Конспект лекцій із навчальної дисципліни «Бухгалтерський та управлінський облік» для студентів за спеціальністю 073 - Менеджмент.

Data 4. 450 differentially expressed lincRNAs with significance (P <0.05, q <0.05). (XLSX 113 kb

<i>IGFBP2</i> expression levels in MSCs.

<p>(A) Real-time RT-PCR revealed that lower <i>IGFBP2</i> expression in WJCMSCs than that in PDLSCs, BMSCs, and ASCs. (B-E) Increased <i>IGFBP2</i> expression after adipogenic induction in PDLSCs (B), BMSCs (C), ASCs (D), and WJCMSCs (E). <i>GAPDH</i> was used as an internal control. **<i>p</i> < 0.01. w: week; PM: proliferation medium; AM: adipose-inducing medium.</p

Effect of Akt inhibitor on <i>IGFBP2</i>-induced adipogenic differentiation of WJCMSCs.

<p>(A) Western Blotting results showed a reduction of p-Akt in WJCMSC-Flag-<i>IGFBP2</i> following treatment with an Akt inhibitor, LY294002 (10 μM, 20 μM, 50 μM or 80 μM in DMSO) for 1 h during adipogenic induction. (B) Quantitative analysis of p-Akt based on Western Blot results. Total Akt was used as internal control. The expression levels that are indicated with the same letter do not differ significantly. (C-D) Oil Red O staining and quantitative analysis showed that 10 μM LY294002 effectively inhibited <i>IGFBP2</i>-mediated adipogenic differentiation. Scale bar: 100 μm. (E-F) Real-time RT-PCR results showed downregulated expressions of <i>PPARγ</i> (E) and <i>LPL</i> (F) in WJCMSC-Flag-<i>IGFBP2</i> cells following 10 μM LY294002 treatment during adipogenic induction at 1, 2, and 3 weeks. <i>GAPDH</i> was used as an internal control. **<i>p</i> < 0.01. α: anti; w: week.</p

<i>BCOR</i> decreases <i>IGFBP2</i> expression and weakens adipogenic differentiation in WJCMSCs.

<p>(A) Flag-<i>BCOR</i>-infected WJCMSCs showed BCOR overexpression, as determined by Western Blot analysis. GAPDH was used as an internal control. (B) Real-time RT-PCR analysis showed that <i>BCOR</i> overexpression suppressed the expression of <i>IGFBP2</i> in WJCMSCs. <i>GAPDH</i> was used as an internal control. (C-D) Oil Red O staining and quantitative analysis showed that <i>BCOR</i> overexpression inhibited the formation of lipid deposits. Scale bar: 500 μm (a, b), 100μm (c, d). **<i>p</i> < 0.01. α: anti; w: week.</p

<i>IGFBP2</i> activates JNK and Akt signaling pathways.

<p>(A) Western Blot analysis demonstrated that <i>IGFBP2</i> overexpression caused an increase in p-JNK and p-Akt in WJCMSCs, however, the total amounts of JNK, ERK, p38, and Akt proteins were not affected; The phosphorylated p38 protein was not found. (B) Quantitative analysis of p-ERK, p-JNK, and p-Akt based on Western Blot results for the WJCMSC-Flag-<i>IGFBP2</i> cells and WJCMSC-Vector cells. Total ERK, JNK, and Akt were used as internal control respectively. **<i>p</i> < 0.01. α: anti.</p

IGFBP2 enhances adipogenic differentiation potentials of mesenchymal stem cells from Wharton's jelly of the umbilical cord <i>via</i> JNK and Akt signaling pathways

<div><p>Mesenchymal stem cell (MSC)-mediated tissue engineering represents a promising strategy to address adipose tissue defects. MSCs derived from Wharton’s jelly of the umbilical cord (WJCMSCs) may serve as an ideal source for adipose tissue engineering due to their abundance, safety profile, and accessibility. How to activate the directed differentiation potentials of WJCMSCs is the core point for their clinical applications. A thorough investigation of mechanisms involved in WJCMSC adipogenic differentiation is necessary to support their application in adipose tissue engineering and address shortcomings. Previous study showed, compared with periodontal ligament stem cells (PDLSCs), WJCMSCs had a weakened adipogenic differentiation potentials and lower expression of insulin-like growth factor binding protein 2 (<i>IGFBP2</i>). IGFBP2 may be involved in the adipogenesis of MSCs. Generally, IGFBP2 is involved in regulating biological activity of insulin-like growth factors, however, its functions in human MSCs are unclear. Here, we found <i>IGFBP2</i> expression was upregulated upon adipogenic induction, and that <i>IGFBP2</i> enhanced adipogenic differentiation of WJCMSCs and BMSCs. Moreover, IGFBP2 increased phosphorylation of c-Jun N-terminal kinase (p-JNK) and p-Akt, and activated JNK or Akt signaling significantly promoted adipogenic differentiation of MSCs. Furthermore, inhibitor-mediated blockage of either JNK or Akt signaling dramatically reduced <i>IGFBP2</i>-mediated adipogenic differentiation. And the JNK inhibitor, SP600125 markedly blocked <i>IGFBP2</i>-mediated Akt activation. Moreover, <i>IGFBP2</i> was negatively regulated by <i>BCOR</i>, which inhibited adipogenic differentiation of WJCMSCs. Overall, our results reveal a new function of <i>IGFBP2</i>, providing a novel insight into the mechanism of adipogenic differentiation and identifying a potential target mediator for improving adipose tissue engineering based on WJCMSCs.</p></div

Effect of JNK inhibitor on <i>IGFBP2</i>-induced adipogenic differentiation of WJCMSCs.

<p>(A) Western Blot analysis showed a reduction of p-JNK in WJCMSC-Flag-<i>IGFBP2</i> after treatment with a JNK inhibitor, SP600125 (10 μM, 20 μM, 50 μM or 100 μM in DMSO) for 48 h during adipogenic induction. (B) Quantitative analysis of p-JNK based on Western Blot results. Total JNK was used as internal control. The expression levels that are indicated with the same letter do not differ significantly. (C-D) Oil Red O staining and quantitative analysis revealed that 20 μM SP600125 effectively suppressed <i>IGFBP2</i>-mediated enhancement of lipid formation. Scale bar: 100 μm. (E-F) Real-time RT-PCR results showed downregulated expressions of <i>PPARγ</i> (E) and <i>LPL</i> (F) in WJCMSC-Flag-<i>IGFBP2</i> cells following 20 μM SP600125 treatment during adipogenic induction at 1, 2, and 3 weeks. <i>GAPDH</i> was used as an internal control. **<i>p</i> < 0.01. α: anti; w: week.</p

<i>IGFBP2</i> overexpression enhances adipogenic differentiation in WJCMSCs.

<p>(A) Flag-<i>IGFBP2</i>-infected WJCMSCs showed <i>IGFBP2</i> overexpression by real-time RT-PCR. <i>GAPDH</i> was used as an internal control. (B) Overexpression of IGFBP2 was verified by Western Blot analysis. (C-D) Oil Red O staining and quantitative analysis showed that <i>IGFBP2</i> overexpression prompted formation of lipid deposits. Scale bar: 100 μm. (E-H) Real-time RT-PCR showed that overexpression of <i>IGFBP2</i> upregulated expressions of <i>PPARγ</i> (E), <i>LPL</i> (F), <i>CD36</i> (G), and <i>CEBPA</i> (H) in WJCMSCs at 0, 1, and 2 weeks after induction. <i>GAPDH</i> was used as an internal control. *<i>p</i> < 0.05. **<i>p</i> < 0.01. α: anti; w: week.</p

A summary of the samples collected and the iodine nutrition status of the survey sites.

<p>A summary of the samples collected and the iodine nutrition status of the survey sites.</p

Diagnostic criteria for the thyroid diseases included in this study.

<p>^*Reference ranges: FT3, 2.77–5.85 pmol/L; FT4, 10.06–23.99 pmol/L; TSH, 0.38–5.57 mIU/L; TPOAb, 0–2.6 IU/ml; TgAb, 0–14.58 IU/ml; TRAb, 0.11–30 IU/ml. Reference ranges were provided by the second affiliated hospital of Harbin Medical University.</p><p>Diagnostic criteria for the thyroid diseases included in this study.</p