Biosynthesis of neuropeptide Y in porcine tissues and generation of N-terminal fragments in neuroblastoma cell lines.
The biosynthesis of neuropeptide Y (NPY) was investigated to determine the efficiency of synthesis and processing of the precursor. In brain tissues examined, the major product was amidated NPY(1-36). Although this was also the major product in adrenal and heart atrium, a minor portion of the immunoreactivity was identified as unprocessed precursor. NPY degradation was investigated using SK-N-MC and SMS-MSN cells in conjunction with iodinated NPY tracers, labeled in either the tyrosine-1 or the tyrosine-36 position. Similar patterns of degradation were observed with both cell lines, and it would appear that the initial proteolytic attack on NPY(1-36) generates predominately N-terminal fragments.
O'Hare
M M
MM
University Department of Clinical Chemistry, Rigshospitalet 6321, Copenhagen, Denmark.
Schwartz
T W
TW
D000311:Adrenal Glands / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D001921:Brain / Q000378:metabolism; D006325:Heart Atria / Q000378:metabolism; D009447:Neuroblastoma / Q000378:metabolism; D009478:Neuropeptide Y / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism; D010446:Peptide Fragments / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism; D011498:Protein Precursors / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D011863:Radioimmunoassay; D013552:Swine; D014018:Tissue Distribution; D014407:Tumor Cells, Cultured
D009478:Neuropeptide Y; D010446:Peptide Fragments; D011498:Protein Precursors