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#33441819   2021/01/13 To Up

Physiological responses of Siberian sturgeon (Acipenser baerii) juveniles fed on full-fat insect-based diet in an aquaponic system.

Over the last years, the potential use of Black Soldier Fly meal (BSF) as a new and sustainable aquafeed ingredient has been largely explored in several fish species. However, only fragmentary information is available about the use of BSF meal-based diets in sturgeon nutrition. In consideration of a circular economy concept and a more sustainable aquaculture development, the present research represents the first comprehensive multidisciplinary study on the physiological effects of a BSF diet during sturgeon culture in an aquaponic system. Siberian sturgeon (Acipenser baerii) juveniles were fed over a 60-days feeding trial on a control diet (Hi0) and a diet containing 50% of full-fat BSF meal respect to fish meal (Hi50). Physiological responses of fish were investigated using several analytical approaches, such as gas chromatography-mass spectrometry, histology, Fourier Transformed Infrared Spectroscopy (FTIR), microbiome sequencing and Real-time PCR. While aquaponic systems performed optimally during the trial, Hi50 group fish showed lower diet acceptance that resulted in growth and survival reduction, a decrease in hepatic lipids and glycogen content (FTIR), a higher hepatic hsp70.1 gene expression and a worsening in gut histological morphometric parameters. The low feed acceptance showed by Hi50 group sturgeon highlighted the necessity to improve the palatability of BSF-based diet designed for sturgeon culture.
Matteo Zarantoniello, Basilio Randazzo, Valentina Nozzi, Cristina Truzzi, Elisabetta Giorgini, Gloriana Cardinaletti, Lorenzo Freddi, Stefano Ratti, Federico Girolametti, Andrea Osimani, Valentina Notarstefano, Vesna Milanović, Paola Riolo, Nunzio Isidoro, Francesca Tulli, Giorgia Gioacchini, Ike Olivotto

2398 related Products with: Physiological responses of Siberian sturgeon (Acipenser baerii) juveniles fed on full-fat insect-based diet in an aquaponic system.

1 mL1 mL100ug100 μg2 Pieces/Box100ug100 μg100 μg100 μg0.1 mg100 μg

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#33169384   2020/11/10 To Up

Hsp70 in cancer: A double agent in the battle between survival and death.

The heat shock protein (Hsps) superfamily, also known as molecular chaperones, are highly conserved and present in all living organisms and play vital roles in protein fate. The HspA1A (Hsp70-1), called Hsp70 in this review, is expressed at low or undetectable levels in most unstressed normal cells, but numerous studies have shown that diverse types of tumor cells express Hsp70 at the plasma membrane that leads to resistance to programmed cell death and tumor progression. Hsp70 is released into the extracellular milieu in three forms including free soluble, complexed with cancer antigenic peptides, and exosome forms. Therefore, it seems to be a promising therapeutic target in human malignancies. However, a great number of studies have indicated that both intracellular and extracellular Hsp70 have a dual function. A line of evidence presented that intracellular Hsp70 has a cytoprotective function via suppression of apoptosis and lysosomal cell death (LCD) as well as that extracellular Hsp70 can promote tumorigenesis and angiogenesis. Other evidence showed intracellular Hsp70 can promote apoptosis and membrane-associated/extracellular Hsp70 can elicit antitumor innate and adaptive immune responses. Given the contradictory functions, as a "double agent," could Hsp70 be a promising tool in the future of targeted cancer therapies? To answer this question, in this review, we will discuss the functions of Hsp70 in cancers besides inhibition and stimulation strategies for targeting Hsp70 along with their challenges.
Mehdi A Vostakolaei, Leila Hatami-Baroogh, Ghader Babaei, Ommoleila Molavi, Shirafkan Kordi, Jalal Abdolalizadeh

1924 related Products with: Hsp70 in cancer: A double agent in the battle between survival and death.

100ug Lyophilized

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#33147473   2020/11/02 To Up

Expression of Heat shock protein 70 (Hsp70-1) in Plasmodium berghei ookinetes and its participation in midgut mosquito infection.

The heat shock protein family 70 (Hsp70) comprises chaperone proteins that play major multiple roles in Plasmodium asexual and sexual development. In this study, we analyzed the expression of Hsp70-1 in gametocytes, gametes, zygotes, and its participation in ookinete formation and their transition into oocysts. A monoclonal antibody against recombinant Hsp70-1 revealed its presence in zygotes and micronemes of ookinetes. Compared to wild type parasites, Hsp70-1 knockout ookinetes produced fewer oocysts in Plasmodium-susceptible Anopheles albimanus mosquitoes. This may indicate a defective transformation of ookinetes into oocysts in the absence of Hsp70-1. The presence of this protein in micronemes suggests its participation in mosquito infection, probably aiding to the adequate structural conformation of proteins in charge of motility, recognition and invasion of the insect midgut epithelium.
Maria Carmen Rodriguez, Jesús Martínez-Barnetche, Alba N Lecona-Valera, Juan Téllez-Sosa, Rocio S Argotte-Ramos, Alejandro Alvarado-Delgado, Marbella T Ovilla, Vianey Saldaña-Navor, Mario H Rodriguez

1887 related Products with: Expression of Heat shock protein 70 (Hsp70-1) in Plasmodium berghei ookinetes and its participation in midgut mosquito infection.

0.1 mg 0.2 mg 50 µg 0.2 mg 25mg0.2 mg1 Set1 Set1 Set10002ug10

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#33041514   2020/04/09 To Up

Proteomic analysis of the monkey hippocampus for elucidating ischemic resistance.

It is well-known that the cornu 1 (CA1) sector of hippocampus is vulnerable for the ischemic insult, whereas the dentate gyrus (DG) is resistant. Here, to elucidate its underlying mechanism, alternations of protein oxidation and expression of DG in the monkey hippocampus after ischemia-reperfusion by the proteomic analysis were studied by comparing CA1 data. Oxidative damage to proteins such as protein carbonylation interrupt the protein function. Carbonyl modification of molecular chaperone, heat shock 70 kDa protein 1 (Hsp70.1) was increased remarkably in CA1, but slightly in DG. In addition, expression levels of nicotinamide adenine dinucleotide (NAD)-dependent protein deacetylase sirtuin-2 (SIRT2) was significantly increased in DG after ischemia, but decreased in CA1. Accordingly, it is likely that SIRT2 upregulation and negligible changes of carbonylation of Hsp70.1 exert its neuroprotective effect in DG. On the contrary, carbonylation level of dihydropyrimidinase related protein 2 (DRP-2) and l-lactate dehydrogenase B chain (LDHB) were slightly increased in CA1 as shown previously, but remarkably increased in DG after ischemia. It is considered that DRP-2 and LDHB are specific targets of oxidative stress by ischemia insult and high carbonylation levels of DRP-2 may play an important role in modulating ischemic neuronal death.
Yurie Mori, Shinji Oikawa, Shota Kurimoto, Yuki Kitamura, Saeko Tada-Oikawa, Hatasu Kobayashi, Tetsumori Yamashima, Mariko Murata

1207 related Products with: Proteomic analysis of the monkey hippocampus for elucidating ischemic resistance.

100ug Lyophilized10.1 mg1mg1 kit(96 Wells)1 module2.5 mg50mg1 module50 assays

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#32903557   2020/08/13 To Up

Intravenous Immunoglobulin G Suppresses Heat Shock Protein (HSP)-70 Expression and Enhances the Activity of HSP90 and Proteasome Inhibitors.

Intravenous immunoglobulin G (IVIgG) is approved for primary immunodeficiency syndromes but may induce anti-cancer effects, and while this has been attributed to its anti-inflammatory properties, IgG against specific tumor targets may play a role. We evaluated IVIgG alone, and with a Heat shock protein (HSP)-90 or proteasome inhibitor, using multiple myeloma and mantle cell lymphoma (MCL) cells , and with the proteasome inhibitor bortezomib . IVIgG inhibited the growth of all cell lines tested, induced G cell cycle arrest, and suppressed pro-tumor cytokines including Interleukin (IL)-6, IL-8, and IL-10. Genomic and proteomic studies showed that IVIgG reduced tumor cell HSP70-1 levels by suppressing the ability of extracellular HSP70-1 to stimulate endogenous promoter activity, and reduced extracellular vesicle uptake. Preparations of IVIgG were found to contain high titers of anti-HSP70-1 IgG, and recombinant HSP70-1 reduced the efficacy of IVIgG to suppress HSP70-1 levels. Combining IVIgG with the HSP90 inhibitor AUY922 produced superior cell growth inhibition and correlated with HSP70-1 suppression. Also, IVIgG with bortezomib or carfilzomib was superior to each single agent, and enhanced bortezomib's activity in bortezomib-resistant myeloma cells. Moreover, IVIgG reduced transfer of extracellular vesicles (EVs) to cells, and blocked transfer of bortezomib resistance through EVs. Finally, IVIgG with bortezomib were superior to the single agents in an myeloma model. These studies support the possibility that anti-HSP70-1 IgG contained in IVIgG can inhibit myeloma and MCL growth by interfering with a novel mechanism involving uptake of exogenous HSP70-1 which then induces its own promoter.
Richard J Jones, Ram K Singh, Fazal Shirazi, Jie Wan, Hua Wang, Xiaobin Wang, Min Jin Ha, Muhamed Baljevic, Isere Kuiatse, Richard E Davis, Robert Z Orlowski

1327 related Products with: Intravenous Immunoglobulin G Suppresses Heat Shock Protein (HSP)-70 Expression and Enhances the Activity of HSP90 and Proteasome Inhibitors.

0.1 mg100 ul96T96T 0.2 mg 500 50gm1000 TESTS/0.65ml100

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#32840700   2020/08/25 To Up

In Silico Analysis of HSP70 Gene Family in Bovine Genome.

Heat shock proteins (HSPs), members of molecular chaperones families fulfill essential roles under normal conditions and provide protection and adaptation during and after stress. Among different HSPs, HSP70 kDa family of proteins is most abundant and well-studied in human and mouse but has not yet been characterized in bovines. In silico analysis was performed to characterize members of HSP70 gene family in bovine genome and a total of 17 genes of bovine HSP70 gene family were identified. The members of HSP70 family were distributed over 12 chromosomes with gene size ranging from 1911 (HSPA2) to 54,017 bp (HSPA4). Five genes were intronless, while rest of 12 genes were multiexonic. Phylogenetic analysis of HSP70 gene family distinguished them into eight major evolutionary groups wherein members of group 1 were most divergent and quite dissimilar than from rest of the HSP70 sequences. Domain structure of all bovine HSP70 genes was conserved and three signature patterns HSP70_1, HSP70_2, and HSP70_3 were identified. HSPA8, HSP9, and HSPA1A showed comparatively higher expression in majority of tissues. Like humans, bovine HSP70 family was characterized by remarkable evolutionary diversity. The analysis also suggested resemblance of bovine HSP70 family to that of human compared to mouse. Overall, the study indicates the presence of diversity for structure, function, localization, and expression in the bovine HSP70 family chaperons which could form the basis to understand thermotolerance/adaptive changes in the bovines.
Kabita Tripathy, Monika Sodhi, R S Kataria, Meenu Chopra, Manishi Mukesh

1899 related Products with: In Silico Analysis of HSP70 Gene Family in Bovine Genome.

500 ml50 ml20 12 x 25 ul10 ml2 Pieces/Box100mg

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#32801239   // To Up

Heat Shock Protein 70 Gene Polymorphism in Egyptian Patients with Type 2 Diabetes Mellitus, with and without Nephropathy.

Heat-shock proteins (HSPs) are a group of proteins that function to protect cells and tissues against different types of damage. The aim of this work was to study the relationship between the genetic variation in HSP70 genes and the risk for development of nephropathy in Egyptian patients with Type 2 diabetes mellitus (DM). This study was carried out on 90 patients divided into three groups: 30 patients of Type 2 DM with nephropathy (Group I), 30 patients of Type 2 DM without nephropathy (Group II) with duration of diabetes > 10 years in both patient groups, and 30 healthy persons, who served as controls (Group III). All the studied patients were submitted to full history taking, complete clinical examination, and laboratory investigations including fasting blood glucose, glycated hemoglobin, renal function tests, and urinary albumin- to-creatinine ratio. HSP70-1 -110 AC, +190 G/C, HSP70-2 +1267 A/G, and shock protein70- hom +2437 T/C gene polymorphism were determined using the polymerase chain reaction- restriction fragment length polymorphism technique (PCR-RFLP). The results of the present study showed a highly statistically significant difference between Group I and Group II regarding family history, systolic and diastolic blood pressure, and duration of diabetes. There was a significant difference in the distribution of C allele of HSP70-1 -110A/C and +190 G/C and G allele of HSP70-2+1267A/G with more frequent detection in nephropathy group versus other groups, while there was no significant difference in genotype and allele distributions among the three studied groups for the HSP70-hom. It can be concluded that the C allele distribution of (HSP70-1 -110 A/C and HSP70+190 C/G) and the G allele distribution of HSP70-2 +1267A/G are associated with the susceptibility to renal complications in Egyptian patients with Type 2 DM.
Osama Mohamady Elshahed, Olfat Gamil Shaker

1068 related Products with: Heat Shock Protein 70 Gene Polymorphism in Egyptian Patients with Type 2 Diabetes Mellitus, with and without Nephropathy.

0.1 mg96T96T10 ìg100 μg21 kit(96 Wells)500 100 ul500 100ug Lyophilized100ug Lyophilized

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#32623461   // To Up

Intake of ω-6 Polyunsaturated Fatty Acid-Rich Vegetable Oils and Risk of Lifestyle Diseases.

Although excessive consumption of deep-fried foods is regarded as 1 of the most important epidemiological factors of lifestyle diseases such as Alzheimer's disease, type 2 diabetes, and obesity, the exact mechanism remains unknown. This review aims to discuss whether heated cooking oil-derived peroxidation products cause cell degeneration/death for the occurrence of lifestyle diseases. Deep-fried foods cooked in ω-6 PUFA-rich vegetable oils such as rapeseed (canola), soybean, sunflower, and corn oils, already contain or intrinsically generate "hydroxynonenal" by peroxidation. As demonstrated previously, hydroxynonenal promotes carbonylation of heat-shock protein 70.1 (Hsp70.1), with the resultant impaired ability of cells to recycle damaged proteins and stabilize the lysosomal membrane. Until now, the implication of lysosomal/autophagy failure due to the daily consumption of ω-6 PUFA-rich vegetable oils in the progression of cell degeneration/death has not been reported. Since the "calpain-cathepsin hypothesis" was formulated as a cause of ischemic neuronal death in 1998, its relevance to Alzheimer's neuronal death has been suggested with particular attention to hydroxynonenal. However, its relevance to cell death of the hypothalamus, liver, and pancreas, especially related to appetite/energy control, is unknown. The hypothalamus senses information from both adipocyte-derived leptin and circulating free fatty acids. Concentrations of circulating fatty acid and its oxidized form, especially hydroxynonenal, are increased in obese and/or aged subjects. As overactivation of the fatty acid receptor G-protein coupled receptor 40 (GPR40) in response to excessive or oxidized fatty acids in these subjects may lead to the disruption of Ca2+ homeostasis, it should be evaluated whether GPR40 overactivation contributes to diverse cell death. Here, we describe the molecular implication of ω-6 PUFA-rich vegetable oil-derived hydroxynonenal in lysosomal destabilization leading to cell death. By oxidizing Hsp70.1, both the dietary PUFA- (exogenous) and the membrane phospholipid- (intrinsic) peroxidation product "hydroxynonenal," when combined, may play crucial roles in the occurrence of diverse lifestyle diseases including Alzheimer's disease.
Tetsumori Yamashima, Tsuguhito Ota, Eishiro Mizukoshi, Hiroyuki Nakamura, Yasuhiko Yamamoto, Mitsuru Kikuchi, Tatsuya Yamashita, Shuichi Kaneko

1819 related Products with: Intake of ω-6 Polyunsaturated Fatty Acid-Rich Vegetable Oils and Risk of Lifestyle Diseases.

500g 5 G 5 G1 g250 mg25 g1 mg2.5 mg 5 G 500 G50 mg1 g

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