Type II Diabetes

Type II Diabetes

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Type II diabetes is a heterogeneous syndrome results from the progressive defects of impairment of ß- cell insulin secretion and insulin resistant of the target tissues. It also increases due to the rising rate of obesity which involves the deficiency of insulin to compensate for insulin resistance by increasing insulin secretion [1]. However it is increasingly clear that reductions in insulin sensitivity and ß- cell functions leads to the rise of type II diabetes [2]. The normal pancreatic ß- cells displaying the remarkable response to nutrients and obesity – associated insulin resistance by the hyper secretion of insulin to maintain fuel homeostasis. But the cellular resistance unable to sustain the ß– cells compensatory response in type II diabetes [3]. Although the cause of the metabolic deterioration is unknown, but several hypothesis have been proposed including mitochondrial dysfunction, oxidative stress, ER stress, and gluco-lipotoxicity [4, 5]. Recent studies with intensive investigations suggesting that elevated glucose along with circulating free fatty acids distributed especially from the intra abdominal fat are the major culprits of insulin resistance and beta cell dysfunction [6, 7]. But the underlying molecular and cellular mechanisms of gluco-lipotoxicity contribute to ß- cell dysfunction and loss in type II diabetes remains debated. A recent observation from experimental, clinical and genetic evidence suggests endoplasmic reticulum was responsible for molecular mechanism of gluco-lipotoxicity which may contribute to ß - cell dysfunction in type II diabetes [8, 9]. In this review, we discussed about the involvement of ER in gluco-lipotoxicity induced ß- cell dysfunction along with the brief involvement of mitochondria.

ER stress response
Adaptation to metabolic changes requires the high regulation and co-ordination of many homeostatic systems, since the quality and quantity of available nutrients does not temporally match their needs. Pancreatic ß - cells displaying remarkable response to nutrients by the balance between the anabolic hormone insulin and the catabolic hormone glucagon in order to maintain fuel homeostasis. For an appropriate response, the cells require the development of suitable sensors and signaling molecules, which integrates all these signals into an appropriate insulin secretory rate in order to maintain homeostasis.

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At the same time, an increase in insulin secretion activates insulin biosynthesis in order to compensate for fluctuations in the secretory rate. The endoplasmic reticulum is an integral contributor responsible for protein synthesis, folding, maturation, quality control, trafficking, degradation and it can be an ideal site for nutrient sensor at the sub cellular level [10]. The quality control machinery in the ER operates via specialized protein and chemical environment to ensure proper folding and processing of secretory proteins including insulin due to heavy engagement in insulin synthesis to maintain glucose homeostasis, causes the more accumulation of misfolded /unfolded proteins in the ER, reduced the quality and quantity of ER [11]. To cope with this condition, cells activate an adaptive system linking the ER lumen with the cytoplasm and nucleus called the unfolded protein response (UPR). The UPR restores ER homeostasis by decreasing the protein load via increasing the expression of genes that induce protein folding capacity and promote ER associated protein degradation to remove misfolded proteins [12]. The three branches of the UPR are mediated by the ER-membrane associated proteins PERK (PKR-like ER kinase), IRE-1 (Inositol requiring enzyme 1) and ATF6 (activating transcription factor 6). In unstressed conditions, these three proteins are held by ER chaperone Bip /GRP78, in their N-terminal domains (PERK, IRE-1) and carboxyl terminal of ATF6, preventing their aggregation and rendered inactive [13]. Once activated, PERK phosphorylates serine 51 of eukaryotic translation initiation factor 2a (eif2α), unable to efficiently initiate translation, leading to global inhibition of protein synthesis at the same time induce the translation of the transcription factor ATF4. ATF4 protein translocates into the nucleus and up-regulates ER stress target genes including C/EBP homologues protein (CHOP) and downstream GADD34. The translational recovery is mediated by the GADD34, which acts as a non-enzymatic cofactor for stress induced protein phosphatase-1 leads to eif2α dephosphoylation [14, 15]. Moreover activation of ATF6 involves the dissociation of GRP78 from its luminal domain and translocate to the Golgi for proteolytic processing where it is cleaved into its active form

which translocates into the nucleus to induce ER stress response genes such as Bip [16]. Inositol-requiring enzyme 1 is a type 1 transmembrane protein with endoribonuclease activity. Activated IRE1 catalyzes the splicing of X-box-binding protein 1 mRNA leads to translation of the active transcription factor XBP1 that induces the expression of genes required for protein folding, ER to Golgi transport and ERAD [17], Figure I.

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