TY - JOUR
T1 - iTRAQ Proteomics Identified the Potential Biomarkers of Coronary Artery Lesion in Kawasaki Disease and In Vitro Studies Demonstrated That S100A4 Treatment Made HCAECs More Susceptible to Neutrophil Infiltration
AU - Weng, Ken Pen
AU - Chien, Kuang Jen
AU - Huang, Shih Hui
AU - Huang, Lien Hung
AU - Lin, Pei Hsien
AU - Lin, Yuyu
AU - Chang, Wei Hsiang
AU - Chen, Chun Yu
AU - Li, Sung Chou
N1 - Funding Information:
This study was supported by the grants from Kaohsiung Chang Gung Hospital (CMRPG8H0511 and CMRPG8M0541) and the Kaohsiung Veterans General Hospital (VGHKS109-108, KSVGH111-101).
Publisher Copyright:
© 2022 by the authors.
PY - 2022/11
Y1 - 2022/11
N2 - Coronary artery lesions (CAL) are a major complication of Kawasaki disease (KD). The early prediction of CAL enables the medical personnel to apply adequate medical intervention. We collected the serum samples from the KD patients with CAL (n = 32) and those without CAL (n = 31), followed by a global screening with isobaric tagging for relative and absolute quantification (iTRAQ) technology and specific validation with an enzyme-linked immunosorbent assay (ELISA). iTRAQ identified 846 proteins in total in the serum samples, and four candidate proteins related to CAL were selected for ELISA validation as follows: Protein S100-A4 (S100A4), Catalase (CAT), Folate receptor gamma (FOLR3), and Galectin 10 (CLC). ELISA validation showed that the S100A4 level was significantly higher in KD patients with CAL than in those without CAL (225.2 ± 209.5 vs. 143.3 ± 83 pg/mL, p < 0.05). In addition, KD patients with CAL had a significantly lower CAT level than those without CAL (1.6 ± 1.5 vs. 2.7 ± 2.3 ng/mL, p < 0.05). Next, we found that S100A4 treatment on human coronary artery endothelial cells (HCAECs) reduced the abundance of cell junction proteins, which promoted the migration of HCAECs. Further assays also demonstrated that S100A4 treatment enhanced the permeability of the endothelial layer. These results concluded that S100A4 treatment resulted in an incompact endothelial layer and made HCAECs more susceptible to in vitro neutrophil infiltration. In addition, both upregulated S100A4 and downregulated CAT increased the risk of CAL in KD. Further in vitro study implied that S100A4 could be a potential therapeutic target for CAL in KD.
AB - Coronary artery lesions (CAL) are a major complication of Kawasaki disease (KD). The early prediction of CAL enables the medical personnel to apply adequate medical intervention. We collected the serum samples from the KD patients with CAL (n = 32) and those without CAL (n = 31), followed by a global screening with isobaric tagging for relative and absolute quantification (iTRAQ) technology and specific validation with an enzyme-linked immunosorbent assay (ELISA). iTRAQ identified 846 proteins in total in the serum samples, and four candidate proteins related to CAL were selected for ELISA validation as follows: Protein S100-A4 (S100A4), Catalase (CAT), Folate receptor gamma (FOLR3), and Galectin 10 (CLC). ELISA validation showed that the S100A4 level was significantly higher in KD patients with CAL than in those without CAL (225.2 ± 209.5 vs. 143.3 ± 83 pg/mL, p < 0.05). In addition, KD patients with CAL had a significantly lower CAT level than those without CAL (1.6 ± 1.5 vs. 2.7 ± 2.3 ng/mL, p < 0.05). Next, we found that S100A4 treatment on human coronary artery endothelial cells (HCAECs) reduced the abundance of cell junction proteins, which promoted the migration of HCAECs. Further assays also demonstrated that S100A4 treatment enhanced the permeability of the endothelial layer. These results concluded that S100A4 treatment resulted in an incompact endothelial layer and made HCAECs more susceptible to in vitro neutrophil infiltration. In addition, both upregulated S100A4 and downregulated CAT increased the risk of CAL in KD. Further in vitro study implied that S100A4 could be a potential therapeutic target for CAL in KD.
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U2 - 10.3390/ijms232112770
DO - 10.3390/ijms232112770
M3 - Article
C2 - 36361563
AN - SCOPUS:85141565119
SN - 1661-6596
VL - 23
JO - International journal of molecular sciences
JF - International journal of molecular sciences
IS - 21
M1 - 12770
ER -