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1.
Sci Rep ; 14(1): 20893, 2024 09 08.
Article in English | MEDLINE | ID: mdl-39245669

ABSTRACT

Investigate the impact of remnant cholesterol (RC) levels on carotid artery intima thickness (CIT) in type 2 diabetes mellitus (T2DM) patients. From September 2021 to September 2023, a prospective multicenter study involved 158 T2DM patients. They were divided into a higher RC group (n = 80) and a lower RC group (n = 78) based on median RC levels. Additionally, 92 healthy volunteers served as the control group. CIT, carotid media thickness (CMT), and carotid intima-media thickness (CIMT) were measured. General clinical data, lab results, CIMT, CIT, and CMT differences among the three groups were compared. Multiple regression analysis explored CIT factors in T2DM patients. 1. No significant sex, age, BMI, high-density lipoprotein cholesterol (HDL-C), T2DM duration, fasting blood glucose, or glycated hemoglobin differences were found among the groups (p > 0.05). 2. CIMT and CIT were significantly higher in T2DM than the control group (p < 0.05). 3. The higher RC group had thicker CIT than the lower RC group (p < 0.05), while CIMT differences were not significant (p > 0.05). Multiple linear regression analysis showed RC as an influencing CIT factor in T2DM patients (ß = 0.473, p = 0.005). CIT is significantly thicker in T2DM patients with higher RC than in those with lower RC, and RC is the influence factor of CIT, which suggests that more attention should be paid to the detection of RC in T2DM patients.


Subject(s)
Carotid Intima-Media Thickness , Cholesterol , Diabetes Mellitus, Type 2 , Humans , Diabetes Mellitus, Type 2/blood , Diabetes Mellitus, Type 2/pathology , Male , Female , Middle Aged , Cholesterol/blood , Prospective Studies , Aged , Case-Control Studies , Adult , Risk Factors
3.
Exp Ther Med ; 27(3): 110, 2024 Mar.
Article in English | MEDLINE | ID: mdl-38361517

ABSTRACT

Diabetic kidney disease (DKD) is a severe microvascular complication of diabetes, one key feature of which includes renal fibrosis. As apelin is an adipokine closely related to diabetes, the present study aimed to evaluate apelin-13 expression levels and the relationship between apelin-13 and disease indicators in patients with diabetic kidney disease (DKD). The present case-control study enrolled 70 patients with diabetes, including 31 with diabetic kidney disease (DKD group), 39 without DKD (non-DKD group) and 30 healthy controls. The levels of serum apelin-13 and TGF-ß1, the key driver of renal fibrosis, were determined by ELISA. Additionally, age, mean disease duration, weight, blood pressure, fasting blood glucose, triglyceride, low-density lipoprotein cholesterol, high-density lipoprotein, cholesterol, urea nitrogen, blood creatinine and 24-hour urinary total protein (24-h UTP) were recorded. The results demonstrated that apelin-13 and TGF-ß1 expression levels, age, blood pressure, fasting blood glucose, cholesterol and blood urea nitrogen levels were significantly higher in patients with diabetes compared with the healthy controls (P<0.05). Moreover, apelin-13 and TGF-ß1 expression levels, mean disease duration, systolic pressure, blood creatinine, blood urea nitrogen and 24-h UTP were significantly higher in the DKD group compared with the non-DKD group (P<0.05). The estimated glomerular filtration rate (eGFR) was significantly reduced in the DKD group compared with the non-DKD group (P<0.05). Correlation analysis demonstrated a negative correlation between apelin-13 and eGFR expression and a positive correlation between apelin-13 expression and 24-h UTP in both the DKD and non-DKD groups (P<0.05). A negative correlation was also demonstrated between apelin-13 and TGF-ß1 expression levels in the DKD group and non-DKD groups (both P<0.05). In conclusion, apelin-13 and TGF-ß1 expression levels were significantly higher in the DKD group compared with those in the non-DKD group. Additionally, apelin-13 expression was negatively correlated with TGF-ß1 expression in the DKD and non-DKD groups. Therefore, apelin-13 could potentially be used in the future as an indicator of renal fibrosis or destruction in patients with DKD. The present trial was retrospectively registered in the Chinese Clinical Trial Registry (trial registration no. ChiCTR2200060945) on 14.06.2022.

4.
Nutrition ; 107: 111882, 2023 03.
Article in English | MEDLINE | ID: mdl-36527890

ABSTRACT

OBJECTIVES: This study aimed to investigate the hypoglycemic effect of highland barley ß-glucan (HBG) on mice with type 2 diabetes (T2D), and determine whether the hypoglycemic effects are related to modulations of the gut microbiota. METHODS: T2D was induced with a high-fat diet and streptozotocin in the mice. HBG was orally administered to mice with T2D for 4 wk, and biochemical indices were analyzed in the serum and liver. Fecal samples were collected and analyzed with high-throughput 16S ribosomal RNA sequencing. RESULTS: Intake of HBG for 4 wk suppressed the body weight, as well as liver and heart indices, and regulated the levels of fasting blood glucose, serum insulin, blood lipid, oxidative damage, and inflammatory reaction in mice with T2D. Furthermore, HBG reversed the gut microbiota dysbiosis in mice with T2D by increasing the abundance of Lachnospiraceae_UCG-006, Streptococcaceae, and Eggerthellaceae, and by decreasing the abundance of Parasutterella. CONCLUSIONS: Our findings indicate that the antidiabetic abilities of HBG might be related to the improvement of gut microbiota imbalance.


Subject(s)
Diabetes Mellitus, Type 2 , Gastrointestinal Microbiome , Hordeum , beta-Glucans , Mice , Animals , Blood Glucose , Diabetes Mellitus, Type 2/drug therapy , Streptozocin/pharmacology , Diet, High-Fat/adverse effects , beta-Glucans/pharmacology , Mice, Inbred C57BL , Hypoglycemic Agents/pharmacology , Hypoglycemic Agents/therapeutic use
5.
Medicine (Baltimore) ; 101(39): e30805, 2022 Sep 30.
Article in English | MEDLINE | ID: mdl-36181058

ABSTRACT

BACKGROUND: Anaphylactic shock is the severe state of the allergic reaction, which is rapid in onset and fatal. This is the first study that discusses the anaphylactic shock of exenatide reexposure in the patient who has interrupted exenatide treatment. PATIENT CONCERNS: A 47-year-old man was treated with exenatide owing to high blood glucose and obesity. Then he developed localized urticarial on the face, white lip, hands tremble, nausea, vomit, chest stuffiness, dizziness, accompanying with confusion and dyspnea. His blood glucose was 4.6 millimole per liter (mmol/L) and blood pressure was 85/50 millimeters of mercury (mm Hg). DIAGNOSIS: Exenatide-induced anaphylactic shock was considered. INTERVENTIONS: The emergency electrocardiogram was performed. The patient was treated with dexamethasone sodium phosphate and calcium gluconate, combined with exenatide withdrawal. He also received oral antiallergic agents and intravenous nutrition treatment. OUTCOMES: After antishock treatment, the clinical response gradually alleviated. LESSONS: Although exenatide is not prone to anaphylaxis, it is the synthetic peptide that can induce antibody formation. Exenatide has immunogenicity with the potential to elicit an allergic reaction upon administration. Clinicians should always pay more attention to the anaphylactic shock of exenatide, when prescribing for diabetics.


Subject(s)
Anaphylaxis , Anti-Allergic Agents , Mercury , Anaphylaxis/drug therapy , Anti-Allergic Agents/therapeutic use , Blood Glucose , Calcium Gluconate/therapeutic use , Exenatide/adverse effects , Humans , Male , Middle Aged
6.
J Biochem Mol Toxicol ; 33(5): e22296, 2019 May.
Article in English | MEDLINE | ID: mdl-30672062

ABSTRACT

Puerarin belongs to one of the most familiar tradition medicines of China, but adverse effects of puerarin during the clinical treatment have been found for years, the mechanisms of which remain unclear. In this study, toxic mechanisms of puerarin on the structure and function of catalase were studied by multiple spectroscopic techniques, isothermal titration calorimetric measurement, and molecular docking methods in vitro. Results showed puerarin could inhibit the activity of catalase due to direct interactions between puerarin and catalase, resulting in conformational and functional changes of the enzyme. To be specific, puerarin statically quenched catalase fluorescence, bound into the active site channel of catalase, hindered the path of the catalytic substrate (H2 O2 ), affected its skeleton conformation and secondary structure, and interacted with the enzymatically related residues through hydrophobic interactions (ΔH > 0 and ΔS > 0) spontaneously (ΔG < 0). This study illustrates potential adverse effects of puerarin, which should catch more attentions during the clinical diagnosis.


Subject(s)
Catalase/chemistry , Isoflavones/chemistry , Molecular Docking Simulation , Animals , Catalysis , Cattle , Hydrogen Peroxide/chemistry
7.
Biol Pharm Bull ; 41(7): 985-993, 2018 Jul 01.
Article in English | MEDLINE | ID: mdl-29709897

ABSTRACT

AMP-activated protein kinase (AMPK) is a metabolic sensor in mammals that is activated when ATP levels in the cell decrease. AMPK is a heterotrimeric protein that comprises 3 subunits, each of which has multiple phosphorylation sites that play critical roles in the regulation of either anabolism or catabolism by directly phosphorylating proteins or modulating gene transcription in multiple pathways, such as synthesis, oxidation and lipolysis of lipid. Research focused on the phosphorylation sites that are involved in lipid metabolism will lead to a better recognition of the role of AMPK in therapeutics for several common diseases. In this review, close attention is paid to the recent research on the structure, and multisite phosphorylation of AMPK subunits, as well as AMPK regulation of lipid metabolism via phosphorylation of related molecules.


Subject(s)
AMP-Activated Protein Kinases/metabolism , Energy Metabolism/physiology , Lipid Metabolism/physiology , Protein Subunits/metabolism , AMP-Activated Protein Kinases/chemistry , Adipose Tissue/metabolism , Animals , Humans , Liver/metabolism , Phosphorylation/physiology , Protein Multimerization/physiology , Protein Subunits/chemistry
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