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In Vivo Neuronal Synthesis and Axonal Transport of Kunitz Protease Inhibitor (KPI)‐Containing Forms of the Amyloid Precursor Protein
Author(s) -
Moya Kenneth L.,
Confaloni AnnaMaria,
Allinquant Bernadette
Publication year - 1994
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1994.63051971.x
Subject(s) - amyloid precursor protein , chemistry , protease inhibitor (pharmacology) , in vivo , amyloid (mycology) , protease , biochemistry , amyloid precursor protein secretase , biophysics , microbiology and biotechnology , neuroscience , alzheimer's disease , biology , enzyme , pathology , medicine , immunology , disease , human immunodeficiency virus (hiv) , antiretroviral therapy , viral load , inorganic chemistry
We have shown previously that the amyloid precursor protein (APP) is synthesized in retinal ganglion cells and is rapidly transported down the axons, and that different molecular weight forms of the precursor have different developmental time courses. Some APP isoforms contain a Kunitz protease inhibitor (KPI) domain, and APP that lacks the KPI domain is considered the predominant isoform in neurons. We now show that, among the various rapidly transported APPs, a 140‐kDa isoform contains the KPI domain. This APP isoform is highly expressed in rapidly growing retinal axons, and it is also prominent in adult axon endings. This 140‐kDa KPI‐containing APP is highly sulfated compared with other axonally transported isoforms. These results show that APP with the KPI domain is a prominent isoform synthesized in neurons in vivo, and they suggest that the regulation of protease activity may be an important factor during the establishment of neuronal connections.