N-Benzoyl-D-alaninol

The present study aimed to investigate the potential molecular mechanisms by which galectin‑1 (Gal‑1) and glucose‑regulated protein 78 (GRP78) influence the development of malignant gastric cancer (GC). Immunohistochemistry and western blotting were used to map the expression and location of the Gal‑1 gene in the 80 paraffin‑embedded GC samples, 16 fresh samples and surrounding tissues. Gal‑1 was overexpressed and knocked down using lentiviral vectors in the human GC cell lines HGC‑27 and AGS. Through the use of the Cell Counting Kit‑8 assay, clone formation assay, wound healing assay, invasion assay and tumor xenograft, the possible biological roles of Gal‑1 were further evaluated. The downstream interacting proteins were predicted by the BioGRID database, and GRP78 was chosen for further investigation. Immunofluorescence labeling and Co‑IP were used to confirm the connection. The statistical tests utilized were the two‑tailed paired Student's t‑test, χ2 test, Kaplan‑Meier and Cox regression analysis, and Spearman's rank correlation coefficients. In GC, Gal‑1 is extensively expressed and has the potential to interact with GRP78. Poor prognosis is linked to high levels of GRP78 and Gal‑1 expression in patients with GC. According to the functional study, Gal‑1 knockdown prevented cells from thriving and pushed Gal‑1 expression, which aided in the proliferation, migration and invasion of GC. Gal‑1 overexpression additionally aided the development of subcutaneous xenograft tumors. The mechanistic investigation proved that GRP78 and Gal‑1 interacted, accelerating the course of GC. Gal‑1 silencing had an inhibitory effect on the proliferation of HGC‑27 cells that was removed by ectopic GRP78 expression, whereas the stimulating effects of Gal‑1 overexpression in AGS cells were inhibited by GRP78 knockdown. In conclusion, Gal‑1 interacts with GRP78 to facilitate the advancement of GC. The Gal‑1/GRP78 axis is supported by the functional data of the present study as a possible GC treatment target.

Background: Recently developed Immunoglobulin-E (IgE) based molecular allergy diagnostics provide the ability of identifying allergenic components or ingredients at the molecular level (component-resolved-diagnosis, CRD). Compared to the classical IgE-based allergy diagnostics, molecular technology is providing more sensitive and specific IgE-sensitization patterns. Certain sensitization patterns are characteristic of large geographic regions. There are only few data available on the molecular IgE sensitization patterns in East-Central Europe. This study aims to present further data from this region. Methods: Data of 3993 stored, anonymized molecular ImmunoCap IgE measurements (CRD), performed in Hungary between January-December 2019 from sera of 1288 subjects (mean age: 27 years ±18 years, male/female ratio 0.56) were analyzed retrospectively, in order to get a local distributional pattern of the sensitizing (IgE >0.35 KU/l) molecular allergens. Results: The proportion of CRD positive cases was 24.3%. Amongst them, the most prevalent inhalative allergens were Amb a 1 (18%) Art v 1 (8%) in adults and Der p 2 (3%) and Der p 1 (3%) and Amb a 1 (4%) in subjects below 18 years of age. The same for food allergens were Gal d 2 (21%), Bos d 4 (17%), Bos d 5 (11%) in adults and Gal d 2 (38%), Gal d 1 (28%), Bos d 4 (21%), Bos d 5 (13%) and Bos d 8 (7%) in children. The ratio of mono-sensitivities among CRD-positive cases was 37.5%. Conclusion: Our results provide region-specific patterns of sensitization and molecular allergen spreading for Hungary. The relatively higher abundance of polysensitization's among allergic cases underlines the need for early diagnostic -and preventive measures in the future.

Dystroglycan (DG), which constitutes a part of the dystrophin-glycoprotein complex, connects the extracellular matrix to the cytoskeleton. The matriglycans presented by the extracellular α-DG serve as a contact point with extracellular matrix proteins (ECM) containing laminin G-like domains, providing cellular stability. However, it remains unknown whether core M1 (GlcNAcβ1-2Man) structures can serve as ligands among the various O-Mannosylated glycans. Therefore, based on the presence of N-acetylLactosamine (LacNAc) in this glycan following the core extension, the binding interactions with adhesion/growth-regulatory galectins were explored. To elucidate this process, the interaction between galectin (Gal)-1, -3, -4 and -9 with α-DG fragment 372TRGAIIQTPTLGPIQPTRV390 core M1-based glycopeptide library were profiled, using glycan microarray and nuclear magnetic resonance studies. The binding of galectins was revealed irrespective of its modular architecture, adding galectins to the list of possible binding partners of α-DG core M1 glycoconjugates by cis-binding (via peptide- and carbohydrate-protein interactions), which can be abrogated by α2,3-sialylation of the LacNAc units. The LacNAc-terminated α-DG glycopeptide interact simultaneously with both the S- and F-faces of Gal-1, thereby inducing oligomerization. Furthermore, Gal-1 can trans-bridge α-DG core M1 structures and laminins, which proposed a possible mechanism by which Gal-1 ameliorates muscular dystrophies; however, this proposal warrants further investigation.