Tissue distribution and processing of proSAAS by proprotein convertases

Journal of Neurochemistry

Volumn 76, Issue 6, 2001, Pages 1833-1841

  Sayah, M ^a   Fortenberry, Y ^a   Cameron, A ^a   Lindberg, I ^a  

^a LOUISIANA STATE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Convertase; Furin post translational processing neuropeptide; PC1; PC2; ProSAAS

Indexed keywords

BINDING PROTEIN; CARBOXYPEPTIDASE; FURIN; HEXAPEPTIDE; NEUROPEPTIDE;

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; HYPOPHYSIS; HYPOTHALAMUS; IMMUNOREACTIVITY; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN PROCESSING; PROTEIN STRUCTURE; TISSUE DISTRIBUTION;

AMINO ACID SEQUENCE; ANIMALS; ASPARTIC ENDOPEPTIDASES; BRAIN; CHO CELLS; CRICETINAE; ENZYME PRECURSORS; FURIN; MICE; MOLECULAR SEQUENCE DATA; NEUROPEPTIDES; PEPTIDE FRAGMENTS; PROPROTEIN CONVERTASE 1; PROPROTEIN CONVERTASE 2; PROPROTEIN CONVERTASES; PROTEIN PRECURSORS; PROTEIN PROCESSING, POST-TRANSLATIONAL; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; SUBTILISINS; TRANSFECTION; TRYPSIN;

ANIMALIA;

EID: 0035109058     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2001.00165.x     Document Type: Article

References (21)

1. Cholecystokinin (CCK) levels are greatly reduced in the brains but not the duodenums of Cpe (fat)/Cpe (fat) mice: A regional difference in the involvement of carboxypeptidase E (Cpe) in pro-CCK processing
2. Polyarginines are potent furin inhibitors
3. The SAAS granin exhibits structural and functional homology to 7B2 and contains a highly potent hexapeptide inhibitor of PC1
4. The tissue distribution of rat chromogranin A-derived peptides: Evidence for differential tissue processing from sequence specific antisera
5. Distribution and regulation of the prohormone convertases PC1 and PC2 in the rat pituitary
6. Immunological studies on the distribution of chromogranin A and B in endocrine and nervous tissues
7. The role of the 7B2 CT peptide in the inhibition of prohormone convertase 2 in endocrine cell lines
8. Identification and characterization of proSAAS, a granin-like neuroendocrine peptide precursor that inhibits prohormone processing
9. Immunolocalization of betagranin: A chromogranin A-related protein of the pancreatic B-cell
10. The proteolytic maturation of prohormone convertase 2 (PC2) is a pH-driven process
11. Purification and enzymatic characterization of recombinant prohormone convertase 2: Stabilization of activity by 21 kDa 7B2
12. Overexpression of neuropeptide precursors and processing enzymes
13. The neuroendocrine polypeptide 7B2 is an endogenous inhibitor of prohormone convertase PC2
14. The cell biology of the prohormone convertases PC1 and PC2
15. The C-terminal region of proSAAS is a potent inhibitor of prohormone convertase 1
16. Proteolytic processing mechanisms in the biosynthesis of neuroendocrine peptides: The subtilisin-like proprotein convertases
17. Proprotein convertases (PC1/PC3 and PC2) in normal and neoplastic human tissues: Their use as markers of neuroendocrine differentiation
18. Proprotein and prohormone convertases: A family of subtilases generating diverse bioactive polypeptides
19. The neuroendocrine protein 7B2 is required for peptide hormone processing in vivo and provides a novel mechanism for pituitary Cushing's disease
20. Regional and cellular localization of the neuroendocrine prohormone convertases PC1 and PC2 in the rat central nervous system
21. The developmental expression in rat of proteases furin, PC1, PC2, and carboxypeptidase E: Implications for early maturation of proteolytic processing capacity