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Udayakumar Karunakaran  (Karunakaran U) 4 Articles
Basic Research
The Role of CD36 in Type 2 Diabetes Mellitus: β-Cell Dysfunction and Beyond
Jun Sung Moon, Udayakumar Karunakaran, Elumalai Suma, Seung Min Chung, Kyu Chang Won
Diabetes Metab J. 2020;44(2):222-233.   Published online April 23, 2020
  • 8,004 View
  • 175 Download
  • 18 Web of Science
  • 17 Crossref
AbstractAbstract PDFPubReader   

Impaired β-cell function is the key pathophysiology of type 2 diabetes mellitus, and chronic exposure of nutrient excess could lead to this tragedy. For preserving β-cell function, it is essential to understand the cause and mechanisms about the progression of β-cells failure. Glucotoxicity, lipotoxicity, and glucolipotoxicity have been suggested to be a major cause of β-cell dysfunction for decades, but not yet fully understood. Fatty acid translocase cluster determinant 36 (CD36), which is part of the free fatty acid (FFA) transporter system, has been identified in several tissues such as muscle, liver, and insulin-producing cells. Several studies have reported that induction of CD36 increases uptake of FFA in several cells, suggesting the functional interplay between glucose and FFA in terms of insulin secretion and oxidative metabolism. However, we do not currently know the regulating mechanism and physiological role of CD36 on glucolipotoxicity in pancreatic β-cells. Also, the downstream and upstream targets of CD36 related signaling have not been defined. In the present review, we will focus on the expression and function of CD36 related signaling in the pancreatic β-cells in response to hyperglycemia and hyperlipidemia (ceramide) along with the clinical studies on the association between CD36 and metabolic disorders.


Citations to this article as recorded by  
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    Clinical Immunology.2024; 260: 109914.     CrossRef
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    Medicine.2024; 103(18): e37933.     CrossRef
  • The association of soluble cluster of differentiation 36 with metabolic diseases: A potential biomarker and therapeutic target
    Yun Li, Yaxi Chen, Xiong Z. Ruan
    Pediatric Discovery.2023;[Epub]     CrossRef
  • The role of candidate transport proteins in β‐cell long‐chain fatty acid uptake: Where are we now?
    Christina Clavelo‐Farrow, Patricia Thomas
    Diabetic Medicine.2023;[Epub]     CrossRef
  • SARS-CoV-2 in the pancreas and the impaired islet function in COVID-19 patients
    Ningfei Ji, Mingshun Zhang, Liang Ren, Yunyun Wang, Bicheng Hu, Jie Xiang, Yingyun Gong, Chaojie Wu, Guoqiang Qu, Wenqiu Ding, Zhiqiang Yin, Shan Li, Zhengxia Wang, Lianzheng Zhou, Xueqin Chen, Yuan Ma, Jinhai Tang, Yun Liu, Liang Liu, Mao Huang
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  • Is imaging-based muscle quantity associated with risk of diabetes? A meta-analysis of cohort studies
    Shanhu Qiu, Xue Cai, Yang Yuan, Bo Xie, Zilin Sun, Tongzhi Wu
    Diabetes Research and Clinical Practice.2022; 189: 109939.     CrossRef
  • Lipotoxicity in a Vicious Cycle of Pancreatic Beta Cell Exhaustion
    Vladimir Grubelnik, Jan Zmazek, Matej Završnik, Marko Marhl
    Biomedicines.2022; 10(7): 1627.     CrossRef
  • Association of cluster determinant 36, scavenger receptor class B type 1, and major facilitator superfamily domain containing the 2a genetic polymorphism with serum lipid profile in aging population with type 2 diabetes mellitus
    Xixiang Wang, Xiaojun Ma, Jingjing Xu, Yujie Guo, Shaobo Zhou, Huiyan Yu, Linhong Yuan
    Frontiers in Nutrition.2022;[Epub]     CrossRef
  • CD36-Fatty Acid-Mediated Metastasis via the Bidirectional Interactions of Cancer Cells and Macrophages
    Noorzaileen Eileena Zaidi, Nur Aima Hafiza Shazali, Thean-Chor Leow, Mohd Azuraidi Osman, Kamariah Ibrahim, Wan-Hee Cheng, Kok-Song Lai, Nik Mohd Afizan Nik Abd Rahman
    Cells.2022; 11(22): 3556.     CrossRef
  • The Past and Present Lives of the Intraocular Transmembrane Protein CD36
    Rucui Yang, Qingping Liu, Mingzhi Zhang
    Cells.2022; 12(1): 171.     CrossRef
  • Implicating the effect of ketogenic diet as a preventive measure to obesity and diabetes mellitus
    Sachin Kumar, Tapan Behl, Monika Sachdeva, Aayush Sehgal, Shilpa Kumari, Arun Kumar, Gagandeep Kaur, Harlokesh Narayan Yadav, Simona Bungau
    Life Sciences.2021; 264: 118661.     CrossRef
  • Contribution of rs3211938 polymorphism at CD36 to glucose levels, oxidized low-density lipoproteins, insulin resistance, and body mass index in Mexican mestizos with type-2 diabetes from western Mexico
    Beatriz Teresita Martín-Márquez, Flavio Sandoval-Garcia, Mónica Vazquez-Del Mercado, Erika-Aurora Martínez-García, Fernanda-Isadora Corona-Meraz, Ana-Lilia Fletes-Rayas, Soraya-Amalí Zavaleta-Muñiz
    Nutrición Hospitalaria.2021;[Epub]     CrossRef
  • Investigating the association of CD36 gene polymorphisms (rs1761667 and rs1527483) with T2DM and dyslipidemia: Statistical analysis, machine learning based prediction, and meta-analysis
    Ma’mon M. Hatmal, Walhan Alshaer, Ismail S. Mahmoud, Mohammad A. I. Al-Hatamleh, Hamzeh J. Al-Ameer, Omar Abuyaman, Malek Zihlif, Rohimah Mohamud, Mais Darras, Mohammad Al Shhab, Rand Abu-Raideh, Hilweh Ismail, Ali Al-Hamadi, Ali Abdelhay, Kanhaiya Singh
    PLOS ONE.2021; 16(10): e0257857.     CrossRef
  • Misregulation of Wnt Signaling Pathways at the Plasma Membrane in Brain and Metabolic Diseases
    Mustafa Karabicici, Yagmur Azbazdar, Evin Iscan, Gunes Ozhan
    Membranes.2021; 11(11): 844.     CrossRef
  • CD36 Signal Transduction in Metabolic Diseases: Novel Insights and Therapeutic Targeting
    Udayakumar Karunakaran, Suma Elumalai, Jun-Sung Moon, Kyu-Chang Won
    Cells.2021; 10(7): 1833.     CrossRef
Islet Studies and Transplantation
Myricetin Protects Against High Glucose-Induced β-Cell Apoptosis by Attenuating Endoplasmic Reticulum Stress via Inactivation of Cyclin-Dependent Kinase 5
Udayakumar Karunakaran, Suma Elumalai, Jun Sung Moon, Jae-Han Jeon, Nam Doo Kim, Keun-Gyu Park, Kyu Chang Won, Jaechan Leem, In-Kyu Lee
Diabetes Metab J. 2019;43(2):192-205.   Published online January 16, 2019
  • 5,368 View
  • 111 Download
  • 36 Web of Science
  • 37 Crossref
AbstractAbstract PDFSupplementary MaterialPubReader   

Chronic hyperglycemia has deleterious effects on pancreatic β-cell function and turnover. Recent studies support the view that cyclin-dependent kinase 5 (CDK5) plays a role in β-cell failure under hyperglycemic conditions. However, little is known about how CDK5 impair β-cell function. Myricetin, a natural flavonoid, has therapeutic potential for the treatment of type 2 diabetes mellitus. In this study, we examined the effect of myricetin on high glucose (HG)-induced β-cell apoptosis and explored the relationship between myricetin and CDK5.


To address this question, we subjected INS-1 cells and isolated rat islets to HG conditions (30 mM) in the presence or absence of myricetin. Docking studies were conducted to validate the interaction between myricetin and CDK5. Gene expression and protein levels of endoplasmic reticulum (ER) stress markers were measured by real-time reverse transcription polymerase chain reaction and Western blot analysis.


Activation of CDK5 in response to HG coupled with the induction of ER stress via the down regulation of sarcoendoplasmic reticulum calcium ATPase 2b (SERCA2b) gene expression and reduced the nuclear accumulation of pancreatic duodenal homeobox 1 (PDX1) leads to β-cell apoptosis. Docking study predicts that myricetin inhibit CDK5 activation by direct binding in the ATP-binding pocket. Myricetin counteracted the decrease in the levels of PDX1 and SERCA2b by HG. Moreover, myricetin attenuated HG-induced apoptosis in INS-1 cells and rat islets and reduce the mitochondrial dysfunction by decreasing reactive oxygen species production and mitochondrial membrane potential (Δψm) loss.


Myricetin protects the β-cells against HG-induced apoptosis by inhibiting ER stress, possibly through inactivation of CDK5 and consequent upregulation of PDX1 and SERCA2b.


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  • Mitochondrial aldehyde dehydrogenase-2 coordinates the hydrogen sulfide - AMPK axis to attenuate high glucose-induced pancreatic β-cell dysfunction by glutathione antioxidant system
    Udayakumar Karunakaran, Suma Elumalai, Seung Min Chung, Kathrin Maedler, Kyu Chang Won, Jun Sung Moon
    Redox Biology.2024; 69: 102994.     CrossRef
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A Systematic Review of Oxidative Stress and Safety of Antioxidants in Diabetes: Focus on Islets and Their Defense
Udayakumar Karunakaran, Keun-Gyu Park
Diabetes Metab J. 2013;37(2):106-112.   Published online April 16, 2013
  • 5,560 View
  • 77 Download
  • 134 Crossref
AbstractAbstract PDFPubReader   

A growing body of evidence suggests that hyperglycemia-induced oxidative stress plays an important role in diabetic complications, especially β-cell dysfunction and failure. Under physiological conditions, reactive oxygen species serve as second messengers that facilitate signal transduction and gene expression in pancreatic β-cells. However, under pathological conditions, an imbalance in redox homeostasis leads to aberrant tissue damage and β-cell death due to a lack of antioxidant defense systems. Taking into account the vulnerability of islets to oxidative damage, induction of endogenous antioxidant enzymes or exogenous antioxidant administration has been proposed as a way to protect β-cells against diabetic insults. Here, we consider recent insights into how the redox response becomes deregulated under diabetic conditions, as well as the therapeutic benefits of antioxidants, which may provide clues for developing strategies aimed at the treatment or prevention of diabetes associated with β-cell failure.


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O-GlcNAc Modification: Friend or Foe in Diabetic Cardiovascular Disease
Udayakumar Karunakaran, Nam Ho Jeoung
Korean Diabetes J. 2010;34(4):211-219.   Published online August 31, 2010
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AbstractAbstract PDFPubReader   

O-Linked β-N-acetyl glucosaminylation (O-GlcNAcylation) is a dynamic post-translational modification that occurs on serine and threonine residues of cytosolic and nuclear proteins in all cell types, including those involved in the cardiovascular system. O-GlcNAcylation is thought to act in a manner analogous to protein phosphorylation. O-GlcNAcylation rapidly cycles on/off proteins in a time scale similar to that for phosphorylation/dephosphorylation of proteins. Several studies indicate that O-GlcNAc might induce nuclear localization of some transcription factors and may affect their DNA binding activities. However, at the cellular level, it has been shown that O-GlcNAc levels increase in response to stress and augmentation of this response suppresses cell survival. Increased levels of O-GlcNAc have been implicated as a pathogenic contributor to glucose toxicity and insulin resistance, which are major hallmarks of type 2 diabetes and diabetes-related cardiovascular complications. Thus, O-GlcNAc and its metabolic functions are not yet well-understood; focusing on the role of O-GlcNAc in the cardiovascular system is a viable target for biomedical investigation. In this review, we summarize our current understanding of the role of O-GlcNAc on the regulation of cell function and survival in the cardiovascular system.


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