Disease relevance of VSNL1

• The neuronal calcium-sensor protein VILIP modulates cyclic AMP accumulation in stably transfected C6 glioma cells: amino-terminal myristoylation determines functional activity [1].
• Correlation of visinin-like-protein-1 expression with clinicopathological features in squamous cell carcinoma of the esophagus [2].

Psychiatry related information on VSNL1

• The anatomical distribution of the neuronal calcium sensor proteins visinin-like protein-1 and -3 (VILIP-1 and -3) was investigated in various neocortical areas of Alzheimer's disease (AD) patients and controls [3].

High impact information on VSNL1

• The neuronal Ca2+ sensor protein visinin-like protein-1 is expressed in pancreatic islets and regulates insulin secretion [4].
• The calcium sensor protein visinin-like protein-1 modulates the surface expression and agonist sensitivity of the alpha 4beta 2 nicotinic acetylcholine receptor [5].
• Chimeric Ca(2+)/calmodulin-dependent protein kinase (CCaMK) is characterized by a serine-threonine kinase domain, an autoinhibitory domain, a calmodulin-binding domain and a neural visinin-like domain with three EF-hands [6].
• The involvement of visinin (VSNL1), a promising candidate gene assigned to chromosome 2p by previous studies, has been excluded by the absence of linkage [7].
• VLP-1 was detected in plasma of patients after stroke and in cerebrospinal fluid of a rat model of stroke [8].

Chemical compound and disease context of VSNL1

• To gain insight into the function of VILIP in cell signaling, we have transfected wild-type VILIP and mutant VILIP lacking the myristoylation consensus sequence into C6 glioma cells [1].

Biological context of VSNL1

• We have mapped the VSNL1 gene to the short arm of chromosome 2 [9].
• In the course of isolation and sequence analysis of microsatellite repeat containing human cDNAs, we have isolated the human homologue of the rat visinin-like peptide gene [9].
• Functional analysis of calcium-binding EF-hand motifs of visinin-like protein-1 [10].
• We studied by immunohistochemical methods the distribution of visinin-like protein-1 (VILIP-1), which is a calcium sensor protein and at the same time a trkB mRNA binding protein, in hippocampi of nine schizophrenic patients and nine matched control subjects [11].
• A novel calcium-binding calcium/calmodulin-dependent protein kinase (CCaMK) with a catalytic domain, calmodulin-binding domain, and a neural visinin-like domain was cloned and characterized from plants [Patil et al., (1995) Proc. Natl. Acad. Sci. USA 92, 4797-4801; Takezawa et al. (1996) J. Biol. Chem. 271, 8126-8132] [12].

Anatomical context of VSNL1

• Glia did not express visinin-like proteins [13].
• The human HLP3 and 4 mRNAs are detected only in the brain and found at high amount in the cerebral cortex and cerebellum by Northern blot analysis [14].
• To study the functions of NCS proteins not expressed in photoreceptor cells we examined Visinin-like protein-1 (VILIP-1) effects on signalling pathways in living neural cells [15].
• In contrast, association of nonmyristoylated mutant VILIP with membranes was strongly reduced [1].
• Visinin-like protein-1 expression increased cGMP levels in transfected C6 and PC12 cells [15].

Associations of VSNL1 with chemical compounds

• Functional Contribution of Ca(2+) and Mg (2+) to the Intermolecular Interaction of Visinin-like Proteins [16].
• In contrast, the nonmyristoylated mutant of VILIP reduced cellular cAMP levels in C6 cells [1].
• However, VILIP expression increased the beta-adrenergic receptor-stimulated cyclic AMP (cAMP) level in these cells severalfold [1].
• In some flat-mounted preparations, glucagon- and serotonin-like reactive amacrine cells and visinin-like immunoreactive bipolar cells (distally located) could be observed [17].
• The NCS family includes NCS-1, visinin-like proteins, recoverins, guanylate cyclase-activating proteins and potassium channel-interacting proteins [18].

Other interactions of VSNL1

• Isolation of two human cDNAs, HLP3 and HLP4, homologous to the neuron-specific calcium-binding protein genes [14].
• The interaction of human visinin-like protein 1 (VILIP1) and visinin-like protein 3 (VILIP3) with divalent cations (Mg(2+), Ca(2+), Sr(2+) and Ba(2+)) was explored using circular dichroism and fluorescence measurement [16].
• Abnormal localization of two neuronal calcium sensor proteins, visinin-like proteins (vilips)-1 and -3, in neocortical brain areas of Alzheimer disease patients [3].
• The complete amino acid sequence of hippocalcin deduced from the cDNA is composed of 195 residues, has a calculated molecular mass of 22,574 daltons, and has a striking sequence homology to those of visinin, recoverin, S-modulin, neurocalcins and neural visinin-like proteins [19].

Analytical, diagnostic and therapeutic context of VSNL1

• Cell fractionation revealed cytoplasmic, membrane- and cytoskeleton-associated pools of VILIP [20].
• Ca2+-dependent mobility shift assays using E. coli-expressed protein from residues 358 520 revealed that Ca2+ binds to the visinin-like domain [21].
• Tissue specificity was tested by Western blot on a human tissue array, and a sensitive and quantitative sandwich immunoassay was developed for the most abundant gene product observed in our search, VLP-1 [8].

References