TY - JOUR
T1 - Processing and intracellular sorting of anglerfish and rat preprosomatostatins in mammalian endocrine cells
AU - Sevarino, Kevin A.
AU - Ventimiglia, Roseann
AU - Stork, Philip
N1 - Funding Information:
From the Department of Psychiatry, Yale University School of Medicine and the Connecticut Mental Health Center, New Haven, CT: and the Division ofM~~~ar Medicine, Deprtment OfMedicine, New Englartd Medics Center, Boston, MA. Supported by grants from the National Institutes of Health fDK31400, lPJOAM34928). K.A.S. was the recipient of a postdoctoral fellowship from the Juvenile Diabetes Foundation. Address reprint requests to Kevin A. Sevarino, MD, PhD, Department of Psychiatry, Yale University School of Medicine, 34 Park St, New Haven, CT 06508. 0 1990 by W.3. Saunders Company. 0026-049~~0/3909-2~~~03.00~
PY - 1990/9
Y1 - 1990/9
N2 - Rat preprosomatostatin (rPPSS) is processed to two distinct end products in a tissue-specific manner. The analogous end products in anglerfish are derived from separate precursors, anglerfish preprosomatostatins-1 and -2 (a(1)PPSS and a(II)PPSS). This report reviews experiments demonstrating that in mammalian cells, the cell of expression, not precursor structure, determines the processing fate of the preprosomatostatins. A fusion precursor of a(II)PPSS and rPPSS was expressed in mammalian cell lines to determine that the amino-terminal 78 residues of rPPSS contain a sorting signal that directs the precursor into a regulated secretory pathway wherein proteolytic processing occurs. Preliminary studies of rPPSS pro-region mutations are presented that attempt to further localize this sorting signal.
AB - Rat preprosomatostatin (rPPSS) is processed to two distinct end products in a tissue-specific manner. The analogous end products in anglerfish are derived from separate precursors, anglerfish preprosomatostatins-1 and -2 (a(1)PPSS and a(II)PPSS). This report reviews experiments demonstrating that in mammalian cells, the cell of expression, not precursor structure, determines the processing fate of the preprosomatostatins. A fusion precursor of a(II)PPSS and rPPSS was expressed in mammalian cell lines to determine that the amino-terminal 78 residues of rPPSS contain a sorting signal that directs the precursor into a regulated secretory pathway wherein proteolytic processing occurs. Preliminary studies of rPPSS pro-region mutations are presented that attempt to further localize this sorting signal.
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U2 - 10.1016/0026-0495(90)90203-O
DO - 10.1016/0026-0495(90)90203-O
M3 - Article
C2 - 1976215
AN - SCOPUS:0025002346
VL - 39
SP - 26
EP - 29
JO - Metabolism: Clinical and Experimental
JF - Metabolism: Clinical and Experimental
SN - 0026-0495
IS - 9 SUPPL. 2
ER -