Altered expression and phosphorylation of amyloid precursor protein in heat shocked neuronal PC12 cells

Johnson, G.; Refolo, Lorenzo M.; Merril, Carl R.; Wallace, William

doi:10.1016/0169-328x(93)90159-m

Cited by 12 publications

(4 citation statements)

References 27 publications

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“…In summary, the HSP70-2 A2 allele appears to confer an increased liability to noncognitive symptoms in the dementia of Alzheimer's type. Since oxidative stress is extensive in AD pathology and an increased synthesis of HSP has been found in heat-shocked cells, 43 the association between HSP70-2 variation with behavioral alter-ations in AD patients is feasible under such pathophysiological conditions. As far as we know, these results represent the most clear relationship between a large group of noncognitive alterations presented in AD patients and a genetic polymorphism.…”

Section: Discussionmentioning

confidence: 99%

HSP70-2 (HSPA1B) is Associated with Noncognitive Symptoms in Late-Onset Alzheimer's Disease

Clarimón

Bertranpetit

Boada

et al. 2003

J Geriatr Psychiatry Neurol

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Neuropsychiatric manifestations are common in Alzheimer's disease (AD) and their phenotypic expression might be related to physiopathological and genetic causes. Multiple studies have implicated oxidative stress to the pathogenesis and possible etiology of AD. One of the mechanisms to protect cells from oxidative stress is the expression of heat-shock proteins (HSP). HSPA1B (alternatively known as HSP70-2) has been related to AD pathophysiology. In the present analysis, 77 AD patients were classified according to their cognitive status with the Neuropsychiatric Inventory and were genotyped for an insertion/deletion (A1/A2) polymorphism. The A2 allele conferred a significant increase of psychiatric morbidity in an allele-dose manner (P < .05). This pattern can be attributed to all AD stages and the severity of the behavioral disturbances was higher for those patients carrying one or two A2 alleles. These results indicate a possible association between the A2 allele and an overexpression of noncognitive symptoms in AD.

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Section: Discussionmentioning

confidence: 99%

HSP70-2 (HSPA1B) is Associated with Noncognitive Symptoms in Late-Onset Alzheimer's Disease

Clarimón

Bertranpetit

Boada

et al. 2003

J Geriatr Psychiatry Neurol

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“…The cytoplasmic domain of APP contains at least two serine residues which are phosphorylated by PKC (Gandy et al, 1988;Suzuki et al, 1992). Recently, it has reported that treatment of PC 12 cultures with the phorbol ester PMA resulted in a decrease in the phosphorylation of mature APP (Johnson et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

Study of the phorbol ester effect on Alzheimer amyloid precursor processing: Sequence requirements and involvement of a Cholera toxin sensitive protein

Efthimiopoulos

Felsenstein

Sambamurti

et al. 1994

J of Neuroscience Research

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Phorbol esters (PDBu) stimulate alpha-secretase cleavage and secretion of the Alzheimer amyloid precursor protein (APP). To determine whether any cytoplasmic residues or sequence motifs mediate the PDBu effect on APP processing, this region of APP was altered by point mutations or deletions. To differentiate the mutated APP from the endogenous APP, the APP751 ectodomain between amino acids 1 and 647 was replaced by a human secreted alkaline phosphatase derivative (SEAP). The resultant fusion protein (SEAP-APP751) was cleaved by alpha-secretase at the same site as full-length APP, and its secretion was stimulated by PDBu at a level similar to APP751. However, PDBu-stimulated secretion of the SEAP-APP751 fusion protein reached its maximum level after 30 min of treatment, while secretion of APP751 reached its maximum after 60 min, suggesting that the APP ectodomain affects the kinetics of APP secretion. Mutation of the cytoplasmic serines to alanines had no effect on the PDBu-stimulated secretion of the SEAP-APP, indicating that protein kinase C (PKC) phosphorylation of the cytoplasmic domain of APP is not important for stimulation of APP secretion. Similarly, deletion of the cytoplasmic domain between amino acids 719 and 751 had no effect on the PDBu-stimulated secretion. However, deletion of amino acids 707-751 resulted in a significant increase in the secretory cleavage of the SEAP-APP707 delta C construct, suggesting that the sequence 707-719 is important for the regulated secretion of APP. Cholera toxin, but not pertussis toxin, reduced the PDBu-induced secretion of APP by more than two-fold, suggesting that the PDBu response may be modulated by a cholera toxin sensitive heterotrimeric G-protein.

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“…Contrary to the beneficial effects in the aforementioned medical practice the thermal exposure upon brain has been proven deleterious and, in some cases, harmful to the functions of cerebral molecular expression [37,38]. Regarding the complication of neuronal degeneration like Alzheimer's and Huntington diseases caused by the toxic aggregation of amyloid β peptides alongside other aggregating molecules of genetically abnormal tau protein and FTDP-17, previous research indicated that treating neuron cells with mild hyperthermia up to the range of 42 • C to 45 • C reduces amyloidal protein-induced toxicity via the induction of heat shocked protein and down-regulation of amyloid proteins in the phosphorylated states [39,40]. Also, Bastus et.…”

Section: Discussionmentioning

confidence: 99%

Hyperthermia Induced by Near-Infrared Laser-Irradiated CsWO3 Nanoparticles Disintegrates Preformed Lysozyme Amyloid Fibrils

Tomašovičová

Chou

et al. 2020

Nanomaterials

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This research study attempts to prove the concept of the applicability of hyperthermia to treating the lysozyme amyloid fibrils (LAFs)’s self-assembled fibrillary aggregates by a feedback-modulated temperature controller ranging from 26 °C to 80 °C, and separately, by near-infrared (NIR) laser-irradiated cesium tungstate (CsWO3) nanoparticle (NPs). The dependence of the final morphology of the amyloidal assembly on external heating and the photothermal effect of the NPs on treating the fibrillary assembly were investigated and analyzed. Experimentally, atomic force microscopy (AFM), optical stereoscopy, and scanning electron microscopy (SEM) were used primarily to ensure mutual interaction between LAFs and NPs, optically elucidate the surface contour and final fibrillary assembly upon the influence of thermal treatment, and further reveal fine-details of the optical samples. Finally, conclusive remarks are drawn that the fibrillary structures doped with the NPs exhibit an increasing degree of unique orthogonality. As the temperature rises, utter deformation of the dendritic structures of fibrillary assemblies at 70 °C was found, and NIR laser-irradiated CsWO3 NPs have been demonstrated to be useful in topically destructing pre-assembled LAFs, which may be conducive to the future development of neurodegenerative therapeutic techniques.

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Altered expression and phosphorylation of amyloid precursor protein in heat shocked neuronal PC12 cells

Cited by 12 publications

References 27 publications

HSP70-2 (HSPA1B) is Associated with Noncognitive Symptoms in Late-Onset Alzheimer's Disease

HSP70-2 (HSPA1B) is Associated with Noncognitive Symptoms in Late-Onset Alzheimer's Disease

Study of the phorbol ester effect on Alzheimer amyloid precursor processing: Sequence requirements and involvement of a Cholera toxin sensitive protein

Hyperthermia Induced by Near-Infrared Laser-Irradiated CsWO3 Nanoparticles Disintegrates Preformed Lysozyme Amyloid Fibrils

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