Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Proteolytic processing of chromogranins is modified in brains of transgenic mice.

Annals of the New York Academy of Sciences - 1 Oct 2002

Laslop Andrea, Becker Alexandra, Lindberg Iris, Fischer-Colbrie Reiner

Abstract excerpt

In normal brain, secretogranin II and chromogranins A and S are extensively converted by endopeptidases to the peptides secretoneurin, GE-19, and PE-11, respectively. After genetic knockout of PC2 or its helper protein 7B2, but not after mutation of carboxypeptidase E, endoproteolytic processing decreased, as indicated by appearance of intermediate-sized processing products.

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Aspartic Acid Endopeptidases
Share to Carboxypeptidases
Share to Chromatography, Gel

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Chromogranins

Share to Endopeptidases

Share to Pituitary Hormones

Share to Proprotein Convertases

Share to Subtilisins

Source

Identifiers

PMID: 12438088
DOI: 10.1111/j.1749-6632.2002.tb04432.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Proteolytic processing of chromogranins is modified in brains of transgenic mice.PMID 12438088Read ↗

Prohormone convertase 7 is necessary for the normal processing of cholecystokinin in mouse brain.Semantic proximity Read ↗

Disruption of PC1/3 expression in mice causes dwarfism and multiple neuroendocrine peptide processing defectsSemantic proximity Read ↗

Knock-out mouse models of proprotein convertases: unique functions or redundancy?Semantic proximity Read ↗

Tachykinins Processing is Significantly Impaired in PC1 and PC2 Mutant Mouse Spinal Cord S9 Fractions.Semantic proximity Read ↗

Dissociated phenotypes in presenilin transgenic mice define functionally distinct gamma-secretases.Semantic proximity Read ↗

Altered neuropeptide profile of Caenorhabditis elegans lacking the chaperone protein 7B2 as analyzed by mass spectrometry.Semantic proximity Read ↗

Chromogranins A and B are key proteins in amine accumulation, but the catecholamine secretory pathway is conserved without them.Semantic proximity Read ↗

Endoproteolysis of Presenilin 1 and Accumulation of Processed Derivatives In VivoSemantic proximity Read ↗

Neuronal over-expression of chromogranin A accelerates disease onset in a mouse model of ALS.Semantic proximity Read ↗

Post-translational processing of proopiomelanocortin (POMC) in mouse pituitary melanotroph tumors induced by a POMC-simian virus 40 large T antigen transgene.Semantic proximity Read ↗

Deficiency of prolyl oligopeptidase in mice disturbs synaptic plasticity and reduces anxiety-like behaviour, body weight, and brain volume.Semantic proximity Read ↗

Mutations in the catalytic domain of prohormone convertase 2 result in decreased binding to 7B2 and loss of inhibition with 7B2 C-terminal peptide.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.