The co-existence of thyrotropin-releasing hormone (TRH)- and mesotocin (MT)-like immunoreactivities in single axon terminals in the frog pars nervosa was observed using a method combining pre-embedding peroxidase-antiperoxidase for TRH with post-embedding immunocolloidal gold staining for MT. Both TRH- and MT-like immunoreactivities were localized in the same large dense elementary granules 130-220 nm in diameter (170 nm mean diameter). A few axons contained only TRH-like immunoreactive small granular vesicles 80-120 nm in diameter (92 nm mean diameter). Axon terminals containing both TRH- and MT-like immunoreactive granules were in direct contact with the perivascular basal lamina of blood capillaries.
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http://dx.doi.org/10.1016/0304-3940(89)90367-4 | DOI Listing |
J Neurochem
January 2025
Centre for Discovery Brain Sciences, Hugh Robson Building, George Square, University of Edinburgh, Edinburgh, Scotland, UK.
Synaptic vesicle protein 2A (SV2A) is an abundant synaptic vesicle cargo with an as yet unconfirmed role in presynaptic function. It is also heavily implicated in epilepsy, firstly being the target of the leading anti-seizure medication levetiracetam and secondly with loss of function mutations culminating in human disease. A range of potential presynaptic functions have been proposed for SV2A; however its interaction with the calcium sensor for synchronous neurotransmitter release, synaptotagmin-1 (Syt1), has received particular attention over the past decade.
View Article and Find Full Text PDFMetab Brain Dis
January 2025
Ann Romney Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Hale Building for Transformative Medicine, Room 10006, 60 Fenwood Road, Boston, MA, 02115, USA.
α-Synuclein (αS) is a 140 amino-acid neuronal protein highly enriched in presynaptic nerve terminals. Its progressive accumulation in Lewy bodies and neurites is the hallmark of Parkinson's disease (PD). A growing number of studies highlights a critical interplay between lipid metabolism and αS biology.
View Article and Find Full Text PDFFront Neural Circuits
January 2025
Department of Neurobiology, Hokkaido University Graduate School of Medicine, Sapporo, Japan.
A strong repetitive stimulus can occasionally enhance axonal excitability, leading to the generation of afterdischarge. This afterdischarge outlasts the stimulus period and originates either from the physiological spike initiation site, typically the axon initial segment, or from ectopic sites for spike generation. One of the possible mechanisms underlying the stimulus-induced ectopic afterdischarge is the local depolarization due to accumulated potassium ions surrounding the axonal membranes of the distal portion.
View Article and Find Full Text PDFHeliyon
January 2025
Department of Biomolecular Sciences, University of Urbino Carlo Bo, Urbino, Italy.
Compelling evidence has demonstrated that rehabilitation through physical exercise, a non-invasive and non-surgical intervention, enhances muscle reinnervation and motor recovery after peripheral nerve injury (PNI) by increasing muscle-derived brain-derived neurotrophic factor (BDNF) expression and triggering TrkB-dependent axonal plasticity. Adenosine has been widely acknowledged to trigger TrkB via A2A receptor (A2AR). Since motor nerve terminals co-express TrkBs and A2ARs and depolarizing conditions increase muscle release of BDNF and adenosine, we examined whether A2ARs activation could recapitulate the functional recovery benefits of intermittent exercise after a nerve crush.
View Article and Find Full Text PDFNeurol Neuroimmunol Neuroinflamm
March 2025
Institute for Clinical Neurobiology, University Hospital, Julius-Maximilians-University of Würzburg, Germany.
Background And Objectives: Autoantibodies (aAbs) against glycine receptors (GlyRs) are mainly associated with the rare neurologic diseases stiff person syndrome (SPS) and progressive encephalomyelitis with rigidity and myoclonus (PERM). GlyR aAbs are also found in other neurologic diseases such as epilepsy. The aAbs bind to different GlyR α-subunits and, more rarely, also to the GlyR β-subunit.
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