Disease relevance of SNAI1

• SNAI1 mRNA was expressed in placenta, neuroblastoma, and diffuse type gastric cancer [1].
• Additionally, colon carcinomas that showed amplification of 20q13, the localization of the human SNAI1 gene, were examined [2].
• Colon cancer tissues display an increased activity of beta-galactoside alpha2,6 sialyltransferase (ST6Gal.I) and an increased reactivity with the lectin from Sambucus nigra (SNA), specific for alpha2,6-sialyl-linkages [3].
• One of the stereotyped nerves of H. medicinalis is a "sex nerve" that projects from the anterior root of ganglion 6 [SNA (6)] to the male reproductive structures in the adjacent anterior segment [4].
• CONCLUSIONS: The increase in basal levels of SNA with increasing concentrations of desflurane persisted despite "fixing" BP and thus is probably not due to hypotension and unloading of the baroreceptors [5].

Psychiatry related information on SNAI1

• Four lectins (Abrus precatorius (APA), Maackia amurensis (MAA), Momordica charantia (MCA) and Sambucus nigra (SNA)) have been used to identify glycohistochemically the microglial cells (MGC) activation in autoptic brain samples from Alzheimer's disease (AD) subjects [6].
• Altered levels of the synaptosomal associated protein SNAP-25 in hippocampus of subjects with mood disorders and schizophrenia [7].

High impact information on SNAI1

• Here we report that inhibition of transmitter release from synaptosomes caused by botulinum neurotoxin A (BoNT/A) is associated with the selective proteolysis of the synaptic protein SNAP-25 [8].
• In neuroendocrine cells, splice variants of the SNARE protein SNAP-25 and phosphorylation of SNAP-25 independently influence the size of the releasable vesicle pool, possibly by altering the rate of vesicle depriming [9].
• Overexpression of the SNARE protein SNAP-25a mutated in a PKA phosphorylation site (Thr-138) eliminated the effect of PKA inhibitors on the vesicle priming process [10].
• These data show that cardiopulmonary baroreflex control of SNA is augmented in borderline hypertensive subjects and that this augmentation does not result from an attenuation of the arterial baroreflex [11].
• Uniquely, 2 syntaxin t-SNAREs, syntaxin 2 and 4, which localize to granules and open canalicular membranes, together with the general target membrane SNAP receptor (t-SNARE) protein SNAP-23 appear to make up the heterodimeric t-SNAREs required for lysosome exocytosis [12].

Chemical compound and disease context of SNAI1

• The 35 Streptococcus suis capsular-type reference strains as well as 45 field strains of type 2 were tested with sialic acid-binding lectins from Sambucus nigra (SNA I), Triticum vulgaris, Maackia amurensis, Homarus americanus, and Limax flavus [13].

Biological context of SNAI1

• SNAI1, functioning as E-cadherin repressor, is implicated in the malignant infiltrating phenotype of diffuse type gastric cancer through the induction of EMT or fibroblastoid transformation [1].
• These results clearly indicate that SNAI1, SNAI2 and SNAI3 constitute a subfamily among SNAG zinc-finger proteins [14].
• Genomic organization, expression, and chromosome location of the human SNAIL gene (SNAI1) and a related processed pseudogene (SNAI1P) [15].
• Here, comparative genomics analyses and comparative proteomics analyses on SNAI family orthologs were performed [1].
• Because SNAI family proteins are implicated in EMT during embryogenesis and carcinogenesis, SNAI family genes are potent targets of pharmacogenomics [1].

Anatomical context of SNAI1

• The labeling of LFA and SNA showed that sialic acids existed mainly in the mucinous granules of secretory cells and ciliated epithelium glycocalyx, and in the mucous blanket [16].
• The epithelial cell (nonsecretory) surface was stained largely by WGA, LFA, SNA, RCA-I, Con-A, and LCA; this finding suggests the presence of alpha-neuraminic acid, beta-galactose, and alpha-mannose [17].
• Epithelial goblet cells were stained predominantly by WGA, LFA, SNA, RCA-I, Con-A, LCA, SBA, PHA-E, and UEA; this finding suggests they contain alpha-neuraminic acid, beta-galactose, alpha-mannose, N-acetyl alpha-galactosamine, and alpha-fucose [17].
• Antibodies neutralize sporozoites (SNA), i.e. abolish their infectivity, and cause, in vitro, the formation of a thread-like precipitate on the parasites (CSP reaction) [18].
• Heart rate (HR; measured by electrocardiograph), blood pressure (BP; measured by arterial catheter), and efferent sympathetic nerve activity (SNA; obtained from percutaneous recordings from the peroneal nerve) were monitored [5].

Associations of SNAI1 with chemical compounds

• Moreover, the same treatment of Neu5Ac(alpha 2-3)lactitol also abolished its ability to inhibit the precipitation reaction, suggesting that the glyceryl side chain of NBu5Ac (especially the C-8 and/or C-9 portion) is an important determinant for SNA [19].
• Conversion of the Neu5Ac residue to its 7-carbon analogue by selective periodate oxidation of its glyceryl side chain, followed by NaBH4 reduction, completely destroyed the ability of fetuin and orosomucoid to precipitate with SNA [19].
• The alpha2,6 sialic acid was detected by elderberry bark lectin (SNA), the exposure of terminal galactose (Gal) and N-acetylgalactosamine (GalNAc) were detected by arachis hypogaea [peanut agglutinin (PNA)] and vilsa villosa lectin (VVL), respectively [20].
• The long latency 5-HT-evoked increase in BAT SNA was prevented by microinjection of methysergide (600 pmol) into the T4 IML [21].
• The 5-HT-mediated potentiation of the increase in BAT SNA evoked by microinjection of NMDA into the T4 IML was reversed by microinjection of methysergide (600 pmol) into the T4 IML [21].

Other interactions of SNAI1

• Those cases were partly analyzed for mRNA expression of N-cadherin (42 cases), TWIST (18 cases), SNAI1 (25 cases) and SIP1 (25 cases) by real-time quantitative RT-PCR [2].
• While human SLUG has been mapped to 8q (Cohen, M.E., Yin, M., Paznekas, W.A., Schertzer, M., Wood, S., Jabs, E.W., 1998. Human SLUG organisation, expression and chromosome map location on 8q. Genomics 51, 468-471), the human sna gene SNA, was previously unmapped [22].
• However, the DRM-associated fraction of the novel protein C8ORF2 ( approximately 5% of total protein) associated with immunoseparated caveolae, in contrast with the raft protein SNAP-23 [23].
• In particular, the hippocampus exhibits reduced levels of synaptophysin and the SNARE protein SNAP-25 [24].
• Our recent findings implicate the SNAP receptor (SNARE) protein SNAP-23 and secretory carrier membrane protein 2 (SCAMP2) as regulators of this process [25].

Analytical, diagnostic and therapeutic context of SNAI1

• We have used sequence similarity to the Fugu genes to identify a human SNA EST and mapped this by radiation hybrid and physical mapping to the distal end of human 20q [22].
• Western blot analysis revealed a strikingly heterogeneous pattern of SNA reactivity among cancer tissues [3].
• Site-directed mutagenesis was used to mimic the conversion of the highly active B-chain of fruit-specific SNA (SNA-If) into the completely inactive B-chain of the closely related and naturally occurring loss-of-activity mutant called S. nigra agglutinin lectin-related protein [26].
• In a multiple regression correlation analysis MP-H, SNB (angle from sella to nasion to subspinale point), SNA (angle from sella to nasion to supramentale point), PAS (posterior airway space), tongue size, and body mass index contributed significantly to the equation explaining the severity of sleep apnoea [27].
• Those derived from SW 948 xenografts showed an enrichment of round, non-adherent cells, strongly reactive with the NeuAc alpha 2,6 Gal/GalNAc-specific lectin from Sambucus nigra (SNA), thus indicating that a selection of these cells has occurred [28].

References