| pubmed-article:18410501 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18410501 | lifeskim:mentions | umls-concept:C0599772 | lld:lifeskim |
| pubmed-article:18410501 | lifeskim:mentions | umls-concept:C0886515 | lld:lifeskim |
| pubmed-article:18410501 | lifeskim:mentions | umls-concept:C0054871 | lld:lifeskim |
| pubmed-article:18410501 | lifeskim:mentions | umls-concept:C0027893 | lld:lifeskim |
| pubmed-article:18410501 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:18410501 | lifeskim:mentions | umls-concept:C1335528 | lld:lifeskim |
| pubmed-article:18410501 | lifeskim:mentions | umls-concept:C0033268 | lld:lifeskim |
| pubmed-article:18410501 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:18410501 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:18410501 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:18410501 | pubmed:dateCreated | 2008-7-2 | lld:pubmed |
| pubmed-article:18410501 | pubmed:abstractText | Neuropeptide Y (NPY) functions as a peptide neurotransmitter and as a neuroendocrine hormone. The active NPY peptide is generated in secretory vesicles by proteolytic processing of proNPY. Novel findings from this study show that cathepsin L participates as a key proteolytic enzyme for NPY production in secretory vesicles. Notably, NPY levels in cathepsin L knockout (KO) mice were substantially reduced in brain and adrenal medulla by 80% and 90%, respectively. Participation of cathepsin L in producing NPY predicts their colocalization in secretory vesicles, a primary site of NPY production. Indeed, cathepsin L was colocalized with NPY in brain cortical neurons and in chromaffin cells of adrenal medulla, demonstrated by immunofluorescence confocal microscopy. Immunoelectron microscopy confirmed the localization of cathepsin L with NPY in regulated secretory vesicles of chromaffin cells. Functional studies showed that coexpression of proNPY with cathepsin L in neuroendocrine PC12 cells resulted in increased production of NPY. Furthermore, in vitro processing indicated cathepsin L processing of proNPY at paired basic residues. These findings demonstrate a role for cathepsin L in the production of NPY from its proNPY precursor. These studies illustrate the novel biological role of cathepsin L in the production of NPY, a peptide neurotransmitter, and neuroendocrine hormone. | lld:pubmed |
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| pubmed-article:18410501 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18410501 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18410501 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18410501 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18410501 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:18410501 | pubmed:issn | 1471-4159 | lld:pubmed |
| pubmed-article:18410501 | pubmed:author | pubmed-author:PetersChristo... | lld:pubmed |
| pubmed-article:18410501 | pubmed:author | pubmed-author:ReinheckelTho... | lld:pubmed |
| pubmed-article:18410501 | pubmed:author | pubmed-author:ToneffThomasT | lld:pubmed |
| pubmed-article:18410501 | pubmed:author | pubmed-author:HwangShin-Ron... | lld:pubmed |
| pubmed-article:18410501 | pubmed:author | pubmed-author:HookVivianV | lld:pubmed |
| pubmed-article:18410501 | pubmed:author | pubmed-author:FunkelsteinLy... | lld:pubmed |
| pubmed-article:18410501 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18410501 | pubmed:volume | 106 | lld:pubmed |
| pubmed-article:18410501 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18410501 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18410501 | pubmed:pagination | 384-91 | lld:pubmed |
| pubmed-article:18410501 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
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