The Effect of Photobiomodulation on Human Mesenchymal Cells: A Literature Review.

Background: Mesenchymal stem cell-based therapy is known to have the potential to induce angiogenesis. However, there are still some limitations regarding their clinical application. Photomodulation/photobiomodulation is non-invasive and non-toxic phototherapy able to stimulate cell viability, proliferation, differentiation, and migration, when the right irradiation parameters are applied.

PTEN suppresses axon outgrowth by down-regulating the level of detyrosinated microtubules.

Inhibition of the phospholipid phosphatase and tumor suppressor PTEN leads to excessive polarized cell growth during directed cell migration and neurite outgrowth. These processes require the precise regulation of both the actin and microtubule cytoskeleton. While PTEN is known to regulate actin dynamics through phospholipid modulation, whether and how PTEN regulates microtubule dynamics is unknown.

Excitotoxicity induced by kainic acid provokes glycogen synthase kinase-3 truncation in the hippocampus.

In neuronal cultures, glycogen synthase kinase 3(GSK3) is truncated at the N-terminal end by calpain downstream of activated glutamate receptors. However, the in vivo biological significance of that truncation has not been explored. In an attempt to elucidate if GSK3 truncation has a pathophysiological relevance, we have used intraperitoneal injections of kainic acid (KA) in rats and intra-amygdala KA microinjections in mice as in vivo models of excitotoxicity.

Calpain regulates N-terminal interaction of GSK-3β with 14-3-3ζ, p53 and PKB but not with axin.

Calpain produces a truncation of GSK3β that removes the N-terminal inhibitory domain. Here we analyze the effect of that truncation on protein-protein interaction. We pulled down GST-tagged proteins in the presence of full length GSK-3β and calpain-cleaved GSK-3β.

Memantine inhibits calpain-mediated truncation of GSK-3 induced by NMDA: implications in Alzheimer's disease.

Deregulation of glycogen synthase kinase-3 (GSK-3) activity is believed to play a key role in the pathogenesis of Alzheimer's disease (AD). GSK-3 activity is regulated by phosphorylation and through interaction with GSK-3-binding proteins. Previously, we demonstrated that calpain activation produces a truncation of GSK-3.

Calpain-mediated truncation of GSK-3 in post-mortem brain samples.

GSK-3 activity can be regulated by phosphorylation and through interaction with GSK-3-binding proteins. In addition, we have recently demonstrated that calpain activation produces a truncation of GSK-3 that removes the N-terminal inhibitory domain (Goñi-Oliver et al. [2007] J.

Role of polyglycine repeats in the regulation of glycogen synthase kinase activity.

Glycogen synthase kinase (GSK3) activity present in one cell is the consequence of the sum of the activities of two different proteins called GSK3alpha and GSK3beta. These isoenzymes are coded by two different genes and share an almost identical sequence at their catalytic domain, but differ in the sequence of putative regulatory regions. In this review, we propose that glycine repeats present only in GSK3alpha may result in the different cleavage of both isoenzymes by the protease calpain, a cleavage that modifies GSK3 activity.

Tau as a molecular marker of development, aging and neurodegenerative disorders.

The purpose of this work is to review the changes that take place in the microtubule associated protein tau during neuronal development, aging and neurodegeneration. Human tau protein is expressed from a single gene located on chromosome 17. The DNA is transcribed into nuclear RNA and this RNA, by alternative splicing, yields different mRNA species which are developmentally regulated.

N-terminal cleavage of GSK-3 by calpain: a new form of GSK-3 regulation.

Although GSK-3 activity can be regulated by phosphorylation and through interaction with GSK-3-binding proteins, here we describe N-terminal proteolysis as a novel way to regulate GSK-3. When brain extracts were exposed to calcium, GSK-3 was truncated, generating two fragments of approximately 40 and 30 kDa, a proteolytic process that was inhibited by specific calpain inhibitors. Interestingly, instead of inhibiting this enzyme, GSK-3 truncation augmented its kinase activity.

Chronic lithium administration to FTDP-17 tau and GSK-3beta overexpressing mice prevents tau hyperphosphorylation and neurofibrillary tangle formation, but pre-formed neurofibrillary tangles do not revert.

Glycogen synthase kinase-3 (GSK-3) has been proposed as the main kinase able to aberrantly phosphorylate tau in Alzheimer's disease (AD) and related tauopathies, raising the possibility of designing novel therapeutic interventions for AD based on GSK-3 inhibition. Lithium, a widely used drug for affective disorders, inhibits GSK-3 at therapeutically relevant concentrations. Therefore, it was of great interest to test the possible protective effects of lithium in an AD animal model based on GSK-3 overexpression.