High impact information on Snap29

• Resealing was also inhibited by botulinum neurotoxins B and A, suggesting that the two synaptosomal-associated proteins synaptobrevin and SNAP-25 also participate in resealing [1].
• The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations [2].
• One is Snapin, a coiled-coil-forming protein previously characterized as a binding partner of synaptosomal-associated proteins 25 and 23 and implicated in the regulation of membrane fusion events [3].
• Botulinum neurotoxin type E inhibited 55% of the KCl-induced Ca2+-dependent glutamate release, followed by specific cleavage of 25 kDa synaptosomal-associated protein [4].
• SNAP-25 is a synaptosomal associated protein localized at the plasma membrane of nerve terminals [5].

Biological context of Snap29

• We therefore determined hippocampal expression of signaling proteins, transcription factors and synaptosomal-associated proteins representing key elements of neuronal plasticity in mice following behavioral training [6].
• Protein samples were examined for changes in SNAP-25 (synaptosomal-associated protein of Mr = 25 kDa) using immunochemistry [7].

Anatomical context of Snap29

• SNAP-25 (synaptosomal associated protein of 25 kDa) is a neural specific protein that has been implicated in the synaptic vesicle docking and fusion process [8].

Associations of Snap29 with chemical compounds

• BoNT/A is a Zn(2+) endopeptidase which selectively cleaves SNAP-25 (synaptosomal-associated protein of 25 kDa), a critical component of the exocytotic machinery [9].
• Syntaxin and 25-kDa synaptosomal-associated protein: differential effects of botulinum neurotoxins C1 and A on neuronal survival [10].

Other interactions of Snap29

• We examined if two alternatively spliced variants of synaptosomal-associated protein of 25 kD, SNAP-25a and SNAP-25b, possessed distinct cellular distribution if coexpressed within the same neuroblastoma cell [11].

Analytical, diagnostic and therapeutic context of Snap29

• In the present work we have investigated the presence of the membrane proteins Syntaxin-1 and synaptosomal-associated protein (SNAP-25) by immunohistochemistry in the different parts of the pituitary of mouse, guinea pig and cat [12].

References