrakt: |
Human pathologies such as Alzheimer's disease, type 2 diabetes-induced insulin resistance, cancer, and cardiovascular diseases have altered lipid homeostasis. Among these imbalanced lipids, the bioactive sphingolipids ceramide and sphingosine-1 phosphate (S1P) are pivotal in the pathophysiology of these diseases. Several enzymes within the sphingolipid pathway contribute to the homeostasis of ceramide and S1P. Ceramidase is key in the degradation of ceramide into sphingosine and free fatty acids. In humans, five different ceramidases are known-acid ceramidase, neutral ceramidase, and alkaline ceramidase 1, 2, and 3-which are encoded by five different genes ( ASAH1 , ASAH2 , ACER1 , ACER2 , and ACER3 , respectively). Notably, the neutral ceramidase N -acylsphingosine amidohydrolase 2 (ASAH2) shows considerable differences between humans and animals in terms of tissue expression levels. Besides, the subcellular localization of ASAH2 remains controversial. In this review, we sum up the results obtained for identifying gene divergence, structure, subcellular localization, and manipulating factors and address the role of ASAH2 along with other ceramidases in human diseases. |
