High impact information on SNPH

• Syntaphilin competes with SNAP-25 for binding to syntaxin-1 and inhibits SNARE complex formation by absorbing free syntaxin-1 [1].
• These findings suggest that syntaphilin may function as a molecular clamp that controls free syntaxin-1 availability for the assembly of the SNARE complex, and thereby regulates synaptic vesicle exocytosis [1].
• Furthermore, introduction of syntaphilin into presynaptic superior cervical ganglion neurons in culture inhibits synaptic transmission [1].
• Phosphorylation of syntaphilin by cAMP-dependent protein kinase modulates its interaction with syntaxin-1 and annuls its inhibitory effect on vesicle exocytosis [2].
• To determine whether PKA phosphorylation of syntaphilin is involved in the regulation of Ca(2+)-dependent exocytosis, we investigated the effect of overexpression of syntaphilin and its S43D mutant on the regulated secretion of human growth hormone from PC12 cells [2].

Biological context of SNPH

• Our data predict that syntaphilin could be a highly regulated molecule and that PKA phosphorylation could act as an "off" switch for syntaphilin, thus blocking its inhibitory function via the cAMP-dependent signal transduction pathway [2].
• Here, we identify one possible target: syntaphilin, which was identified as a molecular clamp that controls free syntaxin-1 and dynamin-1 availability and thereby regulates synaptic vesicle exocytosis and endocytosis [2].
• Molecular cloning and characterization of gene for Golgi-localized syntaphilin-related protein on human chromosome 8q23 [3].

Anatomical context of SNPH

• Although expression of wild type syntaphilin in PC12 cells exhibits significant reduction in high K(+)-induced human growth hormone release, the S43D mutant fails to inhibit exocytosis [2].
• Treatment of rat brain synaptosomes or syntaphilin-transfected HEK 293 cells with the cAMP analogue BIMPS induces in vivo phosphorylation of syntaphilin and inhibits its interaction with syntaxin-1 in neurons [2].
• Immunohistochemical study of m-Golsyn protein showed its prominent expression in the neuronal cells in various regions of the brain and strong expression in the choroid plexus ependymal cells lining the ventricles. m-Golsyn protein was found to be homologous to syntaphilin, a regulator of synaptic vesicle exocytosis [4].

Associations of SNPH with chemical compounds

• A syntaphilin mutation of serine 43 to aspartic acid (S43D) shows similar effects on binding [2].

Other interactions of SNPH

• A regeneration system of G-6-p and G-6-PD was used for reducing the PL-SNP+ to PL-SNPH [5].

Analytical, diagnostic and therapeutic context of SNPH

• METHODS: In a single-center retrospective study, 231 adjustable valves (range, 30-200 mm H(2)O) were the first shunt implantations in 147 patients with idiopathic NPH (INPH) and 71 patients with secondary NPH (SNPH) [6].

References