Alzheimer’s Disease, and Breast and Prostate Cancer Research: Translational Failures and the Importance to Monitor Outputs and Impact of Funded Research
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Alzheimer’s Disease, and Breast and Prostate Cancer Research: Translational Failures and the Importance to Monitor Outputs and Impact of Funded Research
Dementia and cancer are becoming increasingly common in Western countries. In the last two decades, research has focused on Alzheimer’s disease (AD) and cancers, particularly, breast cancer (BC) and prostate cancer (PC), has been substantially funded both in Europe and worldwide.
While the results of scientific research have contributed to improving our understanding of disease etiopathology, still the prevalence of chronic degenerative conditions are still very high in the whole world. By definition, there is the perfect model. In particular, the animal model of AD, BC, and the PC has been and still is traditionally used in basic research / fundamental, translational and preclinical to study human disease mechanisms, identifying new therapeutic targets and develop new drugs
However, inadequate animal models of several important features of the human disease; Therefore, they often can not pave the way for the development of effective drugs in human patients. The emergence of new tools and models of technology in the life sciences, and the growing need for a multidisciplinary approach has prompted many interdisciplinary research initiatives. With substantial funds invested in biomedical research, it is becoming necessary to define and implement indicators to monitor contributions to innovation and impact of funded research.
Here, we discuss some of the issues underlying the failure of translation in AD, BC, and research PCs, and illustrates how the indicators can be applied to the output size and the impact of the retrospective funded biomedical research. Disease coronavirus 19 (COVID-19) has dramatically changed daily life, including the field of research of the disease (AD) Alzheimer’s. This perspective article discusses some of the ways in which COVID-19 has impacted the field, anticipating some long-lasting effects, and explore strategies to address the needs of current and future. Areas of impact include the integrity of the study, regulatory issues and industry, and the involvement of the participants.
The proposed strategy to address these challenges include the analytical method to handle large degree lost data and development, user-friendly, means of data collection and remote patient-centered assessments. We also highlight the importance of maintaining the welfare of participants as a first priority and constant.
Alzheimer’s Disease, and Breast and Prostate Cancer Research: Translational Failures and the Importance to Monitor Outputs and Impact of Funded Research
Synaptosome as a tool in the study of Alzheimer’s disease
synaptic dysfunction is an integral feature of the disease (AD) pathophysiology of Alzheimer’s. In fact, the prodromal manifestations of structural and functional deficits in synaptic much before the appearance of overt disease indicates that pathological hallmarks of AD may be regarded as a degenerative disorder of synapses.
Some research instruments and techniques have allowed us to study synaptic function and plasticity and their changes in pathological conditions, such as AD. One such tool is the biochemical preparation isolated from apart and resealed synaptic terminal, the “synaptosomes”. Due to the preservation of many physiological processes such as metabolism and enzymatic activity, synaptosomes has proven to be an ex vivo model of system is needed for the study of synaptic physiology either when isolated from fresh or cryopreserved tissue, and from animal or human post-mortem tissue.
Description: Human pons tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human pons tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the pons tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The pons tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Human amygdala tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human amygdala tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the amygdala tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The amygdala tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Human thalamus tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human thalamus tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the thalamus tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The thalamus tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Human hippocamps tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human hippocamps tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the hippocamps tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The hippocamps tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Human frontal lobe tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human frontal lobe tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the frontal lobe tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The frontal lobe tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Human parietal lobe tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human parietal lobe tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the parietal lobe tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The parietal lobe tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Human temporal lobe tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human temporal lobe tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the temporal lobe tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The temporal lobe tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Human occipital lobe tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human occipital lobe tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the occipital lobe tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The occipital lobe tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Human corpus Callosum tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human corpus Callosum tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the corpus Callosum tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The corpus Callosum tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Human precentral gyrus tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human precentral gyrus tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the precentral gyrus tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The precentral gyrus tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Human brain amygdala tissue membrane protein lysate was prepared by isolating the membrane protein from whole tissue homogenates using a proprietary technique. The human amygdala tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The membrane protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the isolated brain amygdala tissue membrane protein pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The isolated brain amygdala tissue membrane protein is then Western analyzed by either GAPDH or β-actin antibody to confirm there is no signal or very weak signal.
Description: Human postcentral gyrus tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human postcentral gyrus tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the postcentral gyrus tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The postcentral gyrus tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
Description: Human brain hippocamps tissue membrane protein lysate was prepared by isolating the membrane protein from whole tissue homogenates using a proprietary technique. The human hippocamps tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The membrane protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the isolated brain hippocamps tissue membrane protein pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The isolated brain hippocamps tissue membrane protein is then Western analyzed by either GAPDH or β-actin antibody to confirm there is no signal or very weak signal.
Description: Human brain hippocamps tissue cytoplasmic protein lysate was prepared by isolating the cytoplasmic protein from whole tissue homogenates using a proprietary technique. The human hippocamps tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The cytoplasmic protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, glycerol, and a cocktail of protease inhibitors. For quality control purposes, the isolated brain hippocamps tissue cytoplasmic protein pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The isolated brain hippocamps tissue cytoplasmic protein is then Western analyzed by GAPDH antibody, and the expression level is consistent with each lot.
Description: Human brain temporal lobe tissue membrane protein lysate was prepared by isolating the membrane protein from whole tissue homogenates using a proprietary technique. The human temporal lobe tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The membrane protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the isolated brain temporal lobe tissue membrane protein pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The isolated brain temporal lobe tissue membrane protein is then Western analyzed by either GAPDH or β-actin antibody to confirm there is no signal or very weak signal.
Description: Accumulation of the amyloid-β peptide (Aβ) in the cerebral cortex is a critical event in the pathogenesis of Alzheimer’s disease. The β-amyloid protein precursor (APP) is cleaved by three enzymes (TACE, BACE/BACE2 and γ-secretase) at three distinct sites (α, β and γ respectively). The γ-secretase complex is a membrane-bound aspartyl protease that can cleave certain proteins at peptide bonds buried within the hydrophobic environment of the lipid bilayer and is composed of the proteins APH1, nicastrin, PEN2 and presenilin1. Its cleavage of APP results in either the non-toxic p3 (from the α and γ cleavage site) or the toxic Aβ (from the β and γ cleavage site). APH1 was initially identified as a component of the Notch pathway and exists in at least three distinct isoforms with APH1a as the principal isoform present in the γ-secretase complex. Mice deficient in this isoform, but not the other two, were lethal at E10.5, with impaired vascular and neural development observed. Besides acting as a critical component of the γ-secretase complex, nicastrin is also thought to be involved in cell proliferation and signaling, especially in regards to activation of Notch receptors as loss of nicastrin expression results in mouse embryonic lethality. Presenilin1 was initially identified a marker of susceptibility to early-onset Alzheimer’s disease.;;For images please see PDF data sheet
Total Protein - Multiple Sclerosis Disease: Brain: Pons
Description: Accumulation of the amyloid-β peptide (Aβ) in the cerebral cortex is a critical event in the pathogenesis of Alzheimer’s disease. The βamyloid protein precursor (APP) is cleaved by one of two βsecretases (BACE and BACE2), producing a soluble derivative of the protein and a membrane anchored 99-amino acid carboxy-terminal fragment (C99). The C99 fragment serves as substrate for βsecretase to generate the 4 kDa amyloid-β peptide (Aβ), which is deposited in the Alzheimer’s disease patients’ brains. BACE was identified by several groups independently and designated β-site APP cleaving enzyme (BACE) . BACE is a transmembrane aspartic protease and co-localizes with APP. BACE2 also cleaves APP at β-site and at a different site within Aβ. BACE2 locates on chromosome 21q22.3, the so-called ‘Down critical region’, suggesting that BACE2 and Aβ may also contribute to the pathogenesis of Down syndrome.;;For images please see PDF data sheet
Description: A competitive ELISA for quantitative measurement of Rat Alzheimer associated neuronal thread protein in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Rat Alzheimer associated neuronal thread protein ELISA kit
Description: A competitive ELISA for quantitative measurement of Rat Alzheimer associated neuronal thread protein in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
Rat Alzheimer associated neuronal thread protein ELISA kit
Description: A competitive ELISA for quantitative measurement of Rat Alzheimer associated neuronal thread protein in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.
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This model system has been very successful in the case of post-mortem tissue because of their relative accessibility to acute brain slices or culture. The current review usage details synaptosomes in AD research and its potential as a valuable tool in furthering our understanding of the pathogenesis and in designing and testing therapeutic strategies for this disease.
