Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-2-18
pubmed:abstractText
Axonal transport of puromycin-sensitive aminopeptidase (PSA), a putative neuropeptide degrading-enzyme which removes amino acid residues from the amino-terminal of neuropeptides, was examined in the proximal, middle, and distal segments of rat sciatic nerves using a double-ligation technique. The soluble fraction of each segment was partially purified by MonoQ column chromatography, and showed two peaks of aminopeptidase activity. One of the aminopeptidases was PSA. At 48 h after the ligations, a significant amount of the axonal transport of PSA activity was found in the proximal segment. Western blot analysis of the segments also showed that immunoreactive PSA in the proximal segment was 2.1-fold higher than that in the middle segment. Furthermore, the immunohistochemical analysis of the segments showed an increase of the immunoreactive PSA in the proximal segment in comparison with the enzyme in the distal segment, indicating that PSA is mainly transported by anterograde axonal flow. These results suggest that PSA plays a role in the metabolism of neuropeptides in nerve terminals or synaptic clefts.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0168-0102
pubmed:author
pubmed:issnType
Print
pubmed:volume
42
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
133-40
pubmed:dateRevised
2007-3-27
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Axonal transport of puromycin-sensitive aminopeptidase in rat sciatic nerves.
pubmed:affiliation
Laboratory of Natural Information Science, Graduate School of Integrated Science, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama 236-0027, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't