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Dysregulated kynurenine (KYN) pathway has been implicated in the pathophysiology of depression. In this systematic review, we examined the relationship between kynurenine pathway metabolites (KYN, kynurenic acid KYNA, tryptophan TRP, quinolinic acid QUIN, KYN/TRP ratio) and depression symptoms in the context of pro-inflammatory activation and immune response. Out of 5,082 articles, fifteen studies were suitable; ten studies (N = 315 medically ill patients treated with interferon-alpha IFN-α) reported baseline and post-intervention plasma KYN, TRP and KYN/TRP ratios which were included in quantitative meta-analysis. Data from five studies were summarized (IFN-α, interferon-beta IFN-β, and lipopolysaccharide LPS). We found that IFN-α treatment in patients with chronic illnesses was associated with decreased TRP, increased levels of KYN and KYN/TRP ratio and depression scores from baseline to follow-up at both 4 and 24 weeks. Our findings suggest that increased risk of depression observed after immune-activating agents in patients with chronic medical illnesses is likely mediated by the kynurenine pathway. Further prospective studies are required to investigate the exact pathophysiology of the KYN pathway in depression.Chitotriosidase (Chit1) and acidic mammalian chitinase (AMCase) have been attracting research interest due to their involvement in various pathological conditions such as Gaucher's disease and asthma, respectively. Both enzymes are highly expressed in mice, while the level of AMCase mRNA was low in human tissues. In addition, the chitinolytic activity of the recombinant human AMCase was significantly lower than that of the mouse counterpart. Here, we revealed a substantially higher chitinolytic and transglycosylation activity of human Chit1 against artificial and natural chitin substrates as compared to the mouse enzyme. We found that the substitution of leucine (L) by tryptophan (W) at position 218 markedly reduced both activities in human Chit1. Conversely, the L218W substitution in mouse Chit1 increased the activity of the enzyme. These results suggest that Chit1 may compensate for the low of AMCase activity in humans, while in mice, highly active AMCase may supplements low Chit1 activity.Chemokines are a sub-group of chemotactic cytokines that regulate the leukocyte migration by binding to G-protein coupled receptors (GPCRs) and cell surface glycosaminoglycans (GAGs). Interleukin-8 (CXCL8/IL8) is one of the most essential CXC chemokine that has been reported to be involved in various pathophysiological conditions. Structure-function relationships of human IL8 have been studied extensively. However, no such detailed information is available on IL8 orthologs, although they exhibit significant functional divergence. In order to unravel the differential structure-dynamics-stability-function relationship of IL8 orthologs, comparative molecular analysis was performed on canine (laurasians) and human (primates) IL8 proteins using in-silico molecular evolutionary analysis and solution NMR spectroscopy methods. The residue level NMR studies suggested that, although the overall structural architecture of canine IL8 is similar to that of human IL8, systematic differences were observed in their backbone dynamics and low-energy excited states due to amino acid substitutions. Further, these substitutions also resulted in attenuation of stability and heparin binding affinity in the canine IL8 as compared to its human counterpart. Indeed, structural and sequence analysis evidenced for specificity of molecular interactions with cognate receptor (CXCR1) and glycosaminoglycan (heparin), thus providing evidence for a noticeable functional specificity and divergence between the two IL8 orthologs.The midgut cadherin fragments were extensively studied as Bt synergists in insects, while their synergistic selection modes with Bt toxins in different mechanisms of resistance or insects have never been determined. buy BAL-0028 Here, a soluble Helicoverpa armigera cadherin fragment which corresponds to the Cry1Ac binding region (HaCad-TBR) was expressed in Escherichia coli and its synergism with Cry1Ac toxin in H. armigera and Plutella xylostella larvae as well as Sf9 cells expressing different cadherins was tested. HaCad-TBR exhibited higher synergism factor in P. xylostella larvae (4.84-fold) than in H. armigera larvae (2.45-fold). Among the cells expressing HaCad alleles, HaCad-TBR enhanced the Cry1Ac toxicity only in the cells expressing the mutant lacking the extracellular domain. Moreover, HaCad-TBR had a weak enhancement of Cry1Ac toxicity in Sf9 cells expressing the P. xylostella cadherin. Further researches revealed that the enhancement of toxicity in Sf9 cells was correlated with increased toxin binding. These results suggested that cadherin fragments which have high binding level with Cry1Ac are more likely to enhance toxin toxicity well against the cells or larvae where the cadherin has lower binding level with Cry1Ac, especially in the cases lacking the toxin binding domain.In this study, estrone was used as targeting functionality in chitosan nanoparticles (DoxEs-CSEsNPs) carrying doxorubicin-estrone conjugate for dual targeted intracellular delivery to breast cancer cells. Estrone was conjugated with Dox and CS and characterized by FTIR and FT-NMR spectroscopy. Dox/DoxEs containing CSEsNPs were prepared with ionic gelation method and for the effect of formulation variables a 3-factor, 3-level Box-Behnken design (BBD) was explored, which predict the responses like particle size (Y1) and percent entrapment efficiency (%EE) (Y2) when CSEs TPP ratio (X1), sonication time (X2) and stirring speed (X3) were selected as independent variables. The Dox-CSEsNPs and DoxEs-CSEsNPs were characterized for size, shape, PDI, surface charge and thermal analysis. The drug entrapment efficiency was 66.33 ± 2.82% and 62.25 ± 2.63% for Dox-CSEsNPs and DoxEs-CSEsNPs formulation respectively. The in vitro release, haemolytic toxicity, and fluorescent microscopy studies were also assessed. Anticancer activity on the MCF-7 cell line indicated the higher potency of DoxEs-CSEsNPs as compared to Dox-CSEsNPs, DoxEs, and Dox solution. The findings are decisive for selective targeting of antineoplastic agents to the ERs, which indicate that the DoxEs loaded CSEsNPs were able to significantly improve the efficacy of Dox.
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