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Kuribara, T. Oligomannose-Type Glycan Processing in Diseases. Encyclopedia. Available online: https://encyclopedia.pub/entry/20527 (accessed on 19 April 2025).
Kuribara T. Oligomannose-Type Glycan Processing in Diseases. Encyclopedia. Available at: https://encyclopedia.pub/entry/20527. Accessed April 19, 2025.
Kuribara, Taiki. "Oligomannose-Type Glycan Processing in Diseases" Encyclopedia, https://encyclopedia.pub/entry/20527 (accessed April 19, 2025).
Kuribara, T. (2022, March 14). Oligomannose-Type Glycan Processing in Diseases. In Encyclopedia. https://encyclopedia.pub/entry/20527
Kuribara, Taiki. "Oligomannose-Type Glycan Processing in Diseases." Encyclopedia. Web. 14 March, 2022.
Oligomannose-Type Glycan Processing in Diseases
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This entry is adapted from the peer-reviewed paper 10.3390/biology11020199

Glycoprotein folding plays a critical role in sorting glycoprotein secretion and degradation in the endoplasmic reticulum (ER). Furthermore, relationships between glycoprotein folding and several diseases, such as type 2 diabetes and various neurodegenerative disorders, are indicated. Patients’ cells with type 2 diabetes, and various neurodegenerative disorders induce ER stress, against which the cells utilize the unfolded protein response for protection. However, in some cases, chronic and/or massive ER stress causes critical damage to cells, leading to the onset of ER stress-related diseases, which are categorized into misfolding diseases. Accumulation of misfolded proteins may be a cause of ER stress, in this respect, perturbation of oligomannose-type glycan processing in the ER may occur. A great number of studies indicate the relationships between ER stress and misfolding diseases, while little evidence has been reported on the connection between oligomannose-type glycan processing and misfolding diseases. Alteration of oligomannose-type glycan processing in several ER stress-related diseases were summarized, especially misfolding diseases and show the possibility of these alteration of oligomannose-type glycan processing as indicators of diseases.

glycan processing glycoprotein ERQC diseases

1. Introduction

Glycans play critical roles in mammals [1] and are categorized as O- and N-linked glycans. Specifically, they function as a major signal of biological processes, such as cell–cell interaction, viral infection, protein folding of glycoprotein [2]. Among these, the N-glycan-mediated glycoprotein folding mechanism in the endoplasmic reticulum (ER) is critical for proper glycoprotein folding and functioning in the desired cellular compartment. However, misfolded glycoproteins should be degraded to maintain cellular homeostasis, because the accumulation of misfolded glycoproteins in the ER causes stress to cells, namely ER stress. Therefore, cells have a quality control system named ER glycoprotein quality control (glycoprotein ERQC) [3][4][5][6].
This system enables the secretion of folded glycoprotein to the Golgi apparatus and the removal of misfolded glycoproteins from the ER to the cytosol for degradation. In this system, the glycan attached on proteins is an intriguing molecule in various aspects. First, N-glycans, especially oligomannose-type glycans, on protein scaffolds act as sorting signals for glycoprotein secretion and degradation. Thus, these oligomannose-type glycans may reflect information about protein scaffold-folding states. Second, the operating status of oligomannose-type glycan processing in the ER may reflect various cellular conditions, such as diseases caused by accumulation of (glyco)proteins in the ER. 

2. Endoplasmic Reticulum Stress and Misfolding Diseases

Accumulation of misfolded (glyco)proteins causes ER stress. Therefore, cells have a protective mechanism, called UPR, for accumulated misfolded non-glycoproteins and glycoproteins. UPR is a major mechanism for maintaining ER homeostasis and has already identified three main pathways [7]. In brief, translation of mRNA is suppressed by activating the protein kinase RNA-like ER kinase (PERK) pathway. Activating PERK leads to the phosphorylation of eukaryotic translation initiation factor-2α, which inhibits binding of preinitiation complex to the cap structure of mRNAs, resulting in the suppression of protein translation. Furthermore, the up-regulation of certain genes such as activating transcription factor 4 induces an antioxidant response and promotes protein folding capacity. The stimulation of the activating transcription factor 6 (ATF6) pathway and the up-regulation of ER chaperones induce increased folding capacity and accelerate protein folding in the ER. The inositol-requiring protein 1 α (IRE1) pathway, which is responsible for up-regulating protein folding-related proteins, ER-associated degradation (ERAD)-related proteins, and lipid biosynthesis-related proteins, is activated after the ATF6 pathway to refold and/or remove misfolded glycoproteins [8]. However, chronic or massive ER stress causes severe conditions that make the cells no longer survive. Therefore, these cells are cleared from tissues by activating apoptosis signals. The UPR is widely activated in several diseases, such as type 2 diabetes and a series of neurodegenerative disorders [Alzheimer’s disease (AD), Parkinson’s disease (PD), Huntington’s disease (HD), amyotrophic lateral sclerosis (ALS) and prion diseases]. Several classifications of ER stress-related diseases, including above-mentioned diseases, have reported [9]. For instance, genetic disorders and neurodegenerative disorders are mainly caused by loss of function or misfolding of mutant proteins. Environmental or lifestyle insults such as an excess of nutrients or inflammation induce ER stress, and these are causative to neurodegenerative disorders and metabolic and inflammatory diseases. In particular, accumulation of etiological proteins by genetic mutation or misfolding is categorized into misfolding diseases. The common features are misfolding of (glyco)proteins and forming toxic aggregates that induce ER stress in the original tissue, while disease-associated proteins are quite different. Furthermore, activating UPR pathways vary depending on the disease. In this section, among various misfolding diseases reported,  resesarchers focused on age-related diseases because the world is shifting to an ageing society, and improvement of patients’ quality of life is an urgent need. The most familiar age-related diseases are type 2 diabetes and neurodegenerative disorders, and   discuss these misfolding diseases.

2.1. Type 2 Diabetes

Obesity exacerbates obese type 2 diabetes. Indeed, in high-fat diet-induced genetic (ob/ob) mouse models, obesity causes ER stress and it is considered that obesity contributes to the development of obese type 2 diabetes [10]. ER stress is predominantly induced in liver and adipose tissues and inhibits insulin action in liver cells, which was revealed. This indicates that ER stress leads to the development of insulin resistance and is one of the progression factors to obese type 2 diabetes.
In addition to liver tissue, type 2 diabetes is well characterised in pancreatic β-cells. Major features are dysfunction of β-cells and loss of β-cells mass [11]. These may be explained by various stresses, including ER stress in the β-cells. Islet amyloid polypeptides (IAPP) in β-cells may induce cell toxicity, resulting in ER stress mediating one of the factors for β-cell apoptosis [12]. This may result in impaired insulin release and hyperglycaemia, developing type 2 diabetes. Huang et al., reported that IAPP induces CHOP, which is one of the apoptosis mediators in the PERK pathway [13]. Although CHOP is not the only mediator for apoptosis of the β-cells, these results indicate the relationships between IAPP and ER stress and that IAPP may be one of the associated proteins of type 2 diabetes. Proinsulin is another possibility of associated proteins in type 2 diabetes. Indeed, proinsulin misfolding is observed in an early event in the progression to type 2 diabetes [14]. Interestingly, it is characterised by olanzapine, a second-generation antipsychotic, which causes adverse side effects, including diabetes. A recent study demonstrated that olanzapine-induced diabetes is caused by olanzapine-induced proinsulin misfolding in β-cells [15]. Furthermore, these studies also suggest that the PERK pathway is activated in β-cells. Altogether, IAPP and proinsulin may contribute to type 2 diabetes by activating the PERK pathway, and these studies highlight protein misfolding involved in type 2 diabetes.

2.2. Neurodegenerative Disorders

In neurodegenerative disorders, such as AD, PD, HD, ALS and prion protein disease, several misfolded proteins are observed, such as neurotoxic oligomers of the amyloid β-peptides (Aβ) and Tau in AD, α-synuclein in PD, a polyglutamine (polyQ) extended huntingtin in HD, superoxide dismutase (SOD1), Tar-DNA binding protein (TDP-43) and fused in sarcoma (FUS) in ALS, and prion protein (PrP) in prion diseases. Although the roles of these proteins in neurodegeneration are diverse, ER stress is induced in all diseases. In this section, researchers partially introduce the relationships between disease-associated proteins and ER stress from excellent reviews, in which more details of the pathological mechanism of each neurodegenerative disorder have been described [16][17][18][19][20]

Alzheimer’s Diseases (AD)

In AD [16], it is characterized as an indirect Aβ contribution for ER stress, because interaction with cytosolic oligomers of Aβ and neuronal N-methyl-D-aspartate receptors can disrupt cytosolic calcium balance and after cell signalling, leading to ER stress-dependent cell death [21]. Furthermore, in the case of rare familial AD forms, Aβ accumulation in ER was observed, indicating that Aβ may directly contribute to ER stress induction [22]. In contrast to Aβ, soluble Tau in cytosol inhibit ERAD activity, triggering accumulation of misfolded proteins and causing ER stress [23]. Therefore, in AD, Aβ and Tau contribute to evoking UPR pathways. Although all UPR pathway activations have been known, PERK and IRE1 pathways are well characterized. For instance, the PERK pathway first induces protein translation inhibition and the activation increases the expression of β-amyloid precursor protein cleaving enzyme 1 (BACE1), leading Aβ production [24]. Sustained PERK signalling may cause neuronal loss through apoptosis signals [16], thus the PERK pathway may have a time-dependent response for AD progression. Furthermore, spliced X-box binding protein 1 (XBP1), a major signal transducer in the IRE1 pathway, increases the degradation rate of key AD proteins such as BACE1 and phosphorylated tau. However, sustained IRE1 signalling might induce pro-apoptotic activity by regulated IRE1-dependent decay rather than XBP1s expression. Interestingly, Gerakis et al., proposed connections between UPR and Alzheimer’s disease lesions; they indicated that protein aggregation and accumulation is the first step in Alzheimer’s disease [16]. Thus, the operating status of glycoprotein ERQC may also alter by changing the expression level of ERQC components in an early stage of Alzheimer’s disease.

Parkinson’s Disease (PD)

In PD [17], Overexpression of human α-synuclein and its A53T mutant exhibit toxicity and cause ER stress [25][26]. Although α-synuclein is not an ER-resident protein, α-synuclein-mediated ER stress may be caused either directly or indirectly through several cell signalling pathways [17]. To summarize, toxic α-synuclein can bind synaptic vesicles and biological membranes, including ER, thus affecting intracellular protein trafficking [27][28][29]. Then, toxic α-synuclein and/or its aggregates may induce ER stress. Among all UPR pathways, the PERK pathway may contribute to neurodegeneration. For instance, an overexpressed A53T mutant of α-synuclein in PC12 cells causes the phosphorylation of eukaryotic translation initiation factor-2α and induces CHOP expression, which indicates that the PERK pathway was activated [25]. Furthermore, inhibition of XBP1 protein expression in mice induced chronic ER stress and neurodegeneration, while recovery of XBP1 level by gene therapy protected neuronal cells [30]. Thus, the IRE1 pathway plays a critical role in neuronal survival. Furthermore, ATF6 knockdown in mice exacerbated neurotoxicity after treatment with dopaminergic neurotoxin [31]. These results speculate about the expression alteration of ERQC components; however, scant evidence is reported.

Huntington’s Disease (HD)

In HD [18], patients have a mutation of huntingtin then HD is a genetic disorder. The mutant has polyQ [32] and is prone to misfolding and aggregation in the cytosol. This mutant huntingtin or the aggregate accumulate, leading to ERAD inhibition [33][34]. Interestingly, several studies showed that oligomers of mutant huntingtin are more cytotoxic than their aggregate forms [34][35]. Furthermore, ERAD substrate accumulation was observed and all three pathways of UPR were activated. In addition, activation of the IRE1 pathway was reported in vivo [36]. These results suggest that ERAD inhibition by toxic huntingtin oligomers induces ER stress and the activation of UPR. Furthermore, in the ER stress condition, increased expression of protein disulfide isomerases (PDIs), an important protein for protein folding in the ER, was reported [18][33]. This may indicate at least that the activity of PDIs involved in (glyco)protein folding in the ER is altered in HD.

Amyotrophic Lateral Sclerosis (ALS)

In ALS [19], several proteins have characterized ALS-associated proteins, such as SOD1, TDP-43 and FUS. The mutants of these three proteins are prone to misfolding and aggregation, inducing ER stress. For instance, mutant SOD1 interacts with Derlin-1, which is important for ERAD, inducing ER stress [37]. Similar to SOD1, mutant TDP-43 and FUS activate UPR from the cytosol. CHOP induction was observed and this implicates the activation of the PERK pathway, leading to apoptosis in neuronal cells expressing mutant SOD1 [38]. Interestingly, XBP-1 deficiency can delay ALS disease onset in mutant SOD1 mice by increasing autophagy [39]. This indicates IRE1 pathway can provide a protective effect for ALS. In the case of TDP-43, overexpression of wild-type and mutant TDP-43 induced ER stress by activating XBP-1 and ATF6 pathways [40]. Furthermore, cytosolic FUS induced ER stress and colocalized with PDI [41]. Interestingly, reducing CRT levels in G93A mutant SOD1 mice triggered muscle denervation and motor neuron degeneration in mice [42][43]. These results may indicate that the altered expression of glycoprotein ERQC component in ALS is plausible.

Prion Diseases

In prion diseases [20], PrP is prone to misfolding by abnormal folding because the α-helix rich form of PrP that is frequently observed in normal cellular conditions converts into misfolding prone β-sheet conformation [20]. The conformational changes alter its properties such as solubility and resistance to proteases. Thus, the accumulation of abnormal conformation of PrPs might be associated with ER stress. Hetz et al., reported that highly purified abnormal conformations of PrPs induce ER stress and apoptosis in vitro [44]. The PERK pathway was activated in the hippocampi of PrP-infected and overexpressing mice [45]. In the mouse model, PrP accumulation activated the PERK pathway and resulted in neurodegeneration [45]. Furthermore, PERK pathway inhibition by several pharmacological inhibitors provides neuroprotective activity [46][47]. These studies indicate the importance of the PERK pathway in prion diseases. Additionally, the dominant negative form of IRE1 or XBP1 significantly increased PrP aggregation, while the active mutant form of XBP1 and ATF6 had the opposite effect [48]. These results suggest that all UPR pathways are activated in prion diseases. Furthermore, Yedidia et al., reported approximately 10% of normal conformation of PrP is intrinsically misfolded and degraded by the ERAD pathway [49]. This may imply that PrP itself is involved in the perturbation of glycoprotein ERQC.
Collectively, relationships between ER stress and ER stress-related diseases—especially misfolding diseases—have been demonstrated in a large body of studies. Among them, the involvement of UPR pathways in type 2 diabetes and neurodegenerative diseases is partially demonstrated. In these diseases, toxic proteins lead to misfolding of proteins in the ER, inducing ER stress. Accumulating misfolded proteins activates all three UPR pathways, and may lead to changing expression levels of glycoprotein ERQC components. As described above, although some circumstantial evidence for this possibility has been reported [25][30][33][41][42][43][49], no direct connections between misfolding diseases and glycoprotein ERQC have been reported. Considering these, altered oligomannose-type glycan processing in glycoprotein ERQC might occur; however, this is not well understood.

3. Oligomannose-Type Glycan Processing and Misfolding Disease

In this section, researchers demonstrate whether the alteration in glycan processing in the ER can reflect disease states, such as type 2 diabetes and neurodegenerative disorders. In this respect, a comparison of precise glycan-processing states from healthy and disease samples is needed. Overall, a comparison of glycan-processing analysis is conducted in serum or total cellular proteins. However, at least oligomannose-type glycans mainly exist in ER. Furthermore, they are common intermediates in secretory glycoprotein’s glycan. Therefore, perturbation of oligomannose-type glycans may occur in patients’ ER at the early stage of diseases. However, oligomannose-type glycans convert to several types of other N-glycans in Golgi apparatus (complex- and hybrid-type N-glycans), alteration of oligomannose-type glycans in patients’ samples is often overlooked. To precisely analyse the glycans in ER, total glycan-processing analysis (glycan profiles) using isolated ER is most suitable because isolated ER can reflect the exact glycan profiles in the ER. For this reason, researchers previously tried acquiring glycan profiles in isolated ER from animal model tissues of misfolding disease model. However, the total glycan profiles from isolated ER were not different from healthy controls [50]. This suggests that the direct glycan profile cannot reflect the nature of ER glycan profile, because the recycling of glycoproteins between ER- and Golgi apparatus may mask differences of perturbation of glycan profiles in disease sample.
To overcome this problem, researchers established a novel glycan-processing analysis system named the reconstructed glycan profile method [50]. The method has three main features: (1) ER fraction is derived from model animals as enzymatic reaction sources, (2) synthetic fluorescent-labelled glycan substrates is used to substrates [51], and (3) high-performance liquid chromatography for facilitating separation of various oligomannose-type glycans. With the ER fraction and the synthetic glycan substrates, researchers analysed in vitro operating status of glycan processing at various reaction times. If the alteration of the glycan profiles from healthy to disease-affected is observed, the differences will indicate the feature of diseases. Indeed, the non-obese type 2 diabetes model rat, Goto-Kakizaki rat, osteoporosis and dementia (one of the neurodegenerative disorders) model mouse clearly showed the differences in glycan profiles. Moreover, the study investigated the protein expression of the ER obtained from these disease model animals and the expression of some glycan processing-related proteins altered. Although the relationship between disease manifestation and the alteration of glycan processing in the ER is unclear at this stage, perturbation of glycoprotein ERQC obviously occurs in these diseases.

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Subjects: Biochemistry & Molecular Biology
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Taiki Kuribara
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