Sheep Islet amyloid polypeptide,IAPP ELISA Kit
- Known as:
- Sheep Islet amyloid multipeptide,IAPP Enzyme-linked immunosorbent assay test Kit
- Catalog number:
- E0009Sh
- Product Quantity:
- 96T
- Category:
- Elisa Kits
- Supplier:
- JING
- Gene target:
- Sheep Islet amyloid polypeptide IAPP ELISA Kit
Related genes to: Sheep Islet amyloid polypeptide,IAPP ELISA Kit
- Gene:
- IAPP NIH gene
- Name:
- islet amyloid polypeptide
- Previous symbol:
- -
- Synonyms:
- AMYLIN, DAP, IAP
- Chromosome:
- 12p12.1
- Locus Type:
- gene with protein product
- Date approved:
- 1989-05-24
- Date modifiied:
- 2014-11-19
Related products to: Sheep Islet amyloid polypeptide,IAPP ELISA Kit
Related articles to: Sheep Islet amyloid polypeptide,IAPP ELISA Kit
- Amylin is a pancreatic neuroendocrine peptide that links peripheral metabolic regulation with central homeostatic and neurodegenerative pathways. However, its relevance to the inflammatory and demyelinating processes underlying multiple sclerosis (MS) remains unclear. To date, the role of amylin in MS has not been investigated. This study investigated serum amylin levels in patients with MS and their association with disease status. This cross-sectional case-control study included 62 patients meeting the 2017 McDonald criteria for MS and 63 control participants without MS or associated risk factors. Serum amylin levels were measured using enzyme-linked immunosorbent assay (ELISA). Between-group and phenotype-specific differences were examined. Multivariable logistic regression and receiver operating characteristic (ROC) curve analyses were performed to assess the association between serum amylin and MS status, and the discriminatory performance of serum amylin, respectively. Serum amylin levels were determined in both groups and reported as mean values. Mean serum amylin levels were significantly lower in patients with MS than in controls (234.01 ± 94.84 vs 284.04 ± 110.02 ng/L; P = .003). The groups were comparable across the principal anthropometric, metabolic, and biochemical variables assessed. No significant differences were observed among the relapsing-remitting, secondary progressive, and primary progressive MS (PPMS) phenotypes; however, pairwise analysis demonstrated a significant difference between the relapsing-remitting MS (RRMS) subgroup and controls (P = .017). In multivariable analysis, higher serum amylin levels remained independently associated with lower odds of MS after adjustment for aspartate aminotransferase (AST) activity (P = .02). Despite the significant between-group difference, serum amylin demonstrated only modest discriminatory performance (P = .003). Lower circulating amylin levels were associated with MS status, although their modest discriminatory performance does not support the use of serum amylin as a standalone diagnostic marker, based on the present data. The phenotype-specific difference observed in RRMS warrants further investigation in larger, longitudinal, and clinically characterized cohorts. These findings may deepen insights into MS development and support future biomarker research. - Source: PubMed
Cinkir UfukBir Levent SinanTekin SelmaKaragulmez Ahmet MagrurAvci Cicek EsinSenol Hande - - Source: PubMed
Publication date: 2026/08/29
Li Xiao-LingXu GangChen TianfengWong Yum-ShingZhao Hai-LuFan Rong-RongGu Xue-MeiTong Peter C YChan Juliana C N - Amylin is a peptide hormone co-secreted with insulin by pancreatic β-cells that regulates glucose homeostasis and satiety. In humans, amylin exhibits a strong propensity to aggregate, contributing to β-cell dysfunction and the development of type 2 diabetes mellitus (T2D). Emerging evidence suggests that amylin aggregates may exert systemic effects beyond the pancreas, potentially affecting peripheral tissues and the brain. However, evidence supporting this multi-organ involvement remains limited. In this study, we investigated the impact of human amylin aggregation across metabolic tissues using a transgenic mouse model expressing human IAPP (TghIAPP), fed either a standard diet (STD) or a high-fat diet (HFD), and evaluated the therapeutic potential of resveratrol. HFD-fed TghIAPP mice developed impaired glucose tolerance, increased amyloid aggregation, and enhanced markers of apoptosis and senescence in pancreatic islets. These alterations were associated with activation of endoplasmic reticulum (ER) stress pathways. Resveratrol treatment significantly reduced pancreatic amyloid burden, attenuated ER stress signaling, and improved markers of β-cell integrity. In the liver, TghIAPP mice exhibited increased lipid accumulation, inflammatory markers, and amyloid oligomer deposition, although the effects of resveratrol were modest and did not consistently reach statistical significance. In the brain, amyloid aggregates were detected in the hippocampus; however, resveratrol-induced changes in aggregate load and behavioral performance were limited and should be interpreted cautiously. Overall, these findings support a robust role for amylin aggregation in pancreatic dysfunction and highlight resveratrol as a modulator of pancreatic proteotoxic stress. The observed alterations in liver and brain suggest potential systemic effects of amylin aggregates that warrant further investigation. - Source: PubMed
Publication date: 2026/08/14
Iglesias-Fortes SaraiGarcía-Aguilar AnaGarcía GemaRodríguez-Cueto CarmenFernández-Ruiz JavierMartín-Cámara OlmoMenéndez J CarlosBenito ManuelGuillén Carlos - : Adherence to a low-carbohydrate diet induces distinct metabolic adaptations, yet the acute endocrine responses to individual macronutrients within this adapted state remain incompletely characterized. This study aimed to determine the acute, postprandial endocrine and glycemic kinetics following isolated isocaloric carbohydrate, protein, and fat boluses in healthy adults adapted to a low-carbohydrate diet. : Participants (13 female, 11 male) completed three interventions which consisted of consuming an isovolumetric 300 kcal drink of either whey protein (PRO), dextrose (CHO), or olive oil (FAT) mixed with water. Blood was taken immediately prior to drink consumption and then every 30 min afterwards for 2 h in each condition. Continuous glucose monitoring occurred during each intervention. : Postprandial glucose remained stable following the FAT and PRO conditions, whereas the CHO condition significantly increased glucose concentrations over time ( < 0.01). Glucagon did not differ between FAT and CHO ( = 0.28) but increased following PRO compared to both FAT and CHO ( < 0.01). Insulin, C-peptide and amylin rose in the CHO condition, with smaller increases in PRO and minimal changes in FAT ( < 0.01). GLP-1 was elevated in the PRO condition compared to both FAT and CHO ( < 0.01), while GIP increased most in the CHO condition and differed across all treatments ( < 0.01). Ghrelin decreased after CHO and PRO, leptin did not significantly change across conditions, and both PP and PYY were lower in the CHO condition at later time points relative to FAT and PRO. Inflammatory markers showed minimal acute changes across conditions, although MCP-1 increased over time following PRO. : In low-carbohydrate-adapted individuals, isolated macronutrient boluses elicit highly distinct, divergent endocrine signatures. The robust, acute glucagon response to pure protein does not cause short-term glycemic excursions, indicating that counter-regulatory incretin and insulinotropic pathways remain highly capable of preserving immediate glucose homeostasis. - Source: PubMed
Publication date: 2026/08/15
Deru Landon SBailey Bruce WHales Katelynn EGipson Elizabeth ZMerrill Ray MBikman Benjamin T - : Human islet amyloid polypeptide (IAPP) aggregation plays a critical role in the pathogenesis of type 2 diabetes mellitus (T2DM). Although metabolic alterations are a hallmark of T2DM, the functional roles of differential metabolites in regulating disease-associated molecular processes remain largely unexplored. This study aimed to establish a metabolomics-guided strategy for identifying endogenous metabolites with anti-amyloid activity and to investigate their underlying chemical interactions with IAPP. : Untargeted metabolomic profiling of clinical samples from T2DM patients, obesity patients and healthy controls was performed to identify differential metabolites. Candidate metabolites were subsequently screened for their ability to modulate IAPP aggregation. Transmission electron microscopy (TEM), thioflavin T (ThT) fluorescence assays, and cell viability measurements were employed to evaluate their effects on fibril formation and cytotoxicity. Mass spectrometry was further used to characterize metabolite-IAPP interactions. : Metabolomic analysis identified 3-hydroxypyruvic acid (also known as β-hydroxypyruvic acid, hereafter referred to as HPA) as a significantly altered endogenous metabolite associated with T2DM and a candidate regulator of IAPP aggregation. Functional assays demonstrated that HPA effectively inhibited amyloid fibril formation, as evidenced by the absence of typical fibrillar structures and a prolonged lag phase during aggregation. HPA also significantly alleviated IAPP-induced cytotoxicity. Mass spectrometric analysis revealed the formation of HPA-IAPP oligomer complexes ( < 4), suggesting that HPA directly interacts with early oligomeric intermediates and interferes with their progression toward mature fibrils. : This work demonstrates that untargeted metabolomics of clinical samples can serve as an effective strategy for discovering bioactive endogenous metabolites involved in disease-related molecular processes. The identification of HPA as a potential endogenous inhibitor of IAPP aggregation provides new chemical insight into the relationship between metabolic dysregulation and amyloidogenesis and highlights endogenous metabolites as a valuable source of potential therapeutic lead compounds. - Source: PubMed
Publication date: 2026/08/03
Xia DandanGu LiubaoYang LeiHu JiaojiaoXu XiaoweiJiang DechenZheng QiulingWan Bing