#Poser pro 2014 v10.0.3 Activator

In fact, it has been shown that sorcin interacts with presenilin 2, a component of the γ-secretase, which is involved in the generation of 39–42 amino acid amyloid-β peptides (Aβ) from cleavage of the Aβ protein precursor in Alzheimer’s disease (AD). Increasing evidences highlight the association of sorcin with neurodegeneration. Sorcin is also able to increase mitochondrial Ca 2+ concentration. In the plasma membrane, sorcin modulates the L-type Ca 2+ channels and activates the Na +–Ca 2+ exchangers. Sorcin interacts and inhibits the ryanodine receptor and activates the sarco(endo)plasmic reticulum Ca 2+ ATPase isoform SERCA2a, thereby promoting Ca 2+ accumulation in the ER. The involvement of sorcin in apoptosis and in metastasis of several cancer types has also been described.

Through the binding of Ca 2+ to sorcin, this protein plays a significant role in cancer cells, and in the regulation of angiogenesis, mitosis and endoplasmic reticulum (ER) stress, as revised in Colotti et al. Binding of calcium ions (Ca 2+) is essential to translocate sorcin from the cytoplasm to the cell membrane, and there it can interact with other membrane proteins involved in Ca 2+ homeostasis. Mass spectrometry analysis and database searching have revealed that sorcin is widely expressed in most human tissues, such as skeletal muscle, kidney, brain, cardiac muscle, breast and skin, and it is overexpressed in a variety of human tumors and human cancer cell lines. There are two main isoforms, the 22 kDa isoform which is the most abundant one and is found in the cytosol, and the 18 kDa isoform, which is localized in the mitochondria.

The soluble resistance-related calcium-binding protein (sorcin) is a member of the penta EF-hand family.

#Poser pro 2014 v10.0.3 Activator

Results show sorcin as an activator of PMCA, which also prevents the inhibitory effects of Aβ and tau on the pump, and counteracts the neurotoxicity of Aβ and tau by interacting with them. The present work focuses on sorcin in search of new regulators of PMCA and antagonists of Aβ and tau toxicity. Sorcin has been shown to interact with the intracellular sarco(endo)plasmic reticulum Ca 2+-ATPase (SERCA), and other modulators of intracellular Ca 2+ signaling, such as the ryanodine receptor or presenilin 2, which is closely associated with AD.

On the other hand, sorcin is a Ca 2+-binding protein highly expressed in the brain, although its mechanism of action is far from being clear. In previous work, we have shown that plasma membrane Ca 2+-ATPase (PMCA), a high-affinity Ca 2+ pump, is functionally impaired in AD and is inhibited by amyloid-β peptide (Aβ) and tau, two key components of pathological AD hallmarks. Since dysregulation of intracellular calcium (Ca 2+) levels is a common occurrence in neurodegenerative diseases, including Alzheimer’s disease (AD), the study of proteins that can correct neuronal Ca 2+ dysregulation is of great interest.