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A Novel Truncated Form of Serum Amyloid A in Kawasaki Disease
John C Whitin1, Tom To-Sang Yu1, Xuefeng Bruce Ling2
1Department of Pediatrics, Stanford University, Stanford, California, United States of America.
Insights
Researchers identified a novel truncated form of serum amyloid A in children with Kawasaki disease (KD). This protein shows potential as a specific biomarker for diagnosing KD, distinguishing it from other febrile illnesses.
Area of Science:
- Biochemistry
- Immunology
- Pediatric Medicine
Background:
- Kawasaki disease (KD) is a critical pediatric vasculitis.
- Diagnosis of KD is challenging, lacking specific biomarkers.
- Existing biomarkers fail to differentiate KD from other febrile illnesses.
Purpose of the Study:
- To identify specific protein biomarkers for Kawasaki disease.
- To compare plasma proteomes of KD patients and febrile controls.
- To find novel diagnostic markers for KD.
Main Methods:
- Utilized anion exchange chromatography and SELDI mass spectrometry.
- Analyzed plasma from three independent cohorts of KD and febrile control subjects.
- Focused on statistically significant differences in mass spectra peaks.
Main Results:
- Discovered a 7,860 Da mass spectrometry peak with significantly higher intensity in acute KD.
- Identified this peak as a novel N-terminal truncated form of serum amyloid A.
- This truncated form was present in acute KD plasma and absent after symptom resolution.
Conclusions:
- A novel truncated serum amyloid A is elevated in Kawasaki disease plasma.
- This finding suggests potential as a diagnostic biomarker for KD.
- Further research will explore its role in KD pathophysiology and diagnostics.
Background:
Kawasaki disease (KD) is an acute vasculitis in children that can cause coronary artery abnormalities. Its diagnosis is challenging, and many cytokines, chemokines, acute phase reactants, and growth factors have failed evaluation as specific biomarkers to distinguish KD from other febrile illnesses. We performed protein profiling, comparing plasma from children with KD with febrile control (FC) subjects to determine if there were specific proteins or peptides that could distinguish the two clinical states.
Materials And Methods:
Plasma from three independent cohorts from the blood of 68 KD and 61 FC subjects was fractionated by anion exchange chromatography, followed by surface-enhanced laser desorption ionization (SELDI) mass spectrometry of the fractions. The mass spectra of KD and FC plasma samples were analyzed for peaks that were statistically significantly different.
Results:
A mass spectrometry peak with a mass of 7,860 Da had high intensity in acute KD subjects compared to subacute KD (p = 0.0003) and FC (p = 7.9 x 10-10) subjects. We identified this peak as a novel truncated form of serum amyloid A with N-terminal at Lys-34 of the circulating form and validated its identity using a hybrid mass spectrum immunoassay technique. The truncated form of serum amyloid A was present in plasma of KD subjects when blood was collected in tubes containing protease inhibitors. This peak disappeared when the patients were examined after their symptoms resolved. Intensities of this peptide did not correlate with KD-associated laboratory values or with other mass spectrum peaks from the plasma of these KD subjects.
Conclusions:
Using SELDI mass spectrometry, we have discovered a novel truncated form of serum amyloid A that is elevated in the plasma of KD when compared with FC subjects. Future studies will evaluate its relevance as a diagnostic biomarker and its potential role in the pathophysiology of KD.
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