Frog skin peptides (tigerinin-1R, magainin-AM1, -AM2, CPF-AM1, and PGla-AM1) stimulate secretion of glucagon-like peptide 1 (GLP-1) by GLUTag cells

Ojo, Opeolu O.; Conlon, J. Michael; Flatt, Peter R.; Abdel-Wahab, Yasser

doi:10.1016/j.bbrc.2012.12.116

Cited by 37 publications

(39 citation statements)

References 37 publications

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“…For example, CPF-1, CPF-3, CPF-5 and CPF-6 from X. laevis and CPF-SE1 from S. epitropicalis produced a significant increase in the rate of insulin release from BRIN-BD11 cells at concentrations as low as 0.03 nM. Similarly, magainin-AM1, magainin-AM2, CPF-AM1, and PGLa-AM1 stimulated release of the incretin peptide, GLP-1 from GLUTag cells with magainin-AM2 exhibiting the greatest potency (minimum concentration producing a significant stimulation = 1 nM) and CPF-AM1 producing the maximum stimulatory response (3.2-fold of basal rate at a concentration of 3 µM) [78]. …”

Section: Discussionmentioning

confidence: 99%

Host-Defense Peptides with Therapeutic Potential from Skin Secretions of Frogs from the Family Pipidae

Conlon

Mechkarska

2014

Pharmaceuticals

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Skin secretions from frogs belonging to the genera Xenopus, Silurana, Hymenochirus, and Pseudhymenochirus in the family Pipidae are a rich source of host-defense peptides with varying degrees of antimicrobial activities and cytotoxicities to mammalian cells. Magainin, peptide glycine-leucine-amide (PGLa), caerulein-precursor fragment (CPF), and xenopsin-precursor fragment (XPF) peptides have been isolated from norepinephrine-stimulated skin secretions from several species of Xenopus and Silurana. Hymenochirins and pseudhymenochirins have been isolated from Hymenochirus boettgeri and Pseudhymenochirus merlini. A major obstacle to the development of these peptides as anti-infective agents is their hemolytic activities against human erythrocytes. Analogs of the magainins, CPF peptides and hymenochirin-1B with increased antimicrobial potencies and low cytotoxicities have been developed that are active (MIC < 5 μM) against multidrug-resistant clinical isolates of Staphylococcus aureus, Escherichia coli, Acinetobacter baumannii, Stenotrophomonas maltophilia and Klebsiella pneumoniae. Despite this, the therapeutic potential of frog skin peptides as anti-infective agents has not been realized so that alternative clinical applications as anti-cancer, anti-viral, anti-diabetic, or immunomodulatory drugs are being explored.

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Section: Discussionmentioning

confidence: 99%

Host-Defense Peptides with Therapeutic Potential from Skin Secretions of Frogs from the Family Pipidae

Conlon

Mechkarska

2014

Pharmaceuticals

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“…In addition to antibacterial effects, it has been shown that this peptide stimulates the secretion of glucagon‐like peptide 1 and thus stimulates the insulin production in BRIN‐BD11 rat clonal B cells. Consequently, this peptide has the potential to be developed into molecules for the treatment of patients with Type 2 diabetes …”

Section: Search Strategymentioning

confidence: 99%

Review of antimicrobial peptides with anti‐Helicobacter pylori activity

et al. 2018

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Background The emergence of antibiotic‐resistant Helicobacter pylori strains in recent years has increased the need for finding an alternative in the post‐antibiotic era. One of the fields being considered for this purpose is antimicrobial peptides. The aim of this review was to provide an obvious scheme from the studied anti‐H. pylori peptides and to investigate their common features. Method First, all of the antimicrobial peptides with their anti‐H. pylori effects have been proved up to September 2018 were selected and their information including structure, mechanism of action, and function was reviewed. To achieve this, three databases of PubMed, Scopus, and Web of science were used. Results A total of 9 groups containing 22 antimicrobial peptides were found with demonstrated anti‐H. pylori effects. The nine groups included pexiganan, tilapia piscidins, epinecidin‐1, cathelicidins, defensins, bicarinalin, odorranain‐HP, PGLa‐AM1, and bacteriocins. Most of the antimicrobial peptides, not all, had common features such as the ability to kill antibiotic‐resistant strains, having α‐helical structure, being cationic, with high positive charge and isoelectric point. Conclusion Antimicrobial peptides with anti‐H. pylori effects have the potential to replace the antibiotics, especially in the post‐antibiotic era, if a rapid and low‐cost production method would be found.

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“…PGLa-AM1 and its [A3K], [A14K] and [A20K] analogues were supplied in crude form by GL Biochem Ltd (Shanghai, China) and were purified to near homogeneity (>98% purity) by reversed-phase HPLC by reversed-phase HPLC on a (2.2-cm x 25-cm) Vydac 218TP1022 (C-18) column (Grace, Deerfield, IL, USA) under the conditions previously described [11,12]. The identities of all peptides were confirmed by MALDI-TOF mass spectrometry using a Voyager DE PRO instrument (Applied Biosystems, Foster City, USA).…”

Section: Peptide Synthesis and Purificationmentioning

confidence: 99%

“…The more cationic PGLa-AM1 shows greater growth-inhibitory potency against Escherichia coli and Staphylococcus aureus [10] and the peptide is also active against several oral pathogens at concentrations that do not affect the viability of oral fibroblasts [11]. The possibility that PGLa-AM1 may show 5 potential for development into a drug for the treatment of T2DM is suggested by the observation that PGLa-AM1 stimulates the release of the potent incretin peptide glucagon-like peptide-1 from the GLUTag murine enteroendocrine cell line at concentrations that are not toxic to the cells [12]. The aim of the present study was to investigate the insulinotropic actions of PGLa-AM1 in vitro using BRIN-BD11rat clonal β-cells [13], 1.1B4 human-derived pancreatic β-cells [14], and dispersed isolated mouse islets and in vivo using both lean mice and mice fed a high fat diet to produce obesity and insulin resistance.…”

Section: Introductionmentioning

confidence: 99%

Actions of PGLa-AM1 and its [A14K] and [A20K] analogues and their therapeutic potential as anti-diabetic agents

Owolabi¹,

Musale²,

Ojo³

et al. 2017

Biochimie

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PGLa-AM1 (GMASKAGSVLGKVAKVALKAAL.NH) was first identified in skin secretions of the frog Xenopus amieti (Pipidae) on the basis of its antimicrobial properties. PGLa-AM1 and its [A14K] and [A20K] analogues produced a concentration-dependent stimulation of insulin release from BRIN-BD11 rat clonal β-cells without cytotoxicity at concentrations up to 3 μM. In contrast, the [A3K] analogue was cytotoxic at concentrations ≥ 30 nM. The potency and maximum rate of insulin release produced by the [A14K] and [A20K] peptides were significantly greater than produced by PGLa-AM1. [A14K]PGLa-AM1 also stimulated insulin release from mouse islets at concentrations ≥ 1 nM and from the 1.1B4 human-derived pancreatic β-cell line at concentrations > 30 pM. PGLa-AM1 (1 μM) produced membrane depolarization in BRIN-BD11 cells with a small, but significant (P < 0.05), increase in intracellular Ca concentrations but the peptide had no direct effect on K channels. The [A14K] analogue (1 μM) produced a significant increase in cAMP concentration in BRIN-BD11 cells and down-regulation of the protein kinase A pathway by overnight incubation with forskolin completely abolished the insulin-releasing effects of the peptide. [A14K]PGLa-AM1 (1 μM) protected against cytokine-induced apoptosis (p < 0.001) in BRIN-BD11 cells and augmented (p < 0.001) proliferation of the cells to a similar extent as GLP-1. Intraperitoneal administration of the [A14K] and [A20K] analogues (75 nmol/kg body weight) to both lean mice and high fat-fed mice with insulin resistance improved glucose tolerance with a concomitant increase in insulin secretion. The data provide further support for the assertion that host defense peptides from frogs belonging to the Pipidae family show potential for development into agents for the treatment of patients with Type 2 diabetes.

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Frog skin peptides (tigerinin-1R, magainin-AM1, -AM2, CPF-AM1, and PGla-AM1) stimulate secretion of glucagon-like peptide 1 (GLP-1) by GLUTag cells

Cited by 37 publications

References 37 publications

Host-Defense Peptides with Therapeutic Potential from Skin Secretions of Frogs from the Family Pipidae

Host-Defense Peptides with Therapeutic Potential from Skin Secretions of Frogs from the Family Pipidae

Review of antimicrobial peptides with anti‐Helicobacter pylori activity

Actions of PGLa-AM1 and its [A14K] and [A20K] analogues and their therapeutic potential as anti-diabetic agents

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