SCRN1 enhances calcium-dependent exocytosis in mast cells and neurons, promoting secretion of cytokines (e.g., TGF-β) and matrix metalloproteinases (MMP-2/MMP-9) .
SCRN1 stabilizes ER integrity by oligomerizing at ER membranes via VAP interactions .
Depletion impairs ER remodeling and synaptic vesicle recycling, reducing neurotransmission efficiency by ~40% .
SCRN1 is upregulated in oral squamous cell carcinoma (OSCC), colorectal cancer, and gastric cancer. Key mechanisms include:
Knockdown of SCRN1 in OSCC cell lines (HSC3, SCC15) reduces proliferation by 60% and invasion by 75% .
Alzheimer’s Disease (AD): SCRN1 co-localizes with phosphorylated tau in neurofibrillary tangles (NFTs) and dystrophic neurites. It interacts directly with hyperphosphorylated tau (p-tau), suggesting a role in AD-specific tauopathy .
Primary Age-Related Tauopathy (PART): SCRN1 accumulates in NFTs but not in corticobasal degeneration or Pick’s disease, indicating disease-specific involvement .
SCRN1’s functional network includes:
AD: SCRN1’s specificity for AD tau pathology positions it as a biomarker to distinguish AD from other tauopathies .
Structural basis of SCRN1-VAP binding.
SCRN1’s role in non-exocytic pathways (e.g., ER stress response).
Therapeutic efficacy of SCRN1 inhibition in preclinical models.
Secernin-1 (SCRN1) is a multifunctional protein encoded by the SCRN1 gene on human chromosome 7, with emerging roles in cancer biology and neurodegenerative diseases. Below are research-focused FAQs organized by complexity, supported by experimental evidence from peer-reviewed studies and patents.
SCRN1 regulates calcium-dependent exocytosis in mast cells through its conserved secernin domain, enhancing secretory granule release sensitivity . Key functional characteristics:
Molecular weight: 46.4 kDa (414 amino acids, Swiss-Prot ID: Q12765)
Structural features: Contains dipeptidase-like domain (residues 50-360) critical for vesicle trafficking
Cellular localization: Predominantly cytosolic with association to endoplasmic reticulum membranes
SCRN1 shows diagnostic utility through:
Elevated expression in 14+ cancer types (AUC=0.78-0.92 vs controls) :
Lung cancer: 4.8× increase vs normal (p<0.001)
Colorectal cancer: 3.2× increase (p=0.003)
Cut-off optimization: 98% specificity threshold at 2.7 ng/mL in serum
Prognostic value: Correlates with TNM stage (r=0.67, p<0.01) and recurrence risk
Experimental Design Tip: For longitudinal studies, use EDTA-plasma samples with protease inhibitors to prevent SCRN1 degradation .
SCRN1 demonstrates context-dependent roles:
Perform subcellular fractionation to distinguish cytosolic vs aggregated forms
Validate with RNAscope to confirm transcript vs protein-level changes
| Matrix | Recovery Rate | Interference Factors | Recommended Platform |
|---|---|---|---|
| Serum | 85-92% | Hemolysis (>5% Hb) | Electrochemiluminescence |
| CSF | 78% | High lipid content | LC-MS/MS |
| Urine | <50% | Protease activity | Immunoprecipitation-MS |
Pre-analytical factors: SCRN1 degrades within 2 hrs at RT (t1/2=94 min)
Cross-reactivity: Anti-SCRN1 antibodies show 18% homology with SCRN3
Confirm antibody specificity using recombinant SCRN1 (1-414 aa)
Stratify samples by:
Perform orthogonal validation (e.g., IHC + SRM-MS)
Secernin 1, also known as SCRN1, is a protein that has garnered significant interest in the scientific community due to its various roles in cellular processes and disease mechanisms. This article delves into the background, structure, function, and significance of Secernin 1, particularly focusing on its recombinant form used in research and therapeutic applications.
Secernin 1 is a cytosolic protein with a molecular weight of approximately 50 kDa . The recombinant form of Secernin 1 is typically produced in Escherichia coli (E. coli) and includes an N-terminal His-tag for purification purposes . The amino acid sequence of the recombinant human Secernin 1 corresponds to residues 1-414 of the native protein .
Recent studies have highlighted the involvement of Secernin 1 in neurodegenerative diseases, particularly Alzheimer’s disease . Secernin 1 has been identified as a novel amyloid plaque-associated protein. Immunohistochemistry studies have shown that Secernin 1 is present in plaque-associated dystrophic neurites and co-localizes with neurofibrillary tangles (NFTs) in Alzheimer’s disease . This unique association with tau pathology suggests that Secernin 1 could serve as a potential therapeutic target and biomarker for distinguishing Alzheimer’s disease from other tauopathies .
The recombinant form of Secernin 1 is widely used in research to study its function and role in disease. The protein is produced in E. coli and purified using affinity chromatography techniques . This recombinant protein is essential for various assays, including SDS-PAGE and immunohistochemistry, to investigate its interactions and functions at the molecular level .