Pyroglutamate-Amyloid-β and Glutaminyl Cyclase Are Colocalized with Amyloid-β in Secretory Vesicles and Undergo Activity-Dependent, Regulated Secretion | Zendy

Holger Cynis | Zendy; Lydiane Funkelstein | Zendy; Thomas Toneff | Zendy; Charles Mosier | Zendy; Michael G. Ziegler | Zendy; Birgit C. P. Koch | Zendy; HansUlrich Demuth | Zendy; Vivian Hook | Zendy

Open Access

Pyroglutamate-Amyloid-β and Glutaminyl Cyclase Are Colocalized with Amyloid-β in Secretory Vesicles and Undergo Activity-Dependent, Regulated Secretion

Author(s) -

Holger Cynis,

Lydiane Funkelstein,

Thomas Toneff,

Charles Mosier,

Michael G. Ziegler,

Birgit C. P. Koch,

HansUlrich Demuth,

Vivian Hook

Publication year - 2014

Publication title -

neurodegenerative diseases

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.98

H-Index - 57

eISSN - 1660-2862

pISSN - 1660-2854

DOI - 10.1159/000358430

Subject(s) - secretion , medicine , endocrinology , neuropeptide , neurotransmitter , amyloid (mycology) , catecholamine , neurodegeneration , colocalization , chemistry , secretory vesicle , biology , exocytosis , microbiology and biotechnology , central nervous system , receptor , inorganic chemistry , disease

N-truncated pyroglutamate (pGlu)-amyloid-β [Aβ(3-40/42)] peptides are key components that promote Aβ peptide accumulation, leading to neurodegeneration and memory loss in Alzheimer's disease. Because Aβ deposition in the brain occurs in an activity-dependent manner, it is important to define the subcellular organelle for pGlu-Aβ(3-40/42) production by glutaminyl cyclase (QC) and their colocalization with full-length Aβ(1-40/42) peptides for activity-dependent, regulated secretion. Therefore, the objective of this study was to investigate the hypothesis that pGlu-Aβ and QC are colocalized with Aβ in dense-core secretory vesicles (DCSV) for activity-dependent secretion with neurotransmitters.

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