NDLI: Protease nexin-1, an antithrombin with neurite outgrowth activity, is reduced in Alzheimer disease.

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Localization of virus-specific and group-specific epitopes of plant potyviruses by systematic immunochemical analysis of overlapping peptide fragments.

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Concordant evolution of coding and noncoding regions of DNA made possible by the universal rule of TA/CG deficiency-TG/CT excess.

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Selective loss of cholinergic neurons in the ventral striatum of patients with Alzheimer disease.

Olfactory marker protein gene: its structure and olfactory neuron-specific expression in transgenic mice.

One-way analysis of variance with unequal variances.

Molecular cloning and sequence analysis of 3-hydroxy-3-methylglutaryl-coenzyme A reductase from the human parasite Schistosoma mansoni.

Structural mimicry of adenosine by the antitumor agents 4-methoxy- and 4-amino-8-(beta-D-ribofuranosylamino)pyrimido[5,4-d]pyrimidine as viewed by a molecular modeling method.

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Protease nexin-1, an antithrombin with neurite outgrowth activity, is reduced in Alzheimer disease.

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Hydrophobic effect in protein folding and other noncovalent processes involving proteins.

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Expression in transgenic plants of a viral gene product that mediates insect transmission of potyviruses.

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Specific photoaffinity labeling of two plasma membrane polypeptides with an azido auxin.

Phytochrome induces changes in the immunodetectable level of a wall peroxidase that precede growth changes in maize seedlings.

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Protease nexin-1, an antithrombin with neurite outgrowth activity, is reduced in Alzheimer disease.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Gurwitz, D. Wagner, S. L. Cunningham, D. D. Isackson, P. J. Lau, A. L. Geddes, J. W. Cotman, C. W.
Description	Author Affiliation: Wagner SL ( Department of Microbiology and Molecular Genetics, University of California, Irvine 92717.);
Abstract	Protease nexin-1 (PN-1) is a cell-secreted protein that inhibits certain proteases, particularly thrombin, by forming SDS-stable complexes with the catalytic site serine of the protease. PN-1 was recently shown to be identical to a glial-derived neurite-promoting factor/glial-derived nexin present in rat brain. Its neurite outgrowth activity depends on inhibition of thrombin, presumably because thrombin brings about neurite retraction. Here we show that human brain contains PN-1 and that PN-1 activity in brains of individuals with Alzheimer disease (AD) was only 14% of control values (total of 14 AD patients and 7 control individuals). PN-1 activity in the hippocampus, a region with marked neuropathology in AD, was 15% of control values (10 AD patients and 4 control individuals). Western blot analysis indicated a large decrease in free PN-1 protein and an increase in PN-1-containing complexes that comigrated with PN-1-thrombin complexes. Northern blot analysis indicated that PN-1 mRNA levels were about equal in brains from AD patients and control individuals. Thus these results suggest that the decreases in PN-1 activity and free PN-1 protein are due to formation of PN-1-protease complexes.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	21
Volume Number	86
Language	English
Publisher	National Academy of Sciences
Publisher Date	1989-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Alzheimer Disease Metabolism Axons Physiology Brain Carrier Proteins Plasminogen Activators Protease Inhibitors Amyloid Beta-Protein Precursor Genetics Hippocampus Immunoblotting Organ Specificity Protease Nexins RNA, Messenger Receptors, Cell Surface Reference Values Serpin E2 Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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