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Streicher, J. M.

Publications and source records attributed to Streicher, J. M..

3 recordsLinked to original sources

Inhibition of Heat Shock Protein 90 in the Spinal Cord Improves the Therapeutic Index of Morphine

Opioid drugs like morphine are the gold standard for the treatment of chronic pain, but are limited by adverse side effects, such as tolerance, constipation, and reward/addiction. In our earlier work, we showed that Heat shock protein 90 (Hsp90) has a crucial role in regulating opioid signaling that differs between brain and spinal cord; Hsp90 inhibition in brain blocks opioid pain relief, while inhibition in the spinal cord enhances it. Building on these findings here, we injected the non-selective Hsp90 inhibitor KU-32 directly into the spinal cord of male and female CD-1 mice, showing that morphine anti-nociceptive potency was boosted by 1.9-3.5 fold in the pain models of tail flick, post-surgical paw incision, and HIV peripheral neuropathy. At the same time, morphine tolerance was reduced from 21 fold to 2.9 fold and established tolerance was rescued, while the potency of constipation and reward (as measured by conditioned place preference) was unchanged. These results demonstrate that spinal Hsp90 inhibition can improve the therapeutic index of morphine. However, we also found that systemic non-selective Hsp90 inhibition resulted in a brain-like effect, blocking opioid pain relief. We thus sought a way to circumvent the effects of brain Hsp90 inhibition by investigating the molecular Hsp90 isoforms active in regulating opioid signaling in both regions. Using selective small molecule inhibitors and CRISPR gene editing, we found that 3 Hsp90 isoforms regulated spinal cord opioid signaling (Hsp90, Hsp90{beta}, and Grp94) while our previous work showed only Hsp90 was active in brain. We thus hypothesized that a systemically delivered selective inhibitor to Hsp90{beta} or Grp94 could selectively inhibit spinal cord Hsp90 activity, resulting in enhanced opioid pain relief and decreased side effects. We tested this hypothesis using intravenous delivery of KUNB106 (Hsp90{beta}) and KUNG65 (Grp94), showing that both drugs enhanced morphine potency in tail flick and paw incision pain while rescuing anti-nociceptive tolerance. We also found that intravenous KUNA115 (Hsp90) fully blocked morphine anti-nociception. Together, these results suggest that selective inhibition of spinal cord Hsp90 isoforms is a novel, translationally feasible strategy to improve the therapeutic index of opioids.

neuroscience

Cannabis sativa Terpenes are Cannabimimetic and Provide Support for the Entourage Effect Hypothesis

Limited evidence has suggested that terpenes found in Cannabis sativa are analgesic, and could produce an "entourage effect" whereby they modulate cannabinoids to result in improved outcomes. However this hypothesis is controversial, with limited evidence. We thus investigated Cannabis sativa terpenes alone and with the cannabinoid agonist WIN55,212 using in vitro and in vivo approaches. We found that the terpenes -humulene, geraniol, linalool, and {beta}-pinene produced cannabinoid tetrad behaviors in mice, suggesting cannabimimetic activity. Some behaviors could be blocked by cannabinoid or adenosine receptor antagonists, suggesting a mixed mechanism of action. These behavioral effects were additive with WIN55,212, providing support for a terpene "entourage effect." In vitro experiments showed that all terpenes activated the CB1R, while some activated other targets. Our findings suggest that these Cannabis terpenes are multifunctional cannabimimetic ligands that provide support for the entourage effect hypothesis and could be used to enhance the therapeutic properties of cannabinoids.

pharmacology and toxicology

Targeting the CaV - interaction yields a selective antagonist of the N-type CaV2.2 channel with broad antinociceptive efficacy

Inhibition of voltage-gated calcium (CaV) channels is a potential therapy for many neurological diseases including chronic pain. Neuronal CaV1/CaV2 channels are composed of , {beta} and 2{delta} subunits. The {beta}-subunits of CaV channels are cytoplasmic proteins that increase the surface expression of the pore-forming subunit of CaV. We targeted the high-affinity protein-protein interface of CaV{beta}s pocket within the CaV-subunit. Structure-based virtual screening of 50,000 small molecule library docked to the {beta}-subunit led to the identification of 2-(3,5-dimethylisoxazol-4-yl)-N-((4-((3-phenylpropyl)amino)quinazolin-2-yl)methyl)acetamide (compound 45). This small molecule bound to CaV{beta} and inhibited its coupling with N-type voltage-gated calcium (CaV2.2) channels, leading to a reduction in CaV2.2 currents in rat dorsal root ganglion (DRG) sensory neurons, decreased pre-synaptic localization of CaV2.2 in vivo, decreased frequency of spontaneous excitatory post-synaptic potentials (sEPSC), and inhibited release of the nociceptive neurotransmitter calcitonin gene related peptide (CGRP) from spinal cord. 45 was antinociceptive in naive animals and reversed allodynia and hyperalgesia in models of acute (post-surgical) and neuropathic (spinal nerve ligation, chemotherapy- and gp120-induced peripheral neuropathy, and genome-edited neuropathy) pain. 45 did not cause akinesia or motor impairment, a common adverse effect of CaV2.2 targeting drugs, when injected into the brain. 45, a quinazoline analog, represents a novel class of CaV2.2-targeting compounds that may serve as probes to interrogate CaV-{beta} function and ultimately be developed as a non-opioid therapeutic for chronic pain.

neuroscience