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Fibulin2: a negative regulator of BMSC osteogenic differentiation in infected bone fracture healing
Li Shi-Dan,Xing Wei,Wang Shao-Chuan,Li You-Bin,Jiang Hao,Zheng Han-Xuan,Li Xiao-Ming,Yang Jing,Guo De-Bin,Xie Xiao-Yu,Jiang Ren-Qing,Fan Chao,Li Lei,Xu Xiang,Fei Jun 생화학분자생물학회 2023 Experimental and molecular medicine Vol.55 No.-
Bone fracture remains a common occurrence, with a population-weighted incidence of approximately 3.21 per 1000. In addition, approximately 2% to 50% of patients with skeletal fractures will develop an infection, one of the causes of disordered bone healing. Dysfunction of bone marrow mesenchymal stem cells (BMSCs) plays a key role in disordered bone repair. However, the specific mechanisms underlying BMSC dysfunction caused by bone infection are largely unknown. In this study, we discovered that Fibulin2 expression was upregulated in infected bone tissues and that BMSCs were the source of infection-induced Fibulin2. Importantly, Fibulin2 knockout accelerated mineralized bone formation during skeletal development and inhibited inflammatory bone resorption. We demonstrated that Fibulin2 suppressed BMSC osteogenic differentiation by binding to Notch2 and inactivating the Notch2 signaling pathway. Moreover, Fibulin2 knockdown restored Notch2 pathway activation and promoted BMSC osteogenesis; these outcomes were abolished by DAPT, a Notch inhibitor. Furthermore, transplanted Fibulin2 knockdown BMSCs displayed better bone repair potential in vivo. Altogether, Fibulin2 is a negative regulator of BMSC osteogenic differentiation that inhibits osteogenesis by inactivating the Notch2 signaling pathway in infected bone.
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Li Mao-Ye,Huang Yan,Lei Xiao,Xu Chuan-Tao,Li Bin,Chen De-Xin,Liu Su 한국응용곤충학회 2021 Journal of Asia-Pacific Entomology Vol.24 No.3
Heat shock proteins (HSPs) play essential roles in stress tolerance in insects, such as the cigarette beetle, Lasioderma serricorne, which is an important pest of stored products. However, the function of HSPs in envi ronmental stress response in L. serricorne is poorly understood. In this study, six cDNAs encoding putative HSP70s were identified in L. serricorne (LsHSP70-1 to LsHSP70-6). The LsHSP70 proteins identified have signature motifs of insect HSP70s and exhibit high amino-acid identity with their respective orthologs from other insect species. Phylogenetic analysis showed that these LsHSP70s fall into three major clans: HSP70 in the cytosol (four genes), endoplasmic reticulum (one gene), and mitochondria (one gene). LsHSP70 genes are differentially expressed in different developmental stages. LsHSP70-4 and LsHSP70-5 are mainly expressed at the larval stage, while LsHSP70-3 shows the highest level at the pupal stage. The other genes are ubiquitously expressed. Furthermore, the expression levels of LsHSP70-1 and LsHSP70-4 are significantly upregulated upon exposure to temperatures of both 0 and 15 ◦ C, while LsHSP70-3 is inducible at 15 ◦ C and LsHSP70-6 at 0 ◦ C. In addition, treatment at 0 ◦ C causes significant downregulation of LsHSP70-2 and LsHSP70-3. Exposure to a temperature of 30 ◦ C upregulates LsHSP70-1 expression, while 35 and 40 ◦ C treatments result in significantly enhanced transcription of all the LsHSP70 genes. To the best of the authors’ knowledge, this is the first report on the sequence characteristics, phylogenetic relationships, and expression profiles of HSP70 genes in L. serricorne. The cold- and heat-inducible regulation of LsHSP70s suggests that these genes are related to tolerance of abnormal temperatures.
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Formulation and Evaluation of Irinotecan Suppository for Rectal Administration
( Hai Yang Feng ),( Yu Ping Zhu ),( De Chuan Li ) 한국응용약물학회 2014 Biomolecules & Therapeutics(구 응용약물학회지) Vol.22 No.1
Irinotecan suppository was prepared using the moulding method with a homogeneous blend. A sensitive and specific fluorescence method was developed and validated for the determination of irinotecan in plasma using HPLC. The pharmacokinetics of intravenous administered and rectal administered in rabbits was investigated. Following a single intravenous dose of irinotecan (50 mg/kg), the plasma irinotecan concentration demonstrated a bi-exponential decay, with a rapid decline over 15 min. Cmax, t1/2, AUC0-30h and AUC0-∞ were 16.1 ± 2.7 g/ml, 7.6 ± 1.2 h, 71.3 ± 8.8 μg·h/μl and 82.3 ± 9.5 μg·h/ml, respectively. Following rectal administration of 100 mg/kg irinotecan, the plasma irinotecan concentration reached a peak of 5.3 ± 2.5 μg/ml at 4 h. The AUC0-30h and AUC0-∞ were 32.2 ± 6.2 μg·h/ml and 41.6 ± 7.2 μg·h/ml, respectively. It representing ~50.6% of the absolute bioavailability.
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