Preparation, structural and morphological characterization of cartilage type II collagen peptide assemblies from sturgeon head.

BACKGROUND: Sturgeon cartilage type II collagen peptides (SHCPs) can self-assemble and be used to prepare collagen peptide assemblies. Self-assembled peptides have great potential for applications in the food industry. In the present study, self-assembled peptides were prepared from sturgeon cartilage and then characterized. RESULTS: The SHCPs self-assembled and formed collagen peptide assemblies. After response surface experiment optimization, the optimal enzyme digestion process comprised 43.1 °C, 3.37 h and 0.96% enzyme addition, and the peptide yield was 78.46%. Physicochemical analysis showed that the SHCPs were amphiphilic, with an average molecular weight of 1081 Da, and were rich in hydrophobic amino acids. Peptide sequence identification showed that the peptides of SHCPs with polar amino acids followed by hydrophobic amino acids could be self-assembled through hydrogen bonding and hydrophobic interaction. Through turbidity experiments, Fourier transform infrared spectroscopy and scanning electron microscopy, we demonstrated that SHCPs can self-assemble into reticular and tubular structures under specific conditions. Furthermore, both the SHCPs-Ca and SHCPs-Mg assemblies were stabilized within a pH range consistent with that of the human gastrointestinal tract. CONCLUSION: The present study provides a simple and safe method for preparing novel self-assembled peptide materials from sturgeon by-products, providing a scientific basis for the exploitation of sturgeon cartilage and potentially reducing resource wastage. © 2024 Society of Chemical Industry.

Advanced review on type II collagen and peptide: preparation, functional activities and food industry application.

Type II collagen is a homologous super-helical structure consisting of three identical α1(II) chains. It is a major component of animal cartilage, and is widely used in the food industry. Type II collagen can be extracted by acids, salts, enzymes, and via auxiliary methods and can be further hydrolyzed chemically and enzymatically to produce collagen peptides. Recent studies have shown that type II collagen and its polypeptides have good self-assembly properties and important biological activities, such as maintaining cartilage tissue integrity, inducing immune tolerance, stimulating chondrocyte growth and redifferentiation, and providing antioxidant benefits. This review focuses specifically on type II collagen and describes its structure, extraction, and purification, as well as the preparation of type II collagen peptides. In particular, the self-assembly properties and functional activities of type II collagen and collagen peptides are reviewed. In addition, recent research advances in the application of type II collagen and collagen peptides in functional foods, food additives, food coating materials, edible films, and carriers for the food industry are presented. This paper provides more detailed and comprehensive information on type II collagen and peptide for their application.

Apicidin confers promising therapeutic effect on acute myeloid leukemia cells via increasing QPCT expression.

Acute myeloid leukemia (AML) is a heterogeneous hematologic malignancy characterized by abnormal cell proliferation, apoptosis repression and myeloid differentiation blockade of hematopoietic stem/progenitor cells. Developing and identifying novel therapeutic agents to reverse the pathological processes of AML are of great significance. Here in this study, we found that a fungus-derived histone deacetylase inhibitor, Apicidin, presents promising therapeutic effect on AML by inhibiting cell proliferation, facilitating apoptosis and inducing myeloid differentiation of AML cells. Mechanistic investigation revealed that QPCT is identified as a potential downstream target of Apicidin, which exhibits significantly decreased expression in AML samples compared with the normal controls and is remarkably up-regulated in AML cells upon Apicidin management. Functional study and rescue assay demonstrated that QPCT depletion further promotes cell proliferation, inhibits apoptosis and impairs myeloid differentiation of AML cells, alleviating the anti-leukemic effect of Apicidin on AML. Our findings not only provide novel therapeutic target for AML, but also lay theoretical and experimental foundation for the clinical application of Apicidin in AML patients.

Preparation, structure characterization, and stability analysis of peptide-calcium complex derived from porcine nasal cartilage type II collagen.

BACKGROUND: Porcine nasal cartilage type II collagen-derived peptides (PNCPs) may be complexed with calcium to provide a highly bioavailable, low-cost, and effective calcium food supplement. However, the calcium-binding characteristics of PNCPs have not yet been investigated. In the present study, calcium-binding peptides were derived from porcine nasal cartilage type II collagen and the resulting PNCPs-Ca complex was characterized. RESULTS: The study reveals that the calcium-binding capacity of PNCPs is closely related to enzymatic hydrolysis conditions. The highest calcium-binding capacity of PNCPs was observed at a hydrolysis time of 4 h, temperature of 40 °C, enzyme dosage of 1%, and solid-to-liquid ratio of 1:10. Scanning electron microscopy and energy dispersive X-ray spectroscopy revealed that the PNCPs had a pronounced capacity for calcium binding, with the PNCPs-Ca complex exhibiting a clustered structure consisting of aggregated spherical particles. Fourier-transform infrared spectroscopy, fluorescence spectroscopy, X-ray diffraction, dynamic light scattering, amino acid composition, and molecular weight distribution analyses all indicated that the PNCPs and calcium complexed via the carboxyl oxygen and amino nitrogen atoms, leading to the formation of a ß-sheet structure during the chelation process. In addition, the stability of the PNCPs-Ca complex was maintained over a range of pH values consistent with those found in the human gastrointestinal tract, facilitating calcium absorption. CONCLUSION: These research findings suggest the feasibility of converting by-products from livestock processing into calcium-binding peptides, providing a scientific basis for the development of novel calcium supplements and the potential reduction of resource waste. © 2023 Society of Chemical Industry.

Acetylation stabilizes the signaling protein WISP2 by preventing its degradation to suppress the progression of acute myeloid leukemia.

Acute myeloid leukemia (AML) is challenging to treat due to its heterogeneity, prompting a deep understanding of its pathogenesis mechanisms, diagnosis, and treatment. Here, we found reduced expression and acetylation levels of WISP2 in bone marrow mononuclear cells from AML patients and that AML patients with lower WISP2 expression tended to have reduced survival. At the functional level, overexpression of WISP2 in leukemia cells (HL-60 and Kasumi-1) suppressed cell proliferation, induced cell apoptosis, and exerted antileukemic effects in an in vivo model of AML. Our mechanistic investigation demonstrated that WISP2 deacetylation was regulated by the deacetylase histone deacetylase (HDAC)3. In addition, we determined that crosstalk between acetylation and ubiquitination was involved in the modulation of WISP2 expression in AML. Deacetylation of WISP2 decreased the stability of the WISP2 protein by boosting its ubiquitination mediated by NEDD4 and proteasomal degradation. Moreover, pan-HDAC inhibitors (valproic acid and trichostatin A) and an HDAC3-specific inhibitor (RGFP966) induced WISP2 acetylation at lysine K6 and prevented WISP2 degradation. This regulation led to inhibition of proliferation and induction of apoptosis in AML cells. In summary, our study revealed that WISP2 contributes to tumor suppression in AML, which provided an experimental framework for WISP2 as a candidate for gene therapy of AML.

Advances in sports food: Sports nutrition, food manufacture, opportunities and challenges.

In recent years, the increase in public awareness of sports has greatly promoted the development of the sports food industry. Sports food provides nutrition to meet the metabolic and energy needs of sports people. The nutritional components of sports food can be divided into basic nutrients and functional factors. Basic nutrients refer to the nutrients or metabolites required by the human body. Functional factors are bioactive ingredients that have potential effects in improving functions of the human body, such as protection of articular cartilage and improving muscle quality. Currently, there are various forms of sports foods in the market, including sports drinks, solid sports foods, semi-solid sports foods, and sports nutrition supplements. The sports food industry has seen many opportunities such as the expanding market, manufacturing technology development, and increasing funds investment. However, it also faces many challenges, such as lack of innovation, insufficient in-depth research, risks, and safety issues. This review would provide theoretical guidance for current sports food manufacture to meet the needs of increasing sports people worldwide.

Effects of type II collagen hydrolysates on osteoarthritis through the NF-κB, Wnt/ß-catenin and MAPK pathways.

Osteoarthritis (OA), a degenerative disease, has attracted extensive attention all over the world. In this study, a rat model involving medial meniscus resection (MMx) and anterior to medial collateral ligament (ACL) operation was successfully established to study the effects of bovine cartilage hydrolysates rich in type II collagen peptides (BIIP) on cartilage protection. The results of histological analysis indicated that oral administration of BIIP at doses of 200 and 500 mg kg-1 d-1 ameliorated cartilage degeneration. Moreover, the potential targets of BIIP affecting OA in vivo were studied by proteomics, and the effects of BIIP on OA through signaling pathways, such as NF-κB, Wnt/ß-catenin and MAPK, were further explored at mRNA and protein levels. BIIP downregulated the expression of IL-6, RUNX2, NF-κB p65, HIF-2α, ß-catenin and p-JNK, which may be the main factor leading to the prevention of OA. These results suggest that BIIP can be used as a novel potential substance of functional foods to exert chondroprotective action.

Absolute Lymphocyte Count Prior to Lymphodepletion Impacts Outcomes in Multiple Myeloma Patients Treated with Chimeric Antigen Receptor T Cells.

Chimeric antigen receptor (CAR) T cell therapy has shown unprecedented response rates in patients with relapsed/refractory (R/R) multiple myeloma (MM). However, the factors associated with immediate response and durable remission have not been fully elucidated. This study aimed to investigate the impact of prelymphodepletion (pre-LD) absolute lymphocyte count (ALC) on the outcomes of CAR T cell therapy and cytokine release syndrome (CRS). A receiver operating characteristic curve was used to determine the optimal cutoff value of pre-LD ALC. The correlation of pre-LD ALC with deep response (defined as very good partial response or better), CRS, and long-term outcomes was analyzed in 85 patients with R/R MM who received CAR T cell treatment. The median pre-LD ALC was 1.0 × 109/L (range, 0.1 to 2.9× 109/L). The optimal cutoff value of pre-LD ALC was 0.75 × 109/L. Twenty-two patients (26%) had a low pre-LD ALC (<0.75 × 109/L), and 63 patients (74%) had a high pre-LD ALC (≥0.75 × 109/L). The deep response rate was significantly higher in patients with a high pre-LD ALC compared with patients with a low pre-LD ALC (76% versus 41%; P = .002). Patients with a low pre-LD ALC had significantly inferior overall survival (OS) and progression-free survival (PFS) compared with those with a high pre-LD ALC (median OS, 15.4 months versus not reached [P < .001]; median PFS, 8.4 months versus 27.3 months [P < .001]). No correlation between pre-LD ALC and CRS was observed. Our data indicate that pre-LD ALC may be a useful indicator to predict the outcomes of CAR T cell therapy in patients with R/R MM. © 2021 American Society for Transplantation and Cellular Therapy. Published by Elsevier Inc.