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Amylin 100:1

Amylin - Wikivividly

Amylin - Wikivividly

Wiki as never seen before with video and photo This article is about the polypeptide. For the biotechnology company, see Amylin Pharmaceuticals . IAPP , DAP, IAP, islet amyloid polypeptide Amino acid sequence of amylin with disulfide bridge and cleavage sites of insulin degrading enzyme indicated with arrows Amylin, or islet amyloid polypeptide (IAPP), is a 37-residue peptide hormone . [5] It is cosecreted with insulin from the pancreatic -cells in the ratio of approximately 100:1 (insulin:amylin). Amylin plays a role in glycemic regulation by slowing gastric emptying and promoting satiety, thereby preventing post-prandial spikes in blood glucose levels. IAPP is processed from an 89-residue coding sequence . Proislet amyloid polypeptide (proIAPP, proamylin, proislet protein) is produced in the pancreatic beta cells (-cells) as a 67 amino acid, 7404 Dalton pro-peptide and undergoes post-translational modifications including protease cleavage to produce amylin. [6] Post-translational Modification of proIAPP to form IAPP ProIAPP consists of 67 amino acids , which follow a 22 amino acid signal peptide which is rapidly cleaved after translation of the 89 amino acid coding sequence, the human sequence (from N-terminus to C-terminus ) is: (MGILKLQVFLIVLSVALNHLKA) TPIESHQVEKR^ KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTYG^ KR^ NAVEVLKREPLNYLPL. [6] [7] Once released from the signal peptide, it undergoes additional proteolysis and posttranslational modification (indicated by ^). 11 amino acids are removed from the N-terminus by the enzyme proprotein convertase 2 (PC2) while 16 are removed from the C-terminus of the proIAPP molecule by proprotein convertase 1/3 (PC1/3). [8] At the C-terminus Carboxypeptidase E then removes the terminal lysine and arginine residues. [9] The terminal gly Continue reading >>

Iapp / Amylin Antibody (n-terminus) For Ihc, Icc, If/immunofluorescence, Wb/western Ls-c352341

Iapp / Amylin Antibody (n-terminus) For Ihc, Icc, If/immunofluorescence, Wb/western Ls-c352341

Immunohistochemical analysis of Amylin staining in human brain formalin fixed paraffin embedded tissue section. The section was pre-treated using heat mediated antigen retrieval with sodium citrate buffer (pH 6.0). The section was then incubated with the antibody at room temperature and detected using an HRP conjugated compact polymer system. DAB was used as the chromogen. The section was then counterstained with hematoxylin and mounted with DPX. Immunofluorescent analysis of Amylin staining in HeLa cells. Formalin-fixed cells were permeabilized with 0.1% Triton X-100 in TBS for 5-10 minutes and blocked with 3% BSA-PBS for 30 minutes at room temperature. Cells were probed with the primary antibody in 3% BSA-PBS and incubated overnight at 4 C in a humidified chamber. Cells were washed with PBST and incubated with a DyLight 594-conjugated secondary antibody (red) in PBS at room temperature in the dark. DAPI was used to stain the cell nuclei (blue). Western blot analysis of Amylin expression in MCF7 (A); HeLa (B); mouse kidney (C); rat kidney (D) whole cell lysates. Immunohistochemical analysis of Amylin staining in human brain formalin fixed paraffin embedded tissue section. The section was pre-treated using heat mediated antigen retrieval with sodium citrate buffer (pH 6.0). The section was then incubated with the antibody at room temperature and detected using an HRP conjugated compact polymer system. DAB was used as the chromogen. The section was then counterstained with hematoxylin and mounted with DPX. Immunofluorescent analysis of Amylin staining in HeLa cells. Formalin-fixed cells were permeabilized with 0.1% Triton X-100 in TBS for 5-10 minutes and blocked with 3% BSA-PBS for 30 minutes at room temperature. Cells were probed with the primary antibody in 3% BSA-PB Continue reading >>

-hairpin Of Islet Amyloid Polypeptide Bound To An Aggregation Inhibitor

-hairpin Of Islet Amyloid Polypeptide Bound To An Aggregation Inhibitor

-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation Inhibitor Scientific Reports volume 6, Articlenumber:33474 (2016) | Download Citation In type 2 diabetes, the formation of islet amyloid consisting of islet amyloid polypeptide (IAPP) is associated with reduction in -cell mass and contributes to the failure of islet cell transplantation. Rational design of inhibitors of IAPP amyloid formation has therapeutic potential, but is hampered by the lack of structural information on inhibitor complexes of the conformationally flexible, aggregation-prone IAPP. Here we characterize a -hairpin conformation of IAPP in complex with the engineered binding protein -wrapin HI18. The -strands correspond to two amyloidogenic motifs, 12-LANFLVH-18 and 22-NFGAILS-28, which are connected by a turn established around Ser-20. Besides backbone hydrogen bonding, the IAPP:HI18 interaction surface is dominated by non-polar contacts involving hydrophobic side chains of the IAPP -strands. Apart from monomers, HI18 binds oligomers and fibrils and inhibits IAPP aggregation and toxicity at low substoichiometric concentrations. The IAPP -hairpin can serve as a molecular recognition motif enabling control of IAPP aggregation. Aberrant protein aggregation into amyloid fibrils occurs in many age related diseases, including Alzheimers disease (AD), Parkinsons disease (PD), and Type 2 Diabetes (T2D) 1 . In T2D, the 37 amio acid residue polypeptide IAPP aggregates into pancreatic islet amyloid deposits 2 , 3 . IAPP is a hormone stored in -cell secretory granules and co-secreted with insulin, with putative physiological roles in pancreatic islets as well as in the central nervous system. IAPP can convert into the amyloid state due to the occurrence of three amyloidogenic regions in its amino acid Continue reading >>

The High-fat Hep C Diet

The High-fat Hep C Diet

When this story broke, I had to look up amylin in my biochemistry (Mathews, Van Holde, Aherne 2000) and physiology (Best and Taylor, 1984) texbooks. Neither has amylin indexed. Nor do I remember any insightful blogs about amylin from the usual suspects recently. Flyin' blind here. Thank God for wikipedia. This news story linking amylin build up to diabetes, based on new research conducted jointly in Auckland, New Zealand and Manchester England, makes the case reasonably clearly: Diabetes is defined as thelossof beta-cells, so that insulin production ceases - the insulin dependent stage. Interestingly, amylin allegedly plays the same role in type 1 and 2 diabetes, and the aggregates of amylin areamyloidformations similar to those seen in alzheimers. Before you start thinking of type 3 diabetes, though, the amyloids in Alzheimers aren't made of amylin. Amyloid just means "starch-like". What they have in common is beta-sheet protein structures (nothing to do with beta-cells) misfolding in a contagious, prion-like process. Amylin, AKAIslet Amyloid Polypeptide(IAPP)is a protein produced by beta-cells in tandem with insulin. Insulin promotes glucose uptake and metabolism in cells, amylin slows glucose - and other food - uptake from the gut, by delaying gastric emptying, and decreases appetite; it also seems to be responsible from the switch from muscle glycogenogenesis to adipose lipogenesis, so probably has a role in obesity . According to wiki the ratio is 100:1 in favour of amylin (unless I've read it wrong and it's the other way round). Is the ratio always constant? Does amylin have any independence from insulin? In any case, amylin plus glucose represents a two-pronged approach to preventing systemic over-exposure to glucose; insulin pulls glucose out of, amylin slows a Continue reading >>

Neuroendocrine Hormone Amylin In Diabetes

Neuroendocrine Hormone Amylin In Diabetes

Neuroendocrine hormone amylin in diabetes Xiao-Xi Zhang , Yan-Hong Pan , Yan-Mei Huang , and Hai-Lu Zhao Xiao-Xi Zhang, Yan-Hong Pan, Yan-Mei Huang, Hai-Lu Zhao, Centre of Diabetic Systems Medicine, Guangxi Key Laboratory of Excellence, Guilin Medical University, Guilin 541004, Guangxi Zhuang Autonomous Region, China Xiao-Xi Zhang, Hai-Lu Zhao, Institute of Basic Medical Science, College of Basic Medical Science, Guilin Medical University, Guilin 541004, Guangxi Zhuang Autonomous Region, China Author contributions: Zhang XX performed the majority of the writing, prepared the figures and tables; Pan YH performed data accusation and writing; Huang YM provided the information of tables of the paper; Zhao HL designed the outline and coordinated the writing of the paper. Correspondence to: Hai-Lu Zhao, MD, PhD, Professor, Director, Centre of Diabetic Systems Medicine, Guangxi Key Laboratory of Excellence, Guilin Medical University, Huan Cheng North 2nd Road 109, Guilin 541004, Guangxi Zhuang Autonomous Region, China. [email protected] Telephone: +86-773-5805803 Fax: +86-773-5895805 Received 2016 Jan 6; Revised 2016 Mar 16; Accepted 2016 Apr 5. Copyright The Author(s) 2016. Published by Baishideng Publishing Group Inc. All rights reserved. This article has been cited by other articles in PMC. The neuroendocrine hormone amylin, also known as islet amyloid polypeptide, is co-localized, co-packaged and co-secreted with insulin from adult pancreatic islet cells to maintain glucose homeostasis. Specifically, amylin reduces secretion of nutrient-stimulated glucagon, regulates blood pressure with an effect on renin-angiotensin system, and delays gastric emptying. The physiological actions of human amylin attribute to the conformational -helix monomers whereas the misfolding instab Continue reading >>

Amylin-a Kind Of Peptide Associated With Diabetes

Amylin-a Kind Of Peptide Associated With Diabetes

Amylin-A kind of peptide associated with diabetes Amylin, or Islet Amyloid Polypeptide (IAPP), is a 37-residue peptide hormone.[1] It is cosecreted with insulin from the pancreatic -cells in the ratio of approximately 100:1. Amylin plays a role in glycemic regulation by slowing gastric emptying and promoting satiety, thereby preventing post-prandial spikes in blood glucose levels. IAPP is processed from an 89-residue coding sequence. Proislet Amyloid Polypeptide (proIAPP,Proamylin, Proislet Protein) is produced in the pancreatic beta cells (-cells) as a 67 amino acid, 7404 Dalton pro-peptide and undergoes post-translational modifications including protease cleavage to produce amylin.[2] The human form of IAPP has the amino acid sequence KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY, with a disulfide bridge between cysteine residues 2 and 7. Both the amidated C-terminus and the disulfide bridge are necessary for the full biological activity of amylin. IAPP is capable of forming amyloid fibrils in vitro. Within the fibrillization reaction, the early prefibrillar structures are extremely toxic to beta-cell and insuloma cell cultures.[2] Later amyloid fiber structures also seem to have some cytotoxic effect on cell cultures. Studies have shown that fibrils are the end product and not necessarily the most toxic form of amyloid proteins/peptides in general. A non-fibril forming peptide (1-19 residues of human amylin) is toxic like the full-length peptide but the respective segment of rat amylin is not. It was also demonstrated by solid-state NMR spectroscopy that the fragment 20-29 of the human-amylin fragments membranes. Rats and mice have six substitutions (three of which are proline substitions at positions 25, 28 and 29) that are believed to prevent the formation of amyloid fibr Continue reading >>

Pdf | Neuroinflammation And Neurologic Deficits In Diabetes Linked To Brain Accumulation Of Amylin

Pdf | Neuroinflammation And Neurologic Deficits In Diabetes Linked To Brain Accumulation Of Amylin

Background: We recently found that brain tissue from patients with type-2 diabetes (T2D) and cognitive impairment contains deposits of amylin, an amyloidogenic hormone synthesized and co-secreted with insulin by pancreatic -cells. Amylin deposition is promoted by chronic hypersecretion of amylin (hyperamylinemia), which is common in humans with obesity or pre-diabetic insulin resistance. Human amylin oligomerizes quickly when oversecreted, which is toxic, induces inflammation in pancreatic islets and contributes to the development of T2D. Here, we tested the hypothesis that accumulation of oligomerized amylin affects brain function. Methods: In contrast to amylin from humans, rodent amylin is neither amyloidogenic nor cytotoxic. We exploited this fact by comparing rats overexpressing human amylin in the pancreas (HIP rats) with their littermate rats which express only wild-type (WT) non-amyloidogenic rodent amylin. Cage activity, rotarod and novel object recognition tests were performed on animals nine months of age or older. Amylin deposition in the brain was documented by immunohistochemistry, and western blot. We also measured neuroinflammation by immunohistochemistry, quantitative real-time PCR and cytokine protein levels. Results: Compared to WT rats, HIP rats show i) reduced exploratory drive, ii) impaired recognition memory and iii) no ability to improve the performance on the rotarod. The development of neurological deficits is associated with amylin accumulation in the brain. The level of oligomerized amylin in supernatant fractions and pellets from brain homogenates is almost double in HIP rats compared with WT littermates (P < 0.05). Large amylin deposits (>50 m diameter) were also occasionally seen in HIP rat brains. Accumulation of oligomerized amylin alte Continue reading >>

Probing Amylin Fibrillation At An Early Stage Via A Tetracysteine-recognising Fluorophore

Probing Amylin Fibrillation At An Early Stage Via A Tetracysteine-recognising Fluorophore

Probing amylin fibrillation at an early stage via a tetracysteine-recognising fluorophore Open Access funded by Engineering and Physical Sciences Research Council An early detection assay for amylin fibrillation was developed using a tetracysteine-recognising fluorophore, FlAsH. FlAsH can transform into a fluorescent form upon binding to amylin oligomers. The visualisation of amylin fibrils was achieved. The effects of amyloid inhibitor/modulator on amylin fibrillation was investigated by FlAsH assay. Amyloid fibrillation is a nucleation-dependent process known be involved in the development of more than 20 progressive and chronic diseases. The detection of amyloid formation at the nucleation stage can greatly advance early diagnoses and treatment of diseases. In this work, we developed a new assay for the early detection of amylin fibrillation using the biarsenical dye 4,5-bis(1,3,2-dithiarsolan-2-yl)fluorescein (FlAsH), which could recognise tetracysteine motifs and transform from non-fluorescent form into strongly fluorescent complexes. Due to the close proximity of two cysteine residues within the hydrophilic domain of amylin, a non-contiguous tetracysteine motif can form upon amylin dimerisation or oligomerisation, which can be recognised by FlAsH and emit strong fluorescence. This enables us to report the nucleation-growth process of amylin without modification of the protein sequence. We showed that the use of this assay not only allowed the tracking of initial nucleation events, but also enabled imaging of amyloid fibrils and investigation of the effects of amyloid inhibitor/modulator toward amylin fibrillation. Continue reading >>

Us5175145a - Treatment Of Diabetes Mellitus With Amylin Agonists - Google Patents

Us5175145a - Treatment Of Diabetes Mellitus With Amylin Agonists - Google Patents

US5175145A - Treatment of diabetes mellitus with amylin agonists - Google Patents Treatment of diabetes mellitus with amylin agonists US5175145A US07821479 US82147992A US5175145A US 5175145 A US5175145 A US 5175145A US 07821479 US07821479 US 07821479 US 82147992 A US82147992 A US 82147992A US 5175145 A US5175145 A US 5175145A Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.) Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.) Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.) A61MEDICAL OR VETERINARY SCIENCE; HYGIENE A61KPREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES A61K38/00Medicinal preparations containing peptides A61K38/16Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof A61K38/17Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans A61K38/225Calcitonin gene related peptide A61MEDICAL OR VETERINARY SCIENCE; HYGIENE A61KPREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES A61K38/00Medicinal preparations containing peptides A61K38/16Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof A61K38/17Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans A61MEDICAL OR VETERINARY SCIENCE; HYGIENE A61KPREPARATIONS FOR MEDICAL, DENT

Pancreas Flashcards | Quizlet

Pancreas Flashcards | Quizlet

The overall effect is to slow the rate of appearance (Ra) of glucose in the blood after eating; this is accomplished via coordinate slowing down gastric emptying, inhibition of digestive secretion [gastric acid, pancreatic enzymes, and bile ejection], and a resulting reduction in food intake. How is amylin release altered during diabetes? it is decreased since insulin is decreased Because it is the major nutrient utilized by neural tissue. What are the normal fasting blood glucose concentration? What are the normal postprandial blood glucose levels? Should glucose be maintained between meals? What was liver do with the excess glucose? What 6 organs are responsive for achieving glucose control? pancreas, liver, intestine, muscle, adrenals, brain 3 ways that glucose can enter the bloodstream: How much glycogen does the body usually have stored? 4 types of molecules that glucose is created from: lactate (52% of gluconeo. 13% of glucose) amino acids (28% of gluconeo. 7% of glucose) glycerol (16% of gluconeo. 4% of glucose) What is the main amino acid that is used to make glucose? To increase glucose uptake via GLUT transporters How many membrane spanning domains do glucose transporters have? How many different glucose transporters are there? GLUT transporter for RBC that functions at physiological levels of glucose. GLUT transporter that in mainly in the liver and small intestines, some is also in the kidney. There can be issues with this transported in type 1 and 2 diabetes. GLUT transporter for the brain, placenta, and testes. GLUT transporter for the adipose tissue, skeletal muscle, and cardiac muscle. Has a high turnover rate, and insulin increases this turnover rate even more. These are decreased in obese and type 2 diabetes. What is the synthetic analog of Amylin tha Continue reading >>

Neuroinflammation And Neurologic Deficits In Diabetes Linked To Brain Accumulation Of Amylin

Neuroinflammation And Neurologic Deficits In Diabetes Linked To Brain Accumulation Of Amylin

Neuroinflammation and neurologic deficits in diabetes linked to brain accumulation of amylin Srodulski et al.; licensee BioMed Central Ltd.2014 We recently found that brain tissue from patients with type-2 diabetes (T2D) and cognitive impairment contains deposits of amylin, an amyloidogenic hormone synthesized and co-secreted with insulin by pancreatic -cells. Amylin deposition is promoted by chronic hypersecretion of amylin (hyperamylinemia), which is common in humans with obesity or pre-diabetic insulin resistance. Human amylin oligomerizes quickly when oversecreted, which is toxic, induces inflammation in pancreatic islets and contributes to the development of T2D. Here, we tested the hypothesis that accumulation of oligomerized amylin affects brain function. In contrast to amylin from humans, rodent amylin is neither amyloidogenic nor cytotoxic. We exploited this fact by comparing rats overexpressing human amylin in the pancreas (HIP rats) with their littermate rats which express only wild-type (WT) non-amyloidogenic rodent amylin. Cage activity, rotarod and novel object recognition tests were performed on animals nine months of age or older. Amylin deposition in the brain was documented by immunohistochemistry, and western blot. We also measured neuroinflammation by immunohistochemistry, quantitative real-time PCR and cytokine protein levels. Compared to WT rats, HIP rats show i) reduced exploratory drive, ii) impaired recognition memory and iii) no ability to improve the performance on the rotarod. The development of neurological deficits is associated with amylin accumulation in the brain. The level of oligomerized amylin in supernatant fractions and pellets from brain homogenates is almost double in HIP rats compared with WT littermates (P < 0.05). Large amylin Continue reading >>

Wo2013156594a1 - Human Amylin Analogues - Google Patents

Wo2013156594a1 - Human Amylin Analogues - Google Patents

WO2013156594A1 - Human amylin analogues - Google Patents WO2013156594A1 PCT/EP2013/058165 EP2013058165W WO2013156594A1 WO 2013156594 A1 WO2013156594 A1 WO 2013156594A1 EP 2013058165 W EP2013058165 W EP 2013058165W WO 2013156594 A1 WO2013156594 A1 WO 2013156594A1 Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.) C07K14/00Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof C07K14/435Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans A61MEDICAL OR VETERINARY SCIENCE; HYGIENE A61KPREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES A61K38/00Medicinal preparations containing peptides The invention relates to polypeptides comprising an amino acid sequence which is an analogue of human amylin, pharmaceutical compositions comprising these polypeptides, and these polypeptides for use as medicaments. The invention relates to polypeptides comprising an amino acid sequence which is an analogue of SEQ ID No: 1 (human amylin), pharmaceutical compositions comprising these polypeptides, and these polypeptides for use as medicaments. A large and growing number of people suffer from diabetes mellitus and obesity. Diabetes mellitus is a metabolic disorder in which the ability to utilize glucose is partly or completely lost. A number of treatment regimes target excessive blood glucose whereas others are focused primarily on weight reduction. The most efficient anti-diabetic agent used to lower blood glucose is insulin and analogue(s) thereof. It has been known for a long time that when traditional insulin is used to treat dia

Anti-amylin Antibody [n2c3] | Genetex

Anti-amylin Antibody [n2c3] | Genetex

Application Information: Amylin antibody [N2C3] *Optimal dilutions/concentrations should be determined by the researcher. 0.83 mg/ml (Please refer to the vial label for the specific concentration) Islet, or insulinoma, amyloid polypeptide is commonly found in pancreatic islets of patients suffering diabetes mellitus type II, or harboring an insulinoma. While the assosciation of amylin with the development of type II diabetes has been known for some time, a direct causative role for amylin has been harder to establish. Studies suggest that amylin, like the related beta-amyloid (Abeta) associated with Alzheimer's disease, can induce apoptotic cell-death in particular cultured cells, an effect that may be relevant to the development of type II diabetes. [provided by RefSeq] DAP antibody, IAP antibody, IAPP antibody, diabetes-associated peptide antibody, amylin antibody, Islet amyloid polypeptide (diabetes-associated peptide, amylin) antibody, islet amyloid polypeptide antibody, insulinoma amyloid peptide antibody Continue reading >>

Amylin - Wikipedia

Amylin - Wikipedia

This article is about the polypeptide. For the biotechnology company, see Amylin Pharmaceuticals . IAPP , DAP, IAP, islet amyloid polypeptide Amino acid sequence of amylin with disulfide bridge and cleavage sites of insulin degrading enzyme indicated with arrows Amylin, or islet amyloid polypeptide (IAPP), is a 37-residue peptide hormone . [3] It is cosecreted with insulin from the pancreatic -cells in the ratio of approximately 100:1 (insulin:amylin). Amylin plays a role in glycemic regulation by slowing gastric emptying and promoting satiety, thereby preventing post-prandial spikes in blood glucose levels. IAPP is processed from an 89-residue coding sequence . Proislet amyloid polypeptide (proIAPP, proamylin, proislet protein) is produced in the pancreatic beta cells (-cells) as a 67 amino acid, 7404 Dalton pro-peptide and undergoes post-translational modifications including protease cleavage to produce amylin. [4] Post-translational Modification of proIAPP to form IAPP ProIAPP consists of 67 amino acids , which follow a 22 amino acid signal peptide which is rapidly cleaved after translation of the 89 amino acid coding sequence. The human sequence (from N-terminus to C-terminus ) is: (MGILKLQVFLIVLSVALNHLKA) TPIESHQVEKR^ KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTYG^ KR^ NAVEVLKREPLNYLPL. [4] [5] Once released from the signal peptide, it undergoes additional proteolysis and posttranslational modification (indicated by ^). 11 amino acids are removed from the N-terminus by the enzyme proprotein convertase 2 (PC2) while 16 are removed from the C-terminus of the proIAPP molecule by proprotein convertase 1/3 (PC1/3). [6] At the C-terminus Carboxypeptidase E then removes the terminal lysine and arginine residues. [7] The terminal glycine amino acid that results from this cleavage Continue reading >>

Peptide Synthesis, Custom Peptide, Peptide Coupling Reagents, Hatu, Fmoc Amino Acids Chempep Inc.

Peptide Synthesis, Custom Peptide, Peptide Coupling Reagents, Hatu, Fmoc Amino Acids Chempep Inc.

Amylin, or Islet Amyloid Polypeptide (IAPP), is a 37-residue peptide hormone secreted by pancreatic -cells at the same time as insulin (in a roughly 100:1 ratio). Amylin functions as part of the endocrine pancreas and contributes to glycemic control. Although amylin's complete function may not yet be known, it has been shown to slow gastric emptying, promote satiety, inhibit secretion of glucagon during hyperglycemia, and therein reduce the total insulin demand.[1][2] As insulin lowers blood glucose and glucagon raises blood glucose, amylin supports the stability of blood glucose levels in effect by slowing the rate that digested glucose enters the bloodstream. Rodent amylin knockouts are known to fail to achieve the normal anorexia following food consumption. Because it is an amidated peptide, like many neuropeptides, it is believed to be responsible for the anorectic effect. The human form of IAPP has the amino acid sequence KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY, with a disulfide bridge between cysteine residues 2 and 7. The peptide is secreted from the pancreas into the blood circulation and eventually excreted by the kidneys. IAPP is capable of forming amyloid fibrils in vitro. Within the fibrillization reaction, the early prefibrillar structures are extremely toxic to insuloma cells cultures. Later amyloid fibril structures also seem to have some cytotoxic effect on cell cultures. Rats and mice have proline residues that prevent the formation of amyloid fibrils. IAPP was identified independently by two groups as the major component of diabetes-associated islet amyloid deposits in 1987.[3][4] There appears to be at least three distinct receptor complexes that bind with high affinity to amylin. All three complexes contain the calcitonin receptor at the core, plus on Continue reading >>

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