Clusterin Has Chaperone-like Activity Similar to That of Small Heat Shock Proteins
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TLDR
The results suggest that clusterin may play a sHSP-like role in cytoprotection, and at physiological concentrations, clusterin potently protected glutathione S-transferase and catalase from heat-induced precipitation and α-lactalbumin and bovine serum albumin from precipitation induced by reduction with dithiothreitol.About:
This article is published in Journal of Biological Chemistry.The article was published on 1999-03-12 and is currently open access. It has received 435 citations till now. The article focuses on the topics: Clusterin & Heat shock protein.read more
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Amyloid β Protein and Alzheimer’s Disease: When Computer Simulations Complement Experimental Studies
Jessica Nasica-Labouze,Phuong H. Nguyen,Fabio Sterpone,Olivia Berthoumieu,Nicolae-Viorel Buchete,Sébastien Côté,Alfonso De Simone,Andrew J. Doig,Peter Faller,Angel E. Garcia,Alessandro Laio,Mai Suan Li,Simone Melchionna,Normand Mousseau,Yuguang Mu,Anant K. Paravastu,Samuela Pasquali,David J. Rosenman,Birgit Strodel,Bogdan Tarus,John H. Viles,Tong Zhang,Tong Zhang,Chunyu Wang,Philippe Derreumaux,Philippe Derreumaux +25 more
TL;DR: Simulations Complement Experimental Studies Jessica Nasica-Labouze, Phuong H. Nguyen, Fabio Sterpone,† Olivia Berthoumieu,‡ Nicolae-Viorel Buchete, Sebastien Cote, Alfonso De Simone, Andrew J. Doig, and Philippe Derreumaux are authors of this paper.
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Synthesis and functional analyses of nuclear clusterin, a cell death protein
TL;DR: The results indicate that an inactive precursor of nCLU exists in the cytoplasm of non-irradiated MCF-7 cells, translocates into the nucleus following IR, and induces apoptosis.
Journal ArticleDOI
Clusterin is a secreted mammalian chaperone.
TL;DR: The realization that clusterin is a novel HSP with chaperone activity is an exciting breakthrough, however, many questions remain, and the answers to these questions will keep many of us busy for years to come.
Journal ArticleDOI
Partial amino acid sequence of purified von Willebrand factor-cleaving protease.
TL;DR: Activity of vWF-cp is unusually stable during incubation at 37 degrees C; its in vitro half-life in citrated human plasma, heparin plasma, or serum is longer than 1 week; there was even a temporary increase in protease activity during the first 3 days of incubation.
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Antisense therapy for cancer.
Martin E. Gleave,Brett P. Monia +1 more
TL;DR: The ability of this class of drugs to significantly suppress target-gene expression is confirmed and better chemical modifications of antisense oligonucleotides increase resistance to nuclease digestion, prolong tissue half- Lives and improve scheduling.
References
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Alpha-crystallin can function as a molecular chaperone
TL;DR: It is shown that alpha-crystallin refracts light and protects proteins from aggregation in the transparent eye lens and that in nonlens cells alpha-Crystallin may have other functions in addition to its capacity to suppress aggregation of proteins.
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Induction of the TRPM-2 gene in cells undergoing programmed death.
Ralph Buttyan,Carl A. Olsson,J. Pintar,Chawnshang Chang,Mark G. Bandyk,Po-Ying Ng,Ihor S. Sawczuk +6 more
TL;DR: Although the function(s) of the products encoded by the TRPM-2 gene remains unclear, their presence provides a remarkable and early indicator of programmed cell death in many types of mammalian cells.
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Molecular structure and functional characterization of a human complement cytolysis inhibitor found in blood and seminal plasma: identity to sulfated glycoprotein 2, a constituent of rat testis fluid.
Dieter E. Jenne,J Tschopp +1 more
TL;DR: Functional studies with purified terminal complement components showed that CLI suppresses the cytolytic potential of nascent C5b-7 complexes at physiological blood plasma concentrations, suggesting that CLI protects sperm cells and epithelial tissues against complement attack in the male reproductive tract.
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Purification and characterization of a cell-aggregating factor (clusterin), the major glycoprotein in ram rete testis fluid.
TL;DR: It is shown that Sertoli cells in the seminiferous tubule are one potential source, since primary cultures of rat Sertolis cells secrete a protein having the same immunochemical and physical properties as clusterin isolated from ram rete testis fluid, which binds to concanavalin A-Sepharose and also to wheat germ agglutinin Sepharose.
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Clusterin (apoJ) alters the aggregation of amyloid β-peptide (Aβ1-42) and forms slowly sedimenting Aβ complexes that cause oxidative stress
Tomiichiro Oda,Pat Wals,Heinz H. Osterburg,Steven A. Johnson,Giulio Maria Pasinetti,Todd E. Morgan,Irina Rozovsky,Stine Wb,Seth W. Snyder,Thomas F. Holzman +9 more
TL;DR: This novel activity of slowly sedimenting Aβ may enhance the neurotoxicity of Aβ deposits in AD brains, because soluble complexes have a potential for diffusing to damage distal neurons.