Effect of Electro-Acupuncture on Neuroplasticity of Spinal Cord-Transected Rats.

BACKGROUND This study aimed to evaluate the effects of electro-acupuncture (EA) on neuroplasticity associated with the expressions of neurotrophic factors (NTFs) and their receptors in rats subjected to spinal cord transection (SCT). MATERIAL AND METHODS A total of 144 rats were randomly divided into 3 groups (n=48 per group): sham-operated group, SCT group, and EA (electro-acupuncture) group. Rats in SCT and EA groups received spinal cord transection at T10-T11 vertebral levels. Then, EA group rats received EA treatment. Reverse transcription polymerase chain reaction was used to detect NTFs and receptors at the mRNA level. In situ hybridization (ISH) and immunohistochemistry (IHC) were used to detect the expression of NTFs and their receptors. Basso, Beattie, Bresnahan (BBB) scores and cortical somato-sensory evoked potentials (CSEP) were evaluated to assess the recovery of motor and sensory functions. We also measured BDA (Biotinylated dextran amine) axonal tracing, CGRP (Calcitonin gene-related peptide), GAP-43 (Growth-associated protein), and synaptophysin immunohistochemistry (IHC). RESULTS EA treatment led to obvious improvement in hindlimb locomotor and sensory functions. CNTF, FGF-2, and TrkB mRNA were significantly upregulated, while NGF, PDGF, TGF-b1, IGF-1, TrkA, and TrkC mRNA were concomitantly downregulated in the caudal spinal segment (CSS) following EA. Immunohistochemistry demonstrated an increased number of CGRP fibers, GAP-43, and synaptophysin profiles in the CSS in the EA rats. CONCLUSIONS EA may promote the recovery of neuroplasticity in rats subjected to SCT. This could be attributed to the systematic regulation of NTFs and their receptors after EA.

Lectin from the Late Oyster Mushroom, Hohenbuehelia serotina (Agaricomycetes), and Its Novel Effect as an Adjuvant of the HBV DNA Vaccine.

The biological macromolecule Hohenbuehelia serotina lectin (HSL) was first isolated from dried fruiting bodies of the mushroom H. serotina and identified as a heterodimer with 2 subunits of the same molecular weight (15.6 kDa) but different isoelectric points. Lactose and d-galactose inhibited the hemagglutinating activity of HSL, whereas mental ions Mn2+ and Ca2+ could stimulate its hemagglutination. The HSL hemagglutinating activity was stable for 1 hour in NaOH and HCl solutions up to a concentration of 12.5 or 6 mmol/L. In addition, HSL was stable up to 50°C for 30 minutes; its hemagglutinating activity was halved at 60°C and totally inactivated above 90°C. HSL (10 µg) as an immune adjuvant co-inoculated with the proVAX/S2 vaccine enhanced the level of hepatitis B surface antigen in C57BL/6 mice, induced a high level of T-cell proliferation, and induced the expression of IFN- of CD4+ cells. We further illustrate that HSL, as an adjuvant upregulating the expression of major histocompatibility complex II, contributed to the maturation of dendritic cells. As the first lectin isolated from H. serotina, HSL is a potential adjuvant to chronic hepatitis B virus DNA vaccines and lays a foundation for the prevention of HBV infection.

Derivation of Self-inhibitory Helical Peptides to Target Rho-kinase Dimerization in Cerebrovascular Malformation: Structural Bioinformatics Analysis and Peptide Binding Assay.

Rho-kinase dimerization is essential for its kinase activity and biological function; disruption of the dimerization has recently been established as a new and promising therapeutics strategy for cerebrovascular malformation (CM). Based on Rho-kinase dimer crystal structure we herein combined in silico analysis and in vitro assay to rationally derive self-inhibitory peptides from the dimerization interface. Three peptides namely Hlp1, Hlp2 and Hlp3 were successfully designed that have potential capability to rebind at the dimerization domain of Rho-kinase. Molecular dynamics (MD) simulations revealed that these peptides are helically structured when bound to Rho-kinase, but exhibit partially intrinsic disorder in unbound state. Binding free energy (BFE) analysis suggested that the peptides have a satisfactory energetic profile to interact with Rho-kinase. The computational findings were then substantiated by fluorescence anisotropy assays, conforming that the helical peptides can bind tightly to Rho-kinase with affinity KD at micromolar level. These designed peptides are considered as lead molecular entities that can be further modified and optimized to obtain more potent peptidomimetics as self-competitors to disrupt Rho-kinase dimerization in CM.