PE-11, a peptide derived from chromogranin B, in the human brain

Marksteiner, Josef; Bauer, Richard; Kaufmann, Walter A.; Weiss, Elisabeth M.; Barnas, Usso; Maier, Hans

doi:10.1016/s0306-4522(98)00676-9

Cited by 31 publications

(18 citation statements)

References 45 publications

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“…Of 30 distinct fragments detected in two previous studies, 10 represent cleavage at nonbasic sites and six represent cleavage at basic sites that do not fit the PC consensus sequence (27,39). Other studies detected an Nterminally extended form of PE-11 (23,40,41). However, there are no PC consensus sites within chromogranin B that would produce a peptide of the observed size, suggesting a novel cleavage site.…”

Section: Discussionmentioning

confidence: 87%

Identification of peptides from brain and pituitary of Cpe ^fat /Cpe ^fat mice

Fei

Lin

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

131

157

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Cpe fat ͞Cpe fat mice have a naturally occurring point mutation within the carboxypeptidase E gene that inactivates this enzyme, leading to an accumulation of many neuroendocrine peptides containing C-terminal basic residues. These processing intermediates can be readily purified on an anhydrotrypsin affinity resin. Using MS to obtain molecular mass and partial sequence information, more than 100 peptides have been identified. These peptides represent fragments of 16 known secretory pathway proteins, including proenkephalin, proopiomelanocortin, protachykinins A and B, chromogranin A and B, and secretogranin II. Many of the identified peptides represent previously uncharacterized fragments of the precursors. For example, 12 of the 13 chromogranin B-derived peptides found in the present study have not been previously reported. Of these 13 chromogranin B-derived peptides, only five contain consensus cleavage sites for prohormone convertases at both the C and N termini. Two distinct chromogranin B-derived peptides result from cleavage at Trp-Trp bonds, a site not typically associated with neuropeptide processing. An RIA was used to confirm that one of these peptides, designated WE-15, exists in wild-type mouse brain, thus validating the approach to identify peptides in Cpe fat ͞Cpe fat mice. These ''orphan'' peptides are candidate ligands for orphan G protein-coupled receptors. In addition, the general technique of using affinity chromatography to isolate endogenous substrates from a mutant organism lacking an enzyme should be applicable to a wide range of enzymesubstrate systems.peptide processing ͉ carboxypeptidase E ͉ carboxypeptidase D ͉ chromogranin ͉ secretogranin

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Section: Discussionmentioning

confidence: 87%

Identification of peptides from brain and pituitary of Cpe ^fat /Cpe ^fat mice

Fei

Lin

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

131

157

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“…There are limited data available on the distribution of chromogranins, on the protein level in the rat and human hippocampus, and on epilepsy-induced alterations (4)(5)(6)(7)(8)(9). The goal of the present study was to investigate changes Address correspondence and reprint requests to Dr. Susanne Kandlhofer at Department of Neurosurgery, University of Vienna, Wahringer Gurtel 18-20, A-1090 Vienna, Austria.…”

Section: Conclusion: Chromograninsmentioning

confidence: 99%

Chromogranins in Temporal Lobe Epilepsy

et al. 2000

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Summary:Purpose: Chromogranins are neuropeptide precursors stored in large dense core vesicles. Because physiological functions have been postulated for peptides originating from chromogranins, we investigated the distribution of chromogranins A and B and secretoneurin (a peptide derived from secretogranin 11) in the control and epileptic hippocampus of humans and rats.Methods: Chromogranin immunoreactivity (IR) was investigated in paraformaldehyde-fixed hippocampal specimens from 24 temporal lobe epilepsy patients with intractable seizures, postmortem from 15 patients deceased from nonneurological disorders, in rats 30 days after kainate-induced limbic seizures, and in control rats.Results: In control rats and in humans, chromogranin A and B IR and secretoneurin IR were present in mossy fibers. In addition, chromogranin B IR was found in granule cells, and chromogranin A IR was found in granule and CA2 pyramidal cells in the human hippocampus. In both species, chromogranin B and secretoneurin were unevenly distributed in the molecular layer of the dentate gyrus. The most intriguing change seen in human temporal lobe epilepsy specimens and in the kainic acid model of the rat was the prominent staining of the inner molecular layer, indicating storage of chromogranins A and B and secretoneurin in terminals of reorganized mossy fibers, from which they may be released upon nerve stimulation. Chromogranins are acidic polypeptides with a wide distribution in the nervous and endocrine systems. They are named for their first isolation in secretory granules of chromaffine cells in the adrenal medulla (1). Members of this family are chromogranin A (CgA), chromogranin B (CgB), and secretogranin 11. They are stored in large dense core vesicles in which they are processed to smaller peptides (e.g., secretogranin I1 is processed to secretoneurin). Like classic neuropeptides, chromogranins are thought to be released upon neuronal stimulation and may exert their physiological functions at that time. Conclusion: ChromograninsIn the kainic acid model of temporal lobe epilepsy (TLE), marked changes in CgA and CgB messenger RNA (mRNA) levels were observed in granule cells of the dentate gyrus and in secretogranin I1 mRNA in pyramidal cells (2,3), suggesting a role for chromogranins in experimental epilepsy.There are limited data available on the distribution of chromogranins, on the protein level in the rat and human hippocampus, and on epilepsy-induced alterations (4-9). The goal of the present study was to investigate changes Address correspondence and reprint requests to Dr. Susanne Kandlhofer at Department of Neurosurgery, University of Vienna, Wahringer Gurtel 18-20, A-1090 Vienna, Austria. E-mail: susanne.pirker@univie.ac.at in the distribution of chromogranins in the kainic acid model and in surgical specimens of TLE patients and to evaluate chromogranins as possible markers for hippocampal structures. MATERIALS AND METHODS The kainic acid model of temporal lobe epilepsyRats were injected with kainic acid (KA; 10 mgkg intrap...

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“…Granules were lysed by successive freezing and thawing in 10 mm Tris/HCl, pH 7.4 and the granule membranes were removed by centrifugation at 100 000 g for 30 min. The resulting supernatant was boiled immediately to inactivate proteinases [23] and the boiled extracts were centrifuged at 100 000 g, for 45 min before purification. Proteinase inhibitor (aprotinin) was included in all solutions.…”

Section: Preparation Of Chromaffin Granule Lysatementioning

confidence: 99%

“…Although many studies have been carried out on the biochemical properties [12] and the cellular distribution of CgB [13,14], its precise function remains an open question.…”

mentioning

confidence: 99%

Identification and characterization of novel chromogranin B-derived peptides from porcine chromaffin granules by liquid chromatography/electrospray tandem MS

Wang¹,

Vandenberghe²,

Depreitere³

et al. 2001

Eur J Biochem

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Chromogranin B (CgB) is a regulated secretory protein that is stored in endocrine and neuroendocrine cells. It can be processed proteolytically to small peptide fragments. In the present study three proteolytic products of porcine CgB were obtained after size-exclusion, immunoaffinity, and reversed-phase chromatography, and then identified by electrospray tandem MS. One novel peptide was identified as S586±R602 and is phosphorylated at one or two serine residues. Another novel peptide H603±Q636 (HQ-34), with molecular mass 3815.56 Da, was found to be oxidized at the methionine residue. In addition, a secretolytin-like peptide fragment (KR-11), which is two amino acids shorter than the bovine secretolytin, was found. This is the first report that the C-terminal region of CgB, the homologue of human CCB, is proteolytically processed further into three small peptide fragments.

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PE-11, a peptide derived from chromogranin B, in the human brain

Cited by 31 publications

References 45 publications

Identification of peptides from brain and pituitary of Cpe ^fat /Cpe ^fat mice

Identification of peptides from brain and pituitary of Cpe ^fat /Cpe ^fat mice

Chromogranins in Temporal Lobe Epilepsy

Identification and characterization of novel chromogranin B-derived peptides from porcine chromaffin granules by liquid chromatography/electrospray tandem MS

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PE-11, a peptide derived from chromogranin B, in the human brain

Cited by 31 publications

References 45 publications

Identification of peptides from brain and pituitary of Cpe fat /Cpe fat mice

Identification of peptides from brain and pituitary of Cpe fat /Cpe fat mice

Chromogranins in Temporal Lobe Epilepsy

Identification and characterization of novel chromogranin B-derived peptides from porcine chromaffin granules by liquid chromatography/electrospray tandem MS

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Product

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Identification of peptides from brain and pituitary of Cpe ^fat /Cpe ^fat mice

Identification of peptides from brain and pituitary of Cpe ^fat /Cpe ^fat mice