Peptidomic Profiling of Secreted Products from Pancreatic Islet Culture Results in a Higher Yield of Full-length Peptide Hormones than Found using Cell Lysis Procedures

Taylor, Steven W.; Nikoulina, Svetlana E.; Andon, Nancy L.; Lowe, Carolyn

doi:10.1021/pr400115q

Cited by 25 publications

(40 citation statements)

References 46 publications

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“…Their results confirmed that GLP-1 was produced in and secreted from human islets, specifically the α cells. In a more recent study, Taylor et al (2013) employed Peptide Hormone Acquisition through Smart Sampling Technique-Mass Spectrometry (PHASST-MS), an advanced peptidomics platform that employs high resolution liquid chromatography-mass spectrometry (LC-MS), to identify secreted peptide hormones, and reported that both full-length GLP-1(1–37) and bioactive GLP-1(7–37) were detected in the media of cultured human islets (Taylor, et al 2013). All of these studies support the presence of a local GLP-1 production system within the pancreatic islets.…”

Section: Emerging Evidence Supporting Glp-1 Production In Pancreatmentioning

confidence: 99%

Intra-islet glucagon-like peptide 1

Fava

Dong

2016

Journal of Diabetes and its Complications

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Purpose Glucagon-like peptide-1 (GLP-1) is originally identified in the gut as an incretin hormone, and it is potent in stimulating insulin secretion in the pancreas. However, increasing evidence suggests that GLP-1 is also produced locally within pancreatic islets. This review focuses on the past and current discoveries regarding intra-islet GLP-1 production and its functions. Main findings There has been a long-standing debate with regard to whether GLP-1 is produced in the pancreatic α cells. Early controversies lead to the widely accepted conclusion that the vast majority of proglucagon is processed to form glucagon in the pancreas, whereas an insignificant amount is cleaved to produce GLP-1. With technological advancements, recent studies have shown that bioactive GLP-1 is produced locally in the pancreas, and the expression and secretion of GLP-1 within islets are regulated by various factors such as cytokines, hyperglycemia, and β cell injury. Conclusions GLP-1 is produced by the pancreatic α cells, and it is fully functional as an incretin. Therefore, intra-islet GLP-1 may exert insulinotropic and glucagonostatic effects locally via paracrine and/or autocrine actions, under both normal and diabetic conditions.

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Section: Emerging Evidence Supporting Glp-1 Production In Pancreatmentioning

confidence: 99%

Intra-islet glucagon-like peptide 1

Fava

Dong

2016

Journal of Diabetes and its Complications

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“…; Taylor et al. ). A further peptide, closely related to GRPP, GRPP‐like peptide (GRPP‐LP) was also identified in Wistar rat islets (Stewart et al.…”

Section: Introductionmentioning

confidence: 98%

Glicentin-related pancreatic polypeptide inhibits glucose-stimulated insulin secretion from the isolated pancreas of adult male rats

et al. 2015

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Peptides derived from the glucagon gene Gcg, for example, glucagon and glucagon‐like peptide 1 (GLP‐1), act as physiological regulators of fuel metabolism and are thus of major interest in the pathogenesis of diseases, such as type‐2 diabetes and obesity, and their therapeutic management. Glicentin‐related pancreatic polypeptide (GRPP) is a further, 30 amino acid Gcg‐derived peptide identified in human, mouse, rat, and pig. However, the potential glucoregulatory function of this peptide is largely unknown. Here, we synthesized rat GRPP (rGRPP) and a closely related peptide, rat GRPP‐like peptide (rGRPP‐LP), and investigated their actions in the liver and pancreas of adult male rats by employing isolated‐perfused organ preparations. Rat GRPP and rGRPP‐LP did not affect glucose output from the liver, but both elicited potent inhibition of glucose‐stimulated insulin secretion (GSIS) from the rat pancreas. This action is unlikely to be mediated by glucagon or GLP‐1 receptors, as rGRPP and rGRPP‐LP did not stimulate cyclic adenosine monophosphate (cAMP) production from the glucagon or GLP‐1 receptors, nor did they antagonize glucagon‐ or GLP‐1‐stimulated cAMP‐production at either receptor. GRPP and GRPP‐LP may be novel regulators of insulin secretion, acting through an as‐yet undefined receptor.

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“…Peptidomics attempts to perform a quantitative and qualitative analysis of peptides in a given cell type, tissue or disease state. Through this method, a large number of both intracellular and secreted mammalian peptides have been identified [4][5][6][7][8][9]. Peptides are important bioactive molecules in their own right.…”

Section: Introductionmentioning

confidence: 99%

Peptidomic Analysis of Cultured Cardiomyocytes Exposed to Acute Ischemic-Hypoxia

et al. 2017

Cell Physiol Biochem

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Background: Acute Myocardial Infarction (AMI) is a life-threatening cardiovascular disease involving disruption of blood flow to the heart, consequent tissue damage, and sometimes death. Peptidomics, an emerging branch of proteomics, has attracted wide attention. Methods: A comparative peptidomic profiling was used to explore changes induced by acute ischemichypoxia in primary cultured neonatal rat myocardial cells. Analysis of six-plex tandem mass tag (TMT) labelled peptides was performed using nanoflow liquid chromatography coupled online with an LTQ-Orbitrap Velos mass spectrometer. Results: A total of 220 differentially expressed peptides originating from 119 proteins were identified, of which 37 were upregulated and 183 were downregulated in cardiomyocytes exposed to hypoxia/ischemia conditions. Many of the identified peptides were derived from functional domains of proteins closely associated with cardiomyocyte structure or AMI. Conclusion: Numerous peptides may be involved in process of AMI. These results pave the way for future functional studies of the identified peptides.

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Peptidomic Profiling of Secreted Products from Pancreatic Islet Culture Results in a Higher Yield of Full-length Peptide Hormones than Found using Cell Lysis Procedures

Cited by 25 publications

References 46 publications

Intra-islet glucagon-like peptide 1

Intra-islet glucagon-like peptide 1

Glicentin-related pancreatic polypeptide inhibits glucose-stimulated insulin secretion from the isolated pancreas of adult male rats

Peptidomic Analysis of Cultured Cardiomyocytes Exposed to Acute Ischemic-Hypoxia

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