Disease relevance of Vsnl1

• Low level expression of calcium-sensor protein VILIP induces cAMP-dependent differentiation in rat C6 glioma cells [1].

High impact information on Vsnl1

• The calmodulin-binding region is fused to a neural visinin-like domain that contains three Ca(2+)-binding EF-hand motifs and a biotin-binding site [2].
• Neuronal calcium sensor (NCS) proteins including the subfamily of visinin-like-proteins (VILIPs) are involved in regulation of various signaling cascades [3].
• The deduced amino acid sequences of NVP-2 and NVP-3 are 89.0% and 68.6% identical to that of NVP-1, respectively, and contain consensus sequences for EF-hand Ca(2+)-binding sites [4].
• To identify additional molecular forms of NVP, a rat brain cDNA library was screened for their presence using an NVP-1 cDNA probe under low-stringency hybridization conditions [4].
• In particular, low-molecular-mass proteins, such as hippocalcin, visinin-like proteins, and 14-3-3 proteins were strongly enriched by preparative electrophoresis [5].

Biological context of Vsnl1

• These results suggest that depending on myristoylation, low level ectopic expression of VILIP affects basal cAMP homeostasis differentially, thereby influencing differentiation of C6 model cells [1].
• The calcium-binding protein VILIP in olfactory neurons: regulation of second messenger signaling [6].
• The effects of PCP on the gene expression of NVP-1, a novel Ca(2+)-binding protein, were studied in rats [7].

Anatomical context of Vsnl1

• The development of neural visinin-like Ca(2+)-binding protein 2 immunoreactivity in the rat neocortex and hippocampus [8].
• Neural visinin-like Ca(2+)-binding protein 2 (NVP2) immunoreactivity in the rat neocortex and hippocampus was barely detectable by immunoblot analysis on postnatal day 1 (P1), but increased during postnatal weeks 2-3, reaching a plateau on P28 [8].
• Calcium- and myristoyl-dependent subcellular localization of the neuronal calcium-binding protein VILIP in transfected PC12 cells [9].
• Therefore, a calcium-myristoyl switch seems to be a major, but not sole determinant for the association of VILIP with membranes in living cells [9].
• Ontogeny of visinin-like immunoreactive structures in the rat cerebellum and vestibular nuclei: an immunohistochemical analysis [10].

Associations of Vsnl1 with chemical compounds

• Delayed changes in neural visinin-like calcium-binding protein gene expression caused by acute phencyclidine administration [7].

Physical interactions of Vsnl1

• Expression of hippocalcin and neural visinin-like calcium-binding protein 2 (NVP2) in aging rat brain was investigated by immunoblot and immunohistochemical analyses [11].
• Expression of neural visinin-like calcium-binding protein 3 (NVP3) was assessed by immunoblot and immunohistochemical analyses in rat brain [12].

Regulatory relationships of Vsnl1

• Consistent with this assumption, it was found that recombinant VILIP attenuates in a calcium-dependent manner odorant-induced cAMP formation in olfactory cilia preparations [6].

Other interactions of Vsnl1

• Chimeric plant calcium/calmodulin-dependent protein kinase gene with a neural visinin-like calcium-binding domain [2].

Analytical, diagnostic and therapeutic context of Vsnl1

• Molecular cloning of two additional members of the neural visinin-like Ca(2+)-binding protein gene family [4].
• Northern blot analysis shows that NVP-1, NVP-2, and NVP-3 mRNAs are most highly expressed in brain and are differentially expressed in various regions of rat brain [4].
• Western blot analysis of subcellular fractions has shown that wild-type VILIP associates in a calcium-dependent manner with membrane fractions, whereas the myristoylation mutant only weakly associates with this fraction [9].

References