Target intelligence / Profile preview

Alpha-1-antichymotrypsin (SERPINA3)

Target
SERPINA3
Molecular classification
Serine protease inhibitor (Serpin superfamily), Acute-phase protein (expressed in response to inflammation), Glycoprotein (structurally), Secreted protein
01

Overview

Alpha-1-antichymotrypsin (SERPINA3) is a secreted glycoprotein and member of the serpin (serine protease inhibitor) superfamily, encoded by the SERPINA3 gene. It functions mainly as an acute-phase protein, produced predominantly in the liver in response to inflammatory stimuli. SERPINA3 inhibits activity of multiple serine proteases, especially cathepsin G and mast cell chymase, thus protecting tissues from proteolytic damage and modulating key inflammatory and cell signaling pathways. It is implicated in the regulation of cell proliferation, apoptosis, and extracellular matrix remodeling through the PI3K/AKT and MAPK/ERK signal pathways. SERPINA3 is strongly upregulated during inflammation and in multiple pathological contexts, including cancer, neurodegenerative, and cardiovascular diseases, playing diverse and sometimes opposing roles depending on tissue and disease type. Deficiency or dysregulation of SERPINA3 is associated with a variety of pathological conditions, notably liver disease, neurodegeneration, and poor cancer prognosis.

Other names
Alpha-1-antichymotrypsinAACTACTGIG24GIG25Growth-inhibiting protein 24Growth-inhibiting protein 25Serpine peptidase inhibitor, clade A, member 3SERPINA3Cell growth-inhibiting gene 24/25 proteinSerpin A3
02

Mechanism of action

Direct inhibition or modulation of serine protease activity (exploited in research, not in approved therapeutics); Modulation of apoptosis and proliferation via signal transduction pathways (PI3K/AKT, MAPK/ERK)

03

Biological functions

Inhibition of serine proteases (especially cathepsin G, chymase)Regulation of inflammation (acute-phase anti-inflammatory response)Extracellular matrix protection (limits protease-mediated damage)Cell proliferation regulationCell death/apoptosis modulation (antiapoptotic functions via PI3K/AKT, MAPK/ERK pathways)DNA binding (exact physiological significance remains unclear)Regulation of pancreas secretory functionPromotion/inhibition of adipogenesis depending on context
04

Disease associations

Cancer (prognostic and mechanistic roles in breast, colon, endometrial, gastric, melanoma, glioblastoma, hepatocellular carcinoma, others; correlates with poor prognosis in many types)Neurodegenerative disease (Alzheimer’s, Creutzfeldt–Jakob, Parkinson’s; promotes amyloid formation, implicated in pathogenesis)Cardiovascular disease (heart failure, aortic aneurysm, vascular remodeling)Inflammation (acute phase conditions, chronic inflammatory diseases)Infection (acute-phase response to infection, antiviral roles)Liver disease (deficiency)Chronic obstructive pulmonary disease
05

Safety considerations

Potential for promoting tumor progression (antiapoptotic, associated with poor prognosis in several cancers)Complex role in different disease contexts (may be protective in some cardiovascular scenarios, detrimental in others)Limited direct targeting strategies; approaches focus on modulating downstream effects or expression
06

Interacting drugs

No specific drugs are approved or widely reported to target SERPINA3 directly. Indirect modulation may occur with:

3 more in the full profile.

07

Biomarkers

SERPINA3 plasma/serum levels (acute-phase response, marker of inflammation, monitoring in cancer and neurodegenerative disease)Expression in tumor tissue (prognostic indicator in several cancer subtypes)

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