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Pharmacological and Surgical Interventions to Improve Brain Insulin Resistance
Published in André Kleinridders, Physiological Consequences of Brain Insulin Action, 2023
Linus Haberbosch, Lukas Maurer, Reiner Jumpertz-von Schwartzenberg
Numerous investigations targeting a potential link between central insulin resistance and the different pathological processes potentially underlying the ongoing neurodegenerative changes in diseases such as PD and AD have been performed. There has been shown to be evidence for a link between insulin resistance and alpha-synuclein (20) as well as tau (21) and beta-amyloid protein accumulation (22). This pathophysiological framework has prompted the hypothesis of an impaired insulin signaling to determine the brain’s vulnerability toward protein precursor accumulation associated toxicity (23).
Observing and Describing Disease
Published in Jeremy R. Jass, Understanding Pathology, 2020
In the case of solid organs such as the liver, kidney, thyroid gland or spleen, it is useful to classify disease appearances as: (1) focal (solitary), (2) multifocal or (3) diffuse. Multifocality means that several discrete lesions are separated by normal parenchyma whereas no entirely normal parenchyma is seen in a diffuse process. Examples of diffuse processes are provided in the end stage diseases (see Chapter 33), hyperplasia and hypertrophy (page 105), lobar pneumonia (page 77), congestion (page 113) and polycystic disease of kidney. Many diffuse patterns are caused by cells or cellular products spreading or infiltrating the interstitial spaces between parenchymal cells. White blood cells are adapted for such a mode of spread and will do so on a massive scale in haematological malignancies. Amyloidosis (page 92) is an example of diffuse deposition of a proteinaceous material derived from various types of protein precursor. With the notable exceptions of leukaemia, lymphoma and diffuse type gastric cancer, neoplasms are generally either focal (primary) or multifocal (secondary). Splenic lymphoma may selectively replace the white pulp to produce a multifocal pattern.
Plaques, Tangles and Amyloid:
Published in Robert E. Becker, Ezio Giacobini, Alzheimer Disease, 2020
Robert G. Struble, H. Brent Clark
In addition to the A4 peptide isolated from plaque cores, numerous other markers have been found including IgG, IgM, albumin and several globulins (Powers et al, 1981). Heparin sulfate proteoglycans have been immunohistochemically identified on the β-amyloid fibrils both in plaques and in cerebral amyloid angiopathy suggesting involvement of the extracellular matrix (Snow et al, 1988). Schubert et al, (1988), on the basis of amino acid sequence analysis, suggested that the β-protein precursor might be a heparin sulfate proteoglycan core protein. The presence of these other peptides in β-amyloid could result from either participation in SP formation, or entrapment of local peptides in the highly insoluble β-amyloid.
Research progress in the development of porcine reproductive and respiratory syndrome virus as a viral vector for foreign gene expression and delivery
Published in Expert Review of Vaccines, 2020
Guo Dai, Mei Huang, To Sing Fung, Ding Xiang Liu
Recombinant PRRSVs with a 9-aa hemagglutinin (HA) tag from human influenza A virus directly fused to the N-terminus or the C-terminus of the N protein were constructed based on the infectious cDNA clone of LV. However, those recombinant viruses expressing the HA epitope tended to be unstable and lose the inserted epitope simultaneously after subsequent cell passages. To solve the problem, additional sequences encoding the auto-protease 2A from the foot-and-mouth disease virus (FMDV) were inserted in-frame with the HA and ORF7 sequences. HA epitope could be expressed from a cleavable N protein precursor by the self-cleaving 2A protease [64]. This strategy not only successfully rescued the virus, but also controlled the stable expression of the HA tag [64]. Hence, ORF7 can be selected for the insertion of a foreign gene, but the size limit for foreign genes remains to be further studied.
Maximum likelihood approach suggests positive selection in platelet integrin αIIbβ3 in mammalian species
Published in Platelets, 2019
Luís Bernardo Pina-Cabral, Miguel Carneiro, Begoña Criado, Pedro José Esteves
The coding sequence for ααIIb-subunit is located on the long arm (q) of chromosome 17 (17q21.32), spanning 17324 bp. This gene (ITGA2B) contains 30 exons that will yield a single polypeptide precursor with 1039 residues which will undergo proteolytic cleavage into a heavy (871 residues) and a light chain (137 residues) linked by a disulfide bond. This mature protein is composed of 1008 residues [15,16]. The coding sequence for β3-subunit (ITGB3 gene) is adjacent to the ITGA2B gene on chromosome 17, spanning 58870 bp. It is composed of 15 exons that will yield a protein precursor with 788 residues. After an initial cleavage of 26 residues, the mature protein with 762 residues joins αIIb-subunit to form integrin αIIbβ3 which is incorporated into the membranes in its inactivated state [17,18]. The complete sequences of mature integrins αIIb and β3 from 10 mammalian species were retrieved from GenBank (see Figures 1 and 2) and were aligned using BioEdit software version 7.2.0 [19].
Effect of flavonoids rich extract of Capparis spinosa on inflammatory involved genes in amyloid-beta peptide injected rat model of Alzheimer's disease
Published in Nutritional Neuroscience, 2018
Nazanin Mohebali, Seyed Abolhassan Shahzadeh Fazeli, Hossein Ghafoori, Zeinab Farahmand, Elham MohammadKhani, Faezeh Vakhshiteh, Abdolreza Ghamarian, Mansoureh Farhangniya, Mohammad Hossein Sanati
Alzheimer's disease (AD) is known to be one of the most common chronic neurodegenerative diseases with pathological hallmarks of neuritic plaque and neurofibrillary tangles. These hallmarks are respectively related to the aggregation of the amyloid-beta peptide (Aβ) in brain tissue, and hyperphosphorylation of microtubule-associated tau protein in neurons.1 Several genetic and environmental factors are considered to be involved in amyloidogenic process. AD occurs as a result of Aβ peptide aggregation, which itself is caused by any mutation or malfunction in gamma- and beta-secretase enzymes. Any structural or functional alteration in genes encoding these two enzymes or their subunits could lead to Aβ aggregation. Gamma-secretase enzyme is consisted of four subunits including presenilin 1 and presenilin, which are encoded by PSEN-1 and PSEN-2, respectively. Beta-secretase enzyme is encoded by BACE-1 gene. These two enzymes are responsible for the cleavage of APP, which is the amyloid protein precursor.