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amyloidosis/protease
Ο σύνδεσμος αποθηκεύεται στο πρόχειρο
Σελίδα 1 από 2584 Αποτελέσματα
Sprouting and abnormal contacts of nonmedullated axons, and deposition of extracellular material induced by the amyloid precursor protein (APP) and other protease inhibitors.
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Σύνδεση εγγραφή
We have reported that the local administration of serine protease inhibitors (amyloid precursor protein with the Kunitz insert (APP K+), aprotinin, and leupeptin) to the rat sciatic nerve determines a sprouting response of myelinated axons, proliferation of Schwann cells, and demyelination, 5 to 7
Actin, troponin C, Alzheimer amyloid precursor protein and pro-interleukin 1 beta as substrates of the protease from human immunodeficiency virus.
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Σύνδεση εγγραφή
We show here for the first time that actin, troponin C, Alzheimer amyloid precursor protein (AAP), and pro-interleukin 1 beta (pro-IL-1 beta), are substrates of the protease encoded by the human immunodeficiency virus (HIV) type-1. As has been seen in other non-viral protein substrates of the HIV
Protease nexin-II (amyloid beta-protein precursor): a platelet alpha-granule protein.
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Σύνδεση εγγραφή
Protease nexin-II (PN-II) [amyloid beta-protein precursor (APP)] and the amyloid beta-protein are major constituents of neuritic plaques and cerebrovascular deposits in individuals with Alzheimer's disease and Down syndrome. Both the brain and the circulation have been implicated as sources of these
Protease nexin-2/amyloid beta protein precursor. A tight-binding inhibitor of coagulation factor IXa.
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Σύνδεση εγγραφή
Protease nexin-2/amyloid beta protein precursor (PN-2/A beta PP) is an abundant, secreted platelet protein which is a potent inhibitor of coagulation Factor XIa. We examined other potential anticoagulant activities of PN-2/A beta PP. Purified Kunitz protease inhibitor domain of PN-2/A beta PP and
Amyloid precursor protein mRNA encoding the Kunitz protease inhibitor domain is increased by kainic acid-induced seizures in rat hippocampus.
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A 168-nucleotide exon, found in alternatively spliced amyloid precursor protein (APP) mRNAs, encodes a Kunitz protease inhibitor (KPI) domain. Kainic acid (ip) caused a selective increase of KPI mRNA in rat hippocampus. By in situ hybridization, KPI mRNA was induced in the neuronal layers of the
Fibrillar amyloid beta-protein binds protease nexin-2/amyloid beta-protein precursor: stimulation of its inhibition of coagulation factor XIa.
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Σύνδεση εγγραφή
Cerebrovascular deposition of fibrillar 39-42 amino acid amyloid beta-protein (Abeta), a condition known as cerebral amyloid angiopathy (CAA), is a key pathological feature of Alzheimer's disease and related disorders including hereditary cerebral hemorrhage with amyloidosis-Dutch type (HCHWA-D).
Recombinant Kunitz protease inhibitory domain of the amyloid beta-protein precursor as an anticoagulant in venovenous extracorporeal circulation in rabbits.
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Σύνδεση εγγραφή
Investigations were performed to characterize a recombinant Kunitz protease inhibitory domain of the amyloid beta-protein precursor (rKPI) as anticoagulants. After a single intravenous infusion of wild type rKPI into dogs, its elimination fit a two compartment model with a t1/2alpha and t1/2beta of
Potential role of protease nexin-2/amyloid beta-protein precursor as a cerebral anticoagulant.
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Σύνδεση εγγραφή
The amyloid beta-protein precursor (APP) is the parent molecule to the amyloid beta-protein which is a major constituent of neuritic plaques and cerebrovascular deposits in Alzheimer's disease (AD). The protease inhibitor, protease nexin-2 (PN-2), is the secreted form of APP that contains the Kunitz
Cathepsin protease activity modulates amyloid load in extracerebral amyloidosis.
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Σύνδεση εγγραφή
In cerebral amyloidoses, such as Alzheimer's disease, proteolytic processing of the precursor protein is a fundamental mechanism of the disease, since it generates the amyloid protein. However, the putative significance of proteases in extracerebral amyloidoses is less well defined. In this study,
A novel brain cysteine protease forms an SDS stable complex with the beta-amyloid precursor protein.
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Σύνδεση εγγραφή
Alzheimer's disease (AD) brain accumulates beta-protein (A beta) a peptide proteolytically derived from the beta-amyloid precursor protein (APP). The abnormal production and aggregation of A beta have been implicated in the pathogenesis of the disease. The mechanism of production of A beta in vivo
Accelerated amyloid deposition in mice treated with the aspartic protease inhibitor, pepstatin.
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Σύνδεση εγγραφή
The development of amyloidotic diseases is believed to be determined in large part by the structure and metabolism of the amyloid subunit protein. The amino-terminal region of serum amyloid A (SAA), the subunit precursor protein in reactive amyloidosis, appears to confer fibrillogenic potential.
The kunitz protease inhibitor form of the amyloid precursor protein (KPI/APP) inhibits the proneuropeptide processing enzyme prohormone thiol protease (PTP). Colocalization of KPI/APP and PTP in secretory vesicles.
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Proteolytic processing of proenkephalin and proneuropeptides is required for the production of active neurotransmitters and peptide hormones. Variations in the extent of proenkephalin processing in vivo suggest involvement of endogenous protease inhibitors. This study demonstrates that "protease
High level expression, purification, and characterization of the Kunitz-type protease inhibitor domain of protease nexin-2/amyloid beta-protein precursor.
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Σύνδεση εγγραφή
The protease inhibitor, protease nexin-2 (PN-2), is the secreted isoform of the Alzheimer's amyloid beta-protein precursor (A beta PP) that contains the Kunitz-type protease inhibitor (KPI) domain. Here we describe the use of the methylotrophic industrial yeast Pichia pastoris as a host system for
The protease inhibitory properties of the Alzheimer's beta-amyloid precursor protein.
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We have expressed the 57-amino acid Kunitz domain of the Alzheimer's beta-amyloid precursor protein (APP751) as a bacterial fusion protein. The protease inhibitory properties of the purified fusion protein, BX9, were virtually identical in all respects tested to those of purified secreted APP751.
Ca(2+)-dependent 68-kilodalton protease in familial Alzheimer's disease cells cleaves the N-terminus of beta-amyloid.
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Lymphoblastoid cells derived from patients with early- and late-onset familial Alzheimer's disease express a Ca(2+)-dependent, 68-kDa protease which forms an SDS-stable and heat-labile complex with the beta-amyloid precursor protein. Utilizing this property, we prepared the protein by
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