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Target intelligence / Profile preview
Cytidine monophosphate N-acetylneuraminic acid synthetase (CMAS)
- Target
- CMAS
- Molecular classification
- Enzyme, Transferase, Sialic acid metabolism enzyme
01
Overview
Cytidine monophosphate N-acetylneuraminic acid synthetase (CMAS) is a key enzyme in the sialic acid metabolism pathway, catalyzing the conversion of N-acetylneuraminic acid (Neu5Ac) and CTP into CMP-Neu5Ac—the universal donor for subsequent sialylation reactions. This activation step is essential for the biosynthesis of sialoglycoconjugates—glycoproteins and glycolipids with terminal sialic acids—which mediate critical biological processes such as cell–cell recognition, adhesion, immune modulation, and signal transduction. Changes in CMAS activity are linked to loss of cell surface sialylation, increased cancer cell invasivity, immune evasion in tumors, and defective T cell maintenance and survival. In cancer, particularly triple-negative breast cancer, CMAS is upregulated and promotes tumor growth and metastasis, positioning it as a potential therapeutic target and biomarker for aggressive disease.
- Other names
- N-acylneuraminate cytidylyltransferaseCMP-NeuNAc synthaseCMP-N-acetylneuraminic acid synthaseCMP-Neu5Ac synthetaseCSSCMP-sialic acid synthetaseCytidine 5'-monophosphate N-acetylneuraminic acid synthetase
02
Mechanism of action
Enzyme inhibition (RNA interference or small molecule inhibitors to reduce sialylation/cancer cell invasiveness); Modulation of sialic acid metabolism as potential anti-cancer strategy
03
Biological functions
Sialic acid activation for sialoglycoconjugate biosynthesisRegulation of cell surface sialylationCell–cell recognitionCell adhesionImmune modulationSignal transduction
04
Disease associations
Cancer (especially triple-negative breast cancer and pancreatic cancer)Infection (virulence factor in pathogenic bacteria)Other (glycan and immune-related pathologies)
05
Safety considerations
Targeting CMAS could lead to broad changes in cell surface glycosylation, potentially impairing normal cell recognition, immune function, or causing unanticipated off-target effectsCMAS knockout can abolish cell surface sialylation and disrupt immune cell development and survival
06
Interacting drugs
No clinically approved drugs directly targeting CMAS are known; experimental approaches may include inhibitors, RNAi, or metabolic pathway modulators targeting sialic acid biosynthesis/mechanisms
07
Biomarkers
Elevated CMAS mRNA or protein expression in triple-negative breast cancer and other aggressive cancer subtypes may indicate invasiveness/tumorigenic potentialCell surface sialic acid levels (via lectin binding assays)
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