9 results on '"Meimei Yin"'
Search Results
2. Dynamic interplay between IL-1 and WNT pathways in regulating dermal adipocyte lineage cells during skin development and wound regeneration
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Lixiang Sun, Xiaowei Zhang, Shuai Wu, Youxi Liu, Christian F. Guerrero-Juarez, Wenjie Liu, Jinwen Huang, Qian Yao, Meimei Yin, Jiacheng Li, Raul Ramos, Yanhang Liao, Rundong Wu, Tian Xia, Xinyuan Zhang, Yichun Yang, Fengwu Li, Shujun Heng, Wenlu Zhang, Minggang Yang, Chi-Meng Tzeng, Chao Ji, Maksim V. Plikus, Richard L. Gallo, and Ling-juan Zhang
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CP: Developmental biology ,CP: Stem cell research ,Biology (General) ,QH301-705.5 - Abstract
Summary: Dermal adipocyte lineage cells are highly plastic and can undergo reversible differentiation and dedifferentiation in response to various stimuli. Using single-cell RNA sequencing of developing or wounded mouse skin, we classify dermal fibroblasts (dFBs) into distinct non-adipogenic and adipogenic cell states. Cell differentiation trajectory analyses identify IL-1-NF-κB and WNT-β-catenin as top signaling pathways that positively and negatively associate with adipogenesis, respectively. Upon wounding, activation of adipocyte progenitors and wound-induced adipogenesis are mediated in part by neutrophils through the IL-1R-NF-κB-CREB signaling axis. In contrast, WNT activation, by WNT ligand and/or ablation of Gsk3, inhibits the adipogenic potential of dFBs but promotes lipolysis and dedifferentiation of mature adipocytes, contributing to myofibroblast formation. Finally, sustained WNT activation and inhibition of adipogenesis is seen in human keloids. These data reveal molecular mechanisms underlying the plasticity of dermal adipocyte lineage cells, defining potential therapeutic targets for defective wound healing and scar formation.
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- 2023
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3. Keratin 6, 16 and 17—Critical Barrier Alarmin Molecules in Skin Wounds and Psoriasis
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Xiaowei Zhang, Meimei Yin, and Ling-juan Zhang
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keratins ,epidermal keratinocytes ,barrier alarmins ,skin wounds ,psoriasis ,proliferation ,innate immune responses ,autoimmune ,Cytology ,QH573-671 - Abstract
Located at the skin surface, keratinocytes (KCs) are constantly exposed to external stimuli and are the first responders to invading pathogens and injury. Upon skin injury, activated KCs secrete an array of alarmin molecules, providing a rapid and specific innate immune response against danger signals. However, dysregulation of the innate immune response of KCs may lead to uncontrolled inflammation and psoriasis pathogenesis. Keratins (KRT) are the major structural intermediate filament proteins in KCs and are expressed in a highly specific pattern at different differentiation stages of KCs. While KRT14-KRT5 is restricted to basal proliferative KCs, and KRT10-KRT1 is restricted to suprabasal differentiated KCs in normal skin epidermis, the wound proximal KCs downregulate KRT10-K1 and upregulate KRT16/KRT17-KRT6 upon skin injury. Recent studies have recognized KRT6/16/17 as key early barrier alarmins and upregulation of these keratins alters proliferation, cell adhesion, migration and inflammatory features of KCs, contributing to hyperproliferation and innate immune activation of KCs in response to an epidermal barrier breach, followed by the autoimmune activation of T cells that drives psoriasis. Here, we have reviewed how keratins are dysregulated during skin injury, their roles in wound repairs and in initiating the innate immune system and the subsequent autoimmune amplification that arises in psoriasis.
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- 2019
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4. Regulation of SRF protein stability by an autophagy-dependent pathway
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Meimei Yin, Felix Q Jin, Zheng Gen Jin, and Jinque Luo
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0301 basic medicine ,Serum Response Factor ,genetic structures ,Biophysics ,Cycloheximide ,Biochemistry ,Article ,Culture Media, Serum-Free ,03 medical and health sciences ,chemistry.chemical_compound ,0302 clinical medicine ,Western blot ,Lysosome ,Serum response factor ,Chlorocebus aethiops ,medicine ,Autophagy ,Animals ,Humans ,Molecular Biology ,Zebrafish ,Gene ,Transcription factor ,Cells, Cultured ,Glycogen Synthase Kinase 3 beta ,biology ,medicine.diagnostic_test ,Chemistry ,Protein Stability ,Cell Biology ,biology.organism_classification ,musculoskeletal system ,eye diseases ,Cell biology ,Rats ,030104 developmental biology ,medicine.anatomical_structure ,030220 oncology & carcinogenesis ,embryonic structures ,COS Cells ,cardiovascular system ,Lysosomes - Abstract
Serum response factor (SRF), a key transcription factor, plays an important role in regulating cell functions such as proliferation and differentiation. Most proteins are unstable, and protein stability is regulated through the ubiquitin-proteasome system (UPS) or the autophagy lysosome pathway (ALP). Whether SRF is degraded and what mechanisms control SRF protein stability remain unexplored. Western blot analyses of cells treated with cycloheximide (CHX), a protein synthesis inhibitor, showed that SRF was degraded in a time-dependent manner. Moreover, we observed that SRF undergoes autophagy-dependent destruction, which is accelerated by serum deprivation. Through bioinformatics screening, we found that SRF contains the GSK3β phosphorylation motif (T/SPPXS): SPDSPPRSDPT, which is conserved from zebrafish to humans. Serum deprivation stimulated GSK3β activation that then potentiates SRF degradation through the autophagy lysosome pathway. Since SRF is important for numerous cellular activities, our results suggest that the autophagy-dependent SRF degradation pathway may provide a new avenue to modulate SRF-mediated cell functions.
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- 2019
5. Endothelial-specific YY1 governs sprouting angiogenesis through directly interacting with RBPJ.
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Shuya Zhang, Ji Young Kim, Suowen Xu, Huan Liu, Meimei Yin, Koroleva, Marina, Jia Guo, Xiuying Pei, and Zheng Gen Jin
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NEOVASCULARIZATION ,NOTCH proteins ,RETINAL blood vessels ,TRANSCRIPTION factors ,CARRIER proteins - Abstract
Angiogenesis, the formation of new blood vessels, is tightly regulated by gene transcriptional programs. Yin Ying 1 (YY1) is a ubiquitously distributed transcription factor with diverse and complex biological functions; however, little is known about the cell-type-specific role of YY1 in vascular development and angiogenesis. Here we report that endothelial cell (EC)-specific YY1 deletion in mice led to embryonic lethality as a result of abnormal angiogenesis and vascular defects. Tamoxifen-inducible EC-specific YY1 knockout (YY1
iΔEC ) mice exhibited a scarcity of retinal sprouting angiogenesis with fewer endothelial tip cells. YY1iΔEC mice also displayed severe impairment of retinal vessel maturation. In an ex vivo mouse aortic ring assay and a human EC culture system, YY1 depletion impaired endothelial sprouting and migration. Mechanistically, YY1 functions as a repressor protein of Notch signaling that controls EC tip-stalk fate determination. YY1 deficiency enhanced Notch-dependent gene expression and reduced tip cell formation. Specifically, YY1 bound to the N-terminal domain of RBPJ (recombination signal binding protein for Ig Kappa J region) and competed with the Notch coactivator MAML1 (mastermind-like protein 1) for binding to RBPJ, thereby impairing the NICD (intracellular domain of the Notch protein)/MAML1/RBPJ complex formation. Our study reveals an essential role of endothelial YY1 in controlling sprouting angiogenesis through directly interacting with RBPJ and forming a YY1-RBPJ nuclear repression complex. [ABSTRACT FROM AUTHOR]- Published
- 2020
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6. PECAM1 regulates flow-mediated Gab1 tyrosine phosphorylation and signaling
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Zheng Gen Jin, Chang Hoon Ha, Michael A. Mastrangelo, Marina Koroleva, Meimei Yin, Felix Q Jin, Keigi Fujiwara, Weiye Wang, Xiangbin Xu, and Suowen Xu
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0301 basic medicine ,Nitric Oxide Synthase Type III ,Morpholines ,Protein Tyrosine Phosphatase, Non-Receptor Type 11 ,030204 cardiovascular system & hematology ,Article ,03 medical and health sciences ,chemistry.chemical_compound ,Mice ,0302 clinical medicine ,Enos ,medicine ,Human Umbilical Vein Endothelial Cells ,Animals ,Humans ,Tyrosine ,Phosphorylation ,RNA, Small Interfering ,Protein kinase B ,PI3K/AKT/mTOR pathway ,Adaptor Proteins, Signal Transducing ,Mice, Knockout ,biology ,Hepatocyte Growth Factor ,Tyrosine phosphorylation ,Cell Biology ,biology.organism_classification ,Phosphoproteins ,Recombinant Proteins ,Cell biology ,Mice, Inbred C57BL ,Platelet Endothelial Cell Adhesion Molecule-1 ,030104 developmental biology ,Biochemistry ,chemistry ,Chromones ,Hepatocyte growth factor ,RNA Interference ,Signal transduction ,Proto-Oncogene Proteins c-akt ,medicine.drug ,Signal Transduction - Abstract
Endothelial dysfunction, characterized by impaired activation of endothelial nitric oxide (NO) synthase (eNOS) and ensued decrease of NO production, is a common mechanism of various cardiovascular pathologies, including hypertension and atherosclerosis. Laminar blood flow-mediated specific signaling cascades modulate vascular endothelial cells (ECs) structure and functions. We have previously shown that flow-stimulated Gab1 (Grb2-associated binder-1) tyrosine phosphorylation mediates eNOS activation in ECs, which in part confers laminar flow atheroprotective action. However, the molecular mechanisms whereby flow regulates Gab1 tyrosine phosphorylation and its downstream signaling events remain unclear. Here we show that platelet endothelial cell adhesion molecule-1 (PECAM1), a key molecule in an endothelial mechanosensing complex, specifically mediates Gab1 tyrosine phosphorylation and its downstream Akt and eNOS activation in ECs upon flow rather than hepatocyte growth factor (HGF) stimulation. Small interfering RNA (siRNA) targeting PECAM1 abolished flow- but not HGF-induced Gab1 tyrosine phosphorylation and Akt, eNOS activation as well as Gab1 membrane translocation. Protein-tyrosine phosphatase SHP2, which has been shown to interact with Gab1, was involved in flow signaling and HGF signaling, as SHP2 siRNA diminished the flow- and HGF-induced Gab1 tyrosine phosphorylation, membrane localization and downstream signaling. Pharmacological inhibition of PI3K decreased flow-, but not HGF-mediated Gab1 phosphorylation and membrane localization as well as eNOS activation. Finally, we observed that flow-mediated Gab1 and eNOS phosphorylation in vivo induced by voluntary wheel running was reduced in PECAM1 knockout mice. These results demonstrate a specific role of PECAM1 in flow-mediated Gab1 tyrosine phosphorylation and eNOS signaling in ECs.
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- 2015
7. Early and late effects of the DPP-4 inhibitor vildagliptin in a rat model of post-myocardial infarction heart failure
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Herman H W Silljé, Maxi Meissner, Meimei Yin, Rudolf A. de Boer, Wiek H. van Gilst, and Cardiovascular Centre (CVC)
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Male ,lcsh:Diseases of the circulatory (Cardiovascular) system ,Pyrrolidines ,Time Factors ,Endocrinology, Diabetes and Metabolism ,LEFT-VENTRICULAR PERFORMANCE ,heart failure ,Adamantane ,ISCHEMIA-REPERFUSION INJURY ,Rats, Sprague-Dawley ,Random Allocation ,Atrial natriuretic peptide ,MYOCARDIAL GLUCOSE-UPTAKE ,GLYCEMIC CONTROL ,Vildagliptin ,Myocardial infarction ,Original Investigation ,Ejection fraction ,GLUCAGON-LIKE PEPTIDE-1 ,diabetes ,Dilated cardiomyopathy ,Brain natriuretic peptide ,myocardial infarction ,vildagliptin ,Cardiology ,Cardiology and Cardiovascular Medicine ,medicine.drug ,Cardiac function curve ,medicine.medical_specialty ,Dipeptidyl Peptidase 4 ,ISCHEMIA/REPERFUSION INJURY ,Drug Administration Schedule ,CARDIAC-FUNCTION ,Internal medicine ,Nitriles ,medicine ,Animals ,Dipeptidyl-Peptidase IV Inhibitors ,business.industry ,medicine.disease ,DILATED CARDIOMYOPATHY ,RECEPTOR AGONISTS ,Rats ,Disease Models, Animal ,Endocrinology ,lcsh:RC666-701 ,Heart failure ,cardiac remodeling ,business ,DIPEPTIDYL PEPTIDASE-4 INHIBITORS - Abstract
Background Progressive remodeling after myocardial infarction (MI) is a leading cause of morbidity and mortality. Recently, glucagon-like peptide (GLP)-1 was shown to have cardioprotective effects, but treatment with GLP-1 is limited by its short half-life. It is rapidly degraded by the enzyme dipeptidyl peptidase-4 (DPP-4), an enzyme which inhibits GLP-1 activity. We hypothesized that the DPP-4 inhibitor vildagliptin will increase levels of GLP-1 and may exert protective effects on cardiac function after MI. Methods Sprague-Dawley rats were either subjected to coronary ligation to induce MI and left ventricular (LV) remodeling, or sham operation. Parts of the rats with an MI were pre-treated for 2 days with the DPP-4 inhibitor vildagliptin (MI-Vildagliptin immediate, MI-VI, 15 mg/kg/day). The remainder of the rats was, three weeks after coronary artery ligation, subjected to treatment with DPP-4 inhibitor vildagliptin (MI-Vildagliptin Late, MI-VL) or control (MI). At 12 weeks, echocardiography and invasive hemodynamics were measured and molecular analysis and immunohistochemistry were performed. Results Vildagliptin inhibited the DPP-4 enzymatic activity by almost 70% and increased active GLP-1 levels by about 3-fold in plasma in both treated groups (p < 0.05 vs. non-treated groups). Cardiac function (ejection fraction) was decreased in all 3 MI groups compared with Sham group (p < 0.05); treatment with vildagliptin, either early or late, did not reverse cardiac remodeling. ANP (atrial natriuretic peptide) and BNP (brain natriuretic peptide) mRNA levels were significantly increased in all 3 MI groups, but no significant reductions were observed in both vildagliptin groups. Vildagliptin also did not change cardiomyocyte size or capillary density after MI. No effects were detected on glucose level and body weight in the post-MI remodeling model. Conclusion Vildagliptin increases the active GLP-1 level via inhibition of DPP-4, but it has no substantial protective effects on cardiac function in this well established long-term post-MI cardiac remodeling model.
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- 2011
8. Metformin improves cardiac function in a nondiabetic rat model of post-MI heart failure
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Wiek H. van Gilst, C. Qian, Iwan C. C. van der Horst, Herman H W Silljé, Rudolf A. de Boer, Meimei Yin, Joost P. van Melle, Critical care, Anesthesiology, Peri-operative and Emergency medicine (CAPE), and Cardiovascular Centre (CVC)
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Blood Glucose ,Male ,Time Factors ,endocrine system diseases ,Physiology ,PROGRESSION ,AMP-Activated Protein Kinases ,Ventricular Function, Left ,Muscle hypertrophy ,Rats, Sprague-Dawley ,Insulin ,Myocardial infarction ,Phosphorylation ,IN-VIVO ,remodeling ,Glucose tolerance test ,OUTCOMES ,Ventricular Remodeling ,medicine.diagnostic_test ,diabetes ,ACTIVATED PROTEIN-KINASE ,Metformin ,myocardial infarction ,Cardiology ,Hypertrophy, Left Ventricular ,Cardiology and Cardiovascular Medicine ,Atrial Natriuretic Factor ,medicine.drug ,Cardiac function curve ,medicine.medical_specialty ,Cardiotonic Agents ,METABOLISM ,left ventricular function ,CARDIOPROTECTION ,Physiology (medical) ,Diabetes mellitus ,Internal medicine ,medicine ,Animals ,Hypoglycemic Agents ,CELL ,Heart Failure ,business.industry ,Myocardium ,nutritional and metabolic diseases ,Stroke Volume ,DIABETES-MELLITUS ,Glucose Tolerance Test ,medicine.disease ,Fibrosis ,Rats ,HYPERTROPHY ,Disease Models, Animal ,Gene Expression Regulation ,MYOCARDIAL-INFARCTION ,Heart failure ,Myocardial infarction complications ,Energy Metabolism ,business - Abstract
Yin M, van der Horst IC, van Melle JP, Qian C, van Gilst WH, Sillje HH, de Boer RA. Metformin improves cardiac function in a nondiabetic rat model of post-MI heart failure. Am J Physiol Heart Circ Physiol 301: H459-H468, 2011. First published May 13, 2011; doi:10.1152/ajpheart.00054.2011.-Metformin is the first choice drug for the treatment of patients with diabetes, but its use is debated in patients with advanced cardiorenal disease. Epidemiological data suggest that metformin may reduce cardiac events, in patients both with and without heart failure. Experimental evidence suggests that metformin reduces cardiac ischemia-reperfusion injury. It is unknown whether metformin improves cardiac function (remodeling) in a long-term post-MI remodeling model. We therefore studied male, nondiabetic, Sprague-Dawley rats that were subjected to either myocardial infarction (MI) or sham operation. Animals were randomly allocated to treatment with normal water or metformin-containing water (250 mg.kg(-1).day(-1)). At baseline, 6 wk, and 12 wk, metabolic parameters were analyzed and oral glucose tolerance tests (OGTT) were performed. Echocardiography and hemodynamic parameters were assessed 12 wk after MI. In the MI model, infarct size was significantly smaller after 12-wk metformin treatment (29.6 +/- 3.2 vs. 38.0 +/- 2.2%, P
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- 2011
9. Metformin improves cardiac function in a nondiabetic rat model of post-MI heart failure.
- Author
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Meimei Yin, van der Horst, Iwan C. C., van Melle, Joost P., Cheng Qian, van Gilst, Wiek H., Silljé, Herman H. W., and de Boer, Rudolf A.
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METFORMIN , *MYOCARDIAL infarction , *DIABETES , *ECHOCARDIOGRAPHY , *INSULIN , *RATS , *MESSENGER RNA - Abstract
Metformin is the first choice drug for the treatment of patients with diabetes, but its use is debated in patients with advanced cardiorenal disease. Epidemiological data suggest that metformin may reduce cardiac events, in patients both with and without heart failure. Experimental evidence suggests that metformin reduces cardiac ischemia-reperfusion injury. It is unknown whether metformin improves cardiac function (remodeling) in a long-term post-MI remodeling model. We therefore studied male, nondiabetic, Sprague-Dawley rats that were subjected to either myocardial infarction (MI) or sham operation. Animals were randomly allocated to treatment with normal water or metformin-containing water (250 mg·kg-1·day-1). At baseline, 6 wk, and 12 wk, metabolic parameters were analyzed and oral glucose tolerance tests (OGTT) were performed. Echocardiography and hemodynamic parameters were assessed 12 wk after MI. In the MI model, infarct size was significantly smaller after 12-wk metformin treatment (29.6 ± 3.2 vs. 38.0 ± 2.2%, P < 0.05). Moreover, metformin resulted in less left ventricular dilatation (6.0 ± 0.4 vs. 7.6 ± 0.6 mm, P < 0.05) and preservation of left ventricular ejection fraction (65.8 ± 3.7% vs. 48.6 ± 5.6%, P < 0.05) compared with MI control. The improved cardiac function was associated with decreased atrial natriuretic peptide mRNA levels in the metformin-treated group (50% reduction compared with MI, P < 0.05). Insulin resistance did not occur during cardiac remodeling (as indicated by normal OGTT) and fasting glucose levels and the pattern of the OGTT were not affected by metformin. Molecular analyses suggested that altered AMP kinase phosphorylation status and low insulin levels mediate the salutary effects of metformin. Altogether our results indicate that metformin may have potential to attenuate heart failure development after myocardial infarction, in the absence of diabetes and independent of systemic glucose levels. [ABSTRACT FROM AUTHOR]
- Published
- 2011
- Full Text
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