Abstract:Objective To study the association of the dynamic changes of peripheral blood human cartilage glycoprotein-39 (YKL-40) and high-mobility group box 1 (HMGB1) with bronchopulmonary dysplasia (BPD) in preterm infants. Methods Preterm infants, with a gestational age of 28-32 weeks and a birth weight of <1 500 g, who were admitted to the neonatal intensive care unit from July 2017 to August 2019 were prospectively selected and divided into a BPD group with 35 infants and a non-BPD group with 51 infants. ELISA was used to measure the serum concentrations of YKL-40 and HMGB1 in preterm infants on days 3, 7, and 14 after birth. Results The BPD group had a significantly lower serum YKL-40 concentration and a significantly higher serum HMGB1 concentration than the nonBPD group on days 3, 7, and 14 (P < 0.001). The serum concentrations of YKL-40 and HMGB1 on days 7 and 14 were significantly higher than those on day 3 in both groups (P < 0.017). In the BPD group, HMGB1 concentration on day 14 was significantly higher than that on day 7 (P < 0.017), while there was no significant change in YKL-40 concentration from day 7 to day 14 (P > 0.017). In the non-BPD group, YKL-40 concentration on day 14 was significantly higher than that on day 7 (P < 0.017), while there was no significant change in HMGB1 concentration from day 7 to day 14 (P > 0.017). Conclusions There are significant differences in the levels of YKL-40 and HMGB1 in peripheral blood between the preterm infants with BPD and those without BPD on days 3, 7, and 14 after birth, suggesting that YKL-40 and HMGB1 might be associated with the development of BPD.
ZHOU Yang,MENG Ling-Jian,WANG Jun. Changes in serum human cartilage glycoprotein-39 and high-mobility group box 1 in preterm infants with bronchopulmonary dysplasia[J]. CJCP, 2020, 22(4): 334-338.
Strueby L, Thébaud B. Advances in bronchopulmonary dysplasia[J]. Expert Rev Respir Med, 2014, 8(3):327-338.
[2]
Brener Dik PH, Niño Gualdron YM, Galletti MF, et al. Bronchopulmonary dysplasia:incidence and risk factors[J]. Arch Argent Pediatr, 2017, 115(5):476-482.
[3]
Rehli M, Niller HH, Ammon C, et al. Transcriptional regulation of CHI3L1, a marker gene for late stages of macrophage differentiation[J]. J Biol Chem, 2003, 278(45):44058-44067.
[4]
Francescone RA, Scully S, Faibish M, et al. Role of YKL-40 in the angiogenesis, radioresistance, and progression of glioblastoma[J]. J Biol Chem, 2011, 286(17):15332-15343.
[5]
Fan E, Brodie D, Slutsky AS. Acute respiratory distress syndrome:advances in diagnosis and treatment[J]. JAMA, 2018, 319(7):698-710.
[6]
Lotze MT, Tracey KJ. High-mobility group box 1 protein (HMGB1):nuclear weapon in the immune arsenal[J]. Nat Rev Immunol, 2005, 5(4):331-342.
[7]
Chupp GL, Lee CG, Jarjour N, et al. A chitinase-like protein in the lung and circulation of patients with severe asthma[J]. N Engl J Med, 2007, 357(20):2016-2027.
[8]
Sakazaki Y, Hoshino T, Takei S, et al. Overexpression of chitinase 3-like 1/YKL-40 in lung-specific IL-18-transgenic mice, smokers and COPD[J]. PLoS One, 2011, 6(9):e24177.
[9]
Hou C, Zhao H, Liu L, et al. High mobility group protein Bl (HMGB1) in asthma:comparison of patients with chronic obstructive pulmonary disease and healthy controls[J]. Mol Med, 2011, 17(7-8):807-815.
[10]
Zhou Y, Jiang YQ, Wang WX, et al. HMGB1 and RAGE levels in induced sputum correlate with asthma severity and neutrophil percentage[J]. Hum Immunol, 2012, 73(11):1171-1174.
Jiménez J, Richter J, Nagatomo T, et al. Progressive vascular functional and structural damage in a bronchopulmonary dysplasia model in preterm rabbits exposed to hyperoxia[J]. Int J Mol Sci, 2016, 17(10). pii:E1776.
Shao R, Taylor SL, Oh DS, et al. Vascular heterogeneity and targeting:the role of YKL-40 in glioblastoma vascularization[J]. Oncotarget, 2015, 6(38):40507-40518.
[15]
Park JA, Drazen JM, Tschumperlin DJ. The chitinase-like protein YKL-40 is secreted by airway epithelial cells at base line and in response to compressive mechanical stress[J]. J Biol Chem, 2010, 285(39):29817-29825.
[16]
Rathcke CN, Johansen JS, Vestergaard H. YKL-40, a biomarker of inflammation, is elevated in patients with type 2 diabetes and is related to insulin resistance[J]. Inflamm Res, 2006, 55(2):53-59.
[17]
Bara I, Ozier A, Girodet PO, et al. Role of YKL-40 in bronchial smooth muscle remodeling in asthma[J]. Am J Respir Crit Care Med, 2012, 185(7):715-722.
[18]
Zhu Z, Zheng T, Homer RJ, et al. Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation[J]. Science, 2004, 304(5677):1678-1682.
[19]
Miura T. Models of lung branching morphogenesis[J]. J Biochem, 2015, 157(3):121-127.
[20]
Been JV, Debeer A, van Iwaarden JF, et al. Early alterations of growth factor patterns in bronchoalveolar lavage fluid from preterm infants developing bronchopulmonary dysplasia[J]. Pediatr Res, 2010, 67(1):83-89.
[21]
Matsuura H, Hartl D, Kang MJ, et al. Role of breast regression protein-39 in the pathogenesis of cigarette smoke-induced inflammation and emphysema[J]. Am J Respir Cell Mol Biol, 2011, 44(6):777-786.
[22]
Francescone RA, Scully S, Faibish M, et al. Role of YKL-40 in the angiogenesis, radioresistance, and progression of glioblastoma[J]. J Biol Chem, 2011, 286(17):15332-15343.
Sohn MH, Kang MJ, Matsuura H, et al. The chitinase-like proteins breast regression protein-39 and YKL-40 regulate hyperoxia-induced acute lung injury[J]. Am J Respir Crit Care Med, 2010, 182(7):918-928.
Gong Q, Xu JF, Yin H, et al. Protective effect of antagonist of high-mobility group box 1 on lipopolysaccharide-induced acute lung injury in mice[J]. Scand J Immunol, 2009, 69(1):29-35.
[27]
Yu B, Li X, Wan Q, et al. High-mobility group box-1 protein disrupts alveolar elastogenesis of hyperoxia-injured newborn lungs[J]. J Interferon Cytokine Res, 2016, 36(3):159-168.