Activity of Caprine CSN1S2 Protein Reducing the COX-2 and IL-17 Expression of Aorta Tissue in Type 2 Diabetes Mellitus Rat

Rachmad, Yoga Tribakti; Wihastuti, Titin Andri; Miyajima, Katsuhiro; Fatchiyah, Fatchiyah

doi:10.5614/j.math.fund.sci.2018.50.3.8

Cited by 3 publications

(3 citation statements)

References 29 publications

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“…Systematical effect with potential to progression of PG and correlated with imbalance in the peripheral nerves. In another result also shown that COX-2 gene inactivation protects against diabetes-induced damage in some targeted tissue (Rachmad et al, 2018).…”

Section: Resultsmentioning

confidence: 87%

“…The chlorogenic acid has an affinity with the activator side of COX-2 in amino acid residues, which bind with a hydrogen bond. The inflammation pathway was role by COX-2 such as PI3K, NF-κβ, and Akt was blocked when chlorogenic acid deactivated COX-2 by interaction on (active side domain of COX-2) (Rachmad et al, 2018). COX-2 is a central enzyme in the biosynthesis of prostaglandins.…”

Section: Resultsmentioning

confidence: 99%

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In Silico Insight the Prediction of Chlorogenic Acid in Coffee through Cyclooxygenase-2 (COX2) Interaction

Bare¹,

Sari

Rachmad³

et al. 2019

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Inflammation was signs of pathological or abnormality in tissue to give an alert as a trouble signal to the system. Therapeutic using NSAIDs has some side effects. This research explored the potential role of chlorogenic acid as natural therapeutic compound to inhibit the inflammation target such as COX-2 by interaction model. The research method used in this study was the molecular docking approach, which binds ligand and protein. Protein data provided by Protein Data Bank (ID: 6cox) while, chlorogenic acid obtain from PubChem (CID: 1794427). We docked COX-2 and chlorogenic acid using Hex 8.0.0. Visualization and analysis of the molecular interactions of chlorogenic acid and COX-2 conducted by the Discovery Studio Client 4.1 software. Chlorogenic acid has a high permeability and is easily absorbed based on five Lipinski Rule. Interestingly, we found Fifteen amino acid was binding with chlorogenic acid that formed by hydrogen bond and van der Waals.The interaction between ligand-protein results in energy binding -327.59cal/mol. Chlorogenic acid has a potential role to inhibit inflammation pathway by inhibiting COX-2. We predicted chlorogenic acid has a potential as therapy anti-inflammatory to suppress COX-2 as mediator inflammation.

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Section: Resultsmentioning

confidence: 87%

Section: Resultsmentioning

confidence: 99%

In Silico Insight the Prediction of Chlorogenic Acid in Coffee through Cyclooxygenase-2 (COX2) Interaction

Bare¹,

Sari

Rachmad³

et al. 2019

bio

Self Cite

View full text Add to dashboard Cite

show abstract

“…Interaction ligand and protein had the energy binding of -210.23cal/mol (Table 2). In our previous study, showed that effect of therapeutic nutrition against inflammation has a negative effect on COX-2 activity [22]. COX-2 blocking has a serious effect on tissue improvement.…”

Section: Resultsmentioning

confidence: 94%

The potential role of caffeic acid in coffee as cyclooxygenase-2 (COX-2) inhibitor: in silico study

2019

Biointerface Res Appl Chem

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Caffeic acid was formed from hydrolyzation chlorogenic acid caused roasting coffee. Caffeic acid has anti-inflammatory properties by in vitro and in vivo analysis. Inflammation is the body will be activator COX-2 as mediator inflammation. This study purpose to prediction, investigate and analyze caffeic acid as potential theuraphic to inhibit COX-2 by in silico study. The method of this research using in silico compound interaction models. COX-2 Protein data was taken from Protein Data Bank, caffeic acid from PubChem. Protein-ligand interaction docking using HEX 8.0.0. Although visualization and analysis of the molecular interactions of caffeic acid and COX-2 conducted by the Discovery Studio software 4.1. Caffeic acid is a potential therapist because easily absorbed and has high permeability. The results show that interacted between COX-2 and caffeic acid. The interactions showed by seven amino acid residues, which bind with the caffeic acid with hydrogen bond type. Energy binding formed from ligand and protein -210.23cal/mol. Interaction caffeic acid and COX-2 has a positive impact which potential as inhibitor COX-2.

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A Study of Kir6.2 Gene Sequence in Rat Model of Type 2 Diabetes Mellitus Treated by CSN1S2 Protein of Etawah Crossbred Goat Milk

Meidinna

Fatchiyah

2019

IOP Conf. Ser.: Mater. Sci. Eng.

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Type 2 diabetes mellitus (T2DM) is a metabolic disease characterized by hyperglycemia. High blood glucose levels in T2DM patients are treated by sulfonylurea. However, the long-term use of sulfonylurea can affect the regulation of glucose homeostasis and cause hypoglycemia. The cascade gene associated with the hypoglycemia is Kir6.2, a constituent of ATP-sensitive potassium channel (KATP), in the neuron. Kir6.2 mutations cause dysregulation of insulin secretion by pancreatic beta cells and glucagon secretion by pancreatic alpha cells. The aim of this study was to analyze the effect of CSN1S2 protein of etawah crossbred goat milk on Kir6.2 gene sequences in the rat model of T2DM. The experimental animals used were male Wistar rats (Rattus norvegicus) which were divided into two major groups, namely control group and T2DM group. Each group was administrated by CSN1S2 protein with the dose of 375 mg/kg BW, 750 mg/kg BW, 1500 mg/kg BW, and without CSN1S2 protein administration. Each group was replicated three times. DNA was isolated from the rat brain. Kir6.2 gene was amplified by using specific primers. PCR products were purified and sequenced by using ABI 3730xl DNA Sequencer. DNA sequences were analyzed by using MEGA7 software. Amplification of the Kir6.2 gene produced 1173 bp DNA. There was no change in the Kir6.2 sequence in all treatments. The 25 mg/kg BW dose of streptozotocin had no effect on Kir6.2 gene sequence in the rat brain. This study also showed that administration of CSN1S2 protein at the dose of 375 mg/kg BB, 750 mg/kg BW, and 1500 mg/kg BW did not cause mutations in the Kir6.2 gene in the brain of the rat model of T2DM.

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Activity of Caprine CSN1S2 Protein Reducing the COX-2 and IL-17 Expression of Aorta Tissue in Type 2 Diabetes Mellitus Rat

Cited by 3 publications

References 29 publications

In Silico Insight the Prediction of Chlorogenic Acid in Coffee through Cyclooxygenase-2 (COX2) Interaction

In Silico Insight the Prediction of Chlorogenic Acid in Coffee through Cyclooxygenase-2 (COX2) Interaction

The potential role of caffeic acid in coffee as cyclooxygenase-2 (COX-2) inhibitor: in silico study

A Study of Kir6.2 Gene Sequence in Rat Model of Type 2 Diabetes Mellitus Treated by CSN1S2 Protein of Etawah Crossbred Goat Milk

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