User:Yayinruan/NAD+ glycohydrolase
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Article Draft[edit]
Lead[edit]
NADase is important to regulating adaptive immunity as T cells contain enzymes such as CD38 and SARM1 that consumes NAD+.[1]
Article body[edit]
CD38 is an enzyme that triggers inflammatory responses and type II CD38 contains an ecto-NADase or extracellular NADase, whereas type II CD38 contains an intracellular cADPR.[2] CD38 consumes NAD, which can produce second messengers that help regulate immune activity.[3] Cells that are programmed for cell death or apoptosis releases NAD+, and type II CD38 help recycle the extracellular NAD+ released from apoptosis, where both products of NADase, ADP-ribose and nicotinamide, can be used to resynthesize NAD+ via the NAD+ synthesis pathway.[2] ADP-ribose must be converted to adenosine in order to enter the NAD+ synthesis pathway, where ADP-ribose first gets converted to AMP and then AMP gets converted to adenosine via non-classical adenosine generational pathway.[2] The other product nicotinamide is membrane permeable, which allows the molecule to reenter the NAD synthesis pathway more easily.[2] CD38 NADase is also found in tissues and cells other than T cells, and CD38 is the one of the main form of NADase activity in mammals[3]
SARM1 is a Toll-like receptor protein and also functions as a intracellular NADase.[1] Under normal circumstances NADase activity are inhibited in the presence of NAD+, where NAD+ binds to armadillo/heat motifs (ARMs), which inhibits the dimerization of the toll-like receptor domain that activates the NADase activity.[1] If there are damages to the binding site of NAD+ or disruption that prevents the interaction between ARMs and the toll-like receptor domain, NADase activity will be turned on at a constitutive level.[1] As a result SARM1 will have higher consumption of NAD+ and produce NADase products (ADP-ribose and nicotinamide) rather than the production of cADPR from ADP-ribosyl cyclase.[1]
References[edit]
- ^ a b c d e Fang, Jiankai; Chen, Wangwang; Hou, Pengbo; Liu, Zhanhong; Zuo, Muqiu; Liu, Shisong; Feng, Chao; Han, Yuyi; Li, Peishan; Shi, Yufang; Shao, Changshun (2023-05-10). "NAD+ metabolism-based immunoregulation and therapeutic potential". Cell & Bioscience. 13 (1): 81. doi:10.1186/s13578-023-01031-5. ISSN 2045-3701. PMC 10171153. PMID 37165408.
{{cite journal}}: CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link) - ^ a b c d Lee, Hon Cheung; Deng, Qi Wen; Zhao, Yong Juan (2022-01). "The calcium signaling enzyme CD38 - a paradigm for membrane topology defining distinct protein functions". Cell Calcium. 101: 102514. doi:10.1016/j.ceca.2021.102514. ISSN 1532-1991. PMID 34896700.
{{cite journal}}: Check date values in:|date=(help) - ^ a b Chini, Eduardo Nunes. "CD38 as a Regulator of Cellular NAD: A Novel Potential Pharmacological Target for Metabolic Conditions". Current Pharmaceutical Design. 15 (1): 57–63. doi:10.2174/138161209787185788.