Peptide α‐amidation activity in human plasma: relationship to gastrin processing

Kapuscinski, Mirek; Green, Michelle; Sinha, Sankar Narayan; Shepherd, J. J.; Shulkes, Arthur

doi:10.1111/j.1365-2265.1993.tb01750.x

Cited by 12 publications

(12 citation statements)

References 24 publications

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“…Molecular masses (average) and pI were calculated using http://www.expasy.org/tools/protparam.html basic residue-specific carboxypeptidase. In a second step, the remaining glycine-extended peptide would be converted into a des-Gly peptide amine by a-amidation [28]. A similar amidation signal of X-Gly-Arg/Lys-Arg/Lys is also found in scorpion toxins [29,30].…”

Section: Discussionmentioning

confidence: 99%

Ctenidins: antimicrobial glycine-rich peptides from the hemocytes of the spider Cupiennius salei

Baumann

Kämpfer

Schürch

et al. 2010

Cell. Mol. Life Sci.

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Three novel glycine-rich peptides, named ctenidin 1-3, with activity against the Gram-negative bacterium E. coli, were isolated and characterized from hemocytes of the spider Cupiennius salei. Ctenidins have a high glycine content (>70%), similarly to other glycine-rich peptides, the acanthoscurrins, from another spider, Acanthoscurria gomesiana. A combination of mass spectrometry, Edman degradation, and cDNA cloning revealed the presence of three isoforms of ctenidin, at least two of them originating from simple, intronless genes. The full-length sequences of the ctenidins consist of a 19 amino acid residues signal peptide followed by the mature peptides of 109, 119, or 120 amino acid residues. The mature peptides are post-translationally modified by the cleavage of one or two C-terminal cationic amino acid residue(s) and amidation of the newly created mature C-terminus. Tissue expression analysis revealed that ctenidins are constitutively expressed in hemocytes and to a small extent also in the subesophageal nerve mass.

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Section: Discussionmentioning

confidence: 99%

Ctenidins: antimicrobial glycine-rich peptides from the hemocytes of the spider Cupiennius salei

Baumann

Kämpfer

Schürch

et al. 2010

Cell. Mol. Life Sci.

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“…The failure of oleoylglycine administration to increase serum oleamide concentration was unexpected and suggests that the PAM normally present in the circulation [31,32] may not be enzymatically active within this environment. This conclusion is based upon the assumption that intraperitoneally administered oleoylglycine is absorbed into the circulation, as seen here with oleamide.…”

Section: Discussionmentioning

confidence: 99%

In vivo evidence that N-oleoylglycine acts independently of its conversion to oleamide

Chaturvedi

Driscoll

Elliot

et al. 2006

Prostaglandins & Other Lipid Mediators

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Oleamide (cis-9-octadecenamide) is a member of an emerging class of lipid-signaling molecules, the primary fatty acid amides. A growing body of evidence indicates that oleamide mediates fundamental neurochemical processes including sleep, thermoregulation, and nociception. Nevertheless, the mechanism for oleamide biosynthesis remains unknown. The leading hypothesis holds that oleamide is synthesized from oleoylglycine via the actions of the peptide amidating enzyme, peptidylglycine alpha amidating monooxygenase (PAM). The present study investigated this hypothesis using pharmacologic treatments, physiologic assessments, and measurements of serum oleamide levels using a newly development enzyme-linked immunosorbant assay (ELISA). Oleamide and oleoylglycine both induced profound hypothermia and decreased locomotion, over equivalent dose ranges and time courses, whereas, closely related compounds, stearamide and oleic acid, were essentially without effect. While the biologic actions of oleamide and oleoylglycine were equivalent, the two compounds differed dramatically with respect to their effects on serum levels of oleamide. Oleamide administration (80 mg/kg) elevated blood-borne oleamide by eight-fold, whereas, the same dose of oleoylglycine had no effect on circulating oleamide levels. In addition, pretreatment with the established PAM inhibitor, disulfiram, produced modest reductions in the hypothermic responses to both oleoylglycine and oleamide, suggesting that the effects of disulfiram were not mediated through inhibition of PAM and a resulting decrease in the formation of oleamide from oleoylglycine. Collectively, these findings raise the possibilities that: (1) oleoylglycine possesses biologic activity that is independent of its conversion to oleamide, and (2) the increased availability of oleoylglycine as a potential substrate does not drive the biosynthesis of oleamide.

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“…However, the amino acid sequence of the isolated GLWamide-like peptide (Val-His-Leu-Thr-Asp-Ala-Glu-LysAla-Ala-Val-Asn-Gly-Leu-Trp-NH 2 ) completely corresponds to an N-terminal fragment of rat beta-globin. Although this peptide has an amidated C-terminal end, we cannot rule out the possibility that the peptide is artificially converted, by alpha-amidation activity in plasma or cerebrospinal fluid (Kapuscinski et al 1993;Wand et al 1985), from an N-terminal 2-16 fragment of beta-globin with a C-terminal glycine residue during the purification process. Further studies will be required to identify authentic mammalian GLW-amide-like peptides.…”

Section: Discussionmentioning

confidence: 95%

Immunohistochemical evidence for the existence of novel mammalian neuropeptides related to the Hydra GLW-amide neuropeptide family

et al. 2009

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The GLW-amide family is a neuropeptide family found in cnidarian species and is characterized by the C-terminal amino acid sequence -Gly-Leu-Trp-NH(2). To detect mammalian peptides structurally related to the GLW-amide family, we examined rat brain by immunohistochemistry with an anti-GLW-amide antibody. GLW-amide-like immunoreactivity (GLW-amide-LI) was observed in thin varicose fibers in some regions of the brain. Most neurons showing GLW-amide-LI were observed in the laterodorsal tegmental nucleus, pedunculopontine tegmental nucleus, and trigeminal/spinal ganglia. These results strongly suggest that the rat nervous system contains as yet unidentified GLW-amide-like peptides, and that GLW-amide-LI in the brain is a good marker for ascending projections from mesopontine cholinergic neurons.

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Peptide α‐amidation activity in human plasma: relationship to gastrin processing

Abstract: The results support the view that gastrin is amidated at the site of its synthesis and that hypergastrinaemia is associated with elevated plasma amidating enzyme activity only when the gastrin originates from tumour sources.

Cited by 12 publications

References 24 publications

Ctenidins: antimicrobial glycine-rich peptides from the hemocytes of the spider Cupiennius salei

Ctenidins: antimicrobial glycine-rich peptides from the hemocytes of the spider Cupiennius salei

In vivo evidence that N-oleoylglycine acts independently of its conversion to oleamide

Immunohistochemical evidence for the existence of novel mammalian neuropeptides related to the Hydra GLW-amide neuropeptide family

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