Victoria Stöckl , Georgios Blatsios , Christian Humpel , Zenon Pidsudko , Vincenzo Provitera , Germar-Michael Pinggera , Teresa Rauchegger , Josef Troger
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引用次数: 0
Abstract
Aim
The chromogranin A-derived peptide catestatin has previously been shown to be a constituent of the sensory innervation of the eye and dental pulp. The antibody used in these studies not only recognizes authentic catestatin but also larger molecules containing the sequence of catestatin. Therefore, the authors now aimed to explore whether there are additional molecular forms present in the rat skin, rat trigeminal ganglion and rat dorsal root ganglia apart from free catestatin.
Methods
Western blot analysis was performed in these tissues and and double immunofluorescence techniques in rat dorsal root ganglia.
Results
A very prominent band was found at approximately 50 kDa in the skin representing a middle-sized fragment containing the sequence of this peptide. Recently, the same result has been obtained in the dental pulp indicating that this fragment might represent a main molecular form in various other tissues of the body. It is likely of sensory nature since the band was also present of weaker intensity both in the trigeminal ganglion and dorsal root ganglia and since abundant cells expressed catestatin-like immunoreactivity in rat dorsal root ganglia. Another small sized fragment of weaker intensity was found in these tissues as well. No band was observed in the position of intact chromogranin A in the Western blot.
Conclusion
Chromogranin A is proteolytically processed in sensory ganglia to at least two fragments containing the sequence of catestatin which are then anterogradely transported to the skin and the 50 kDa fragment obviously becomes aggregated there in nerve endings.
期刊介绍:
The aim of Neuropeptides is the rapid publication of original research and review articles, dealing with the structure, distribution, actions and functions of peptides in the central and peripheral nervous systems. The explosion of research activity in this field has led to the identification of numerous naturally occurring endogenous peptides which act as neurotransmitters, neuromodulators, or trophic factors, to mediate nervous system functions. Increasing numbers of non-peptide ligands of neuropeptide receptors have been developed, which act as agonists or antagonists in peptidergic systems.
The journal provides a unique opportunity of integrating the many disciplines involved in all neuropeptide research. The journal publishes articles on all aspects of the neuropeptide field, with particular emphasis on gene regulation of peptide expression, peptide receptor subtypes, transgenic and knockout mice with mutations in genes for neuropeptides and peptide receptors, neuroanatomy, physiology, behaviour, neurotrophic factors, preclinical drug evaluation, clinical studies, and clinical trials.