Selenoprotein S: a therapeutic target for diabetes and macroangiopathy?

Shan-Shan Yu, Jian-Ling Du, Shan-Shan Yu, Jian-Ling Du

Abstract

Inflammatory response, oxidative stress, and endoplasmic reticulum (ER) stress are important pathophysiological bases of the occurrence and development of diabetes mellitus (DM) and macroangiopathy complications. Selenoprotein S (SELENOS) is involved in the regulation of these mechanisms; therefore, its association with DM and macroangiopathy has gradually received attention from scholars worldwide. SELENOS has different biological functions in different tissues and organs: it exerts antioxidant protection and has anti-ER stress effects in the pancreas and blood vessels, while it promotes the occurrence and development of insulin resistance in the liver, adipose tissue, and skeletal muscle. In addition, studies have confirmed that some SELENOS gene polymorphisms can influence the inflammatory response and are closely associated with the risk for developing DM and macroangiopathy. Therefore, comprehensive understanding of the association between SELENOS and inflammation, oxidative stress, and ER stress may better elucidate and supplement the pathogenic mechanisms of DM and macroangiopathy complications. Furthermore, in-depth investigation of the association of SELENOS function in different tissues and organs with DM and macroangiopathy may facilitate the development of new strategies for the prevention and treatment of DM and macrovascular complications. Here, we summarize the consensus and controversy regarding functions of SELENOS on currently available evidence.

Keywords: Atherosclerosis; Cardiovascular diseases; Diabetes mellitus; Selenoprotein S; Single nucleotide polymorphism.

Figures

Fig. 1
Fig. 1
Schematic of the encoding of SELENOS mRNA variants and protein isoforms. The human SELENOS gene encodes two transcripts: variant 1 mRNA and variant 2 mRNA. They differ in a splicing event that removes a portion of the 3′UTR sequence containing a SECIS element from variant 1. The SECIS element is necessary to recode the 188UGA stop codon in the CDS of the SELENOS mRNA sequence to a selenocysteine. As a result, two SELENOS protein isoforms are expressed: the 187-aa isoform 1 from variant 1 and the 189-aa isoform 2 from variant 2. UTR untranslated region, CDS coding domain sequence, SECIS selenocysteine insertion sequence, Gly glycine, Sec selenocysteine
Fig. 2
Fig. 2
Effects of SELENOS expressed in different tissues and organs on glucose metabolism and macroangiopathy. HOMA-IR homeostasis model assessment of insulin resistance, SAA serum amyloid A, ER endoplasmic reticulum, FPG fasting plasma glucose

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Source: PubMed

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