Vasopressin and bradykinin regulate secretory processing of the amyloid protein precursor of Alzheimer's disease

Neurochemical Research

Volumn 23, Issue 5, 1998, Pages 807-814

  Nitsch, Roger M ^a,e   Kim, Cindy ^b   Growdon, John H ^c,d  

^a UNIVERSITY OF HAMBURG   (Germany)

^b Dept of Brain and Cogn Sciences ^*

^c MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^d MASSACHUSETTS GENERAL HOSPITAL   (United States)

^e UNIVERSITY MEDICAL CENTER HAMBURG EPPENDORF   (Germany)

Author keywords

secretase processing; Alzheimer's Disease; Amyloid; Bradykinin; Neuropeptides; Receptors; Vasopressin

Indexed keywords

AMYLOID PRECURSOR PROTEIN; BRADYKININ; VASOPRESSIN;

ALZHEIMER DISEASE; ANIMAL TISSUE; ARTICLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PROCESSING; PROTEIN SECRETION; RAT;

ALZHEIMER DISEASE; AMYLOID BETA-PROTEIN; AMYLOID BETA-PROTEIN PRECURSOR; AMYLOID PRECURSOR PROTEIN SECRETASES; ANIMALS; ARGININE VASOPRESSIN; BRADYKININ; CELL LINE; ENDOPEPTIDASES; GTP-BINDING PROTEINS; INOSITOL; INOSITOL PHOSPHATES; KIDNEY; KINETICS; NEUROPEPTIDES; PC12 CELLS; PHOSPHATIDYLINOSITOLS; PROTEIN KINASE C; PROTEIN PROCESSING, POST-TRANSLATIONAL; RATS; RECEPTORS, BRADYKININ; RECEPTORS, VASOPRESSIN; SIGNAL TRANSDUCTION;

EID: 0031898094     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1022423813362     Document Type: Article

References (34)

1. Borkowski, J. A., Ransom, R. W., Seabrook, G. R., Trumbauer, M., Chen, H., Hill, R. G., Strader, C. D., and Hess, J. F. 1995. Targeted disruption of a B2 bradykinin receptor gene in mice eliminates bradykinin action in smooth muscle and neurons. J. Biol. Chem. 270:13706-13710.
2. Jones, S., Brown, D. A., Milligan, G., Willer, E. Buckley, N. J. and Caulfield, M. P. 1995. Bradykinin excited rat sympathetic neurons by inhibition of M current through a mechanism involving B2 receptors and G alpha q/11. Neuron 14:399-405.
3. Weinreich, D., Koschorke, G. M., Undem, B. J., and Taylor, G. E. 1995. Prevention of the excitatory actions of bradykinin by inhibition of PG12 formation in nodose neurones of the guinea pig. J. Physiol. 483:735-746.
4. 2 bradykinin binding sites on cultured cortical astrocytes. J. Neurochem. 57:1456-1458.
5. 9 bradykinin modulates DNA synthesis, phospholipase C, and protein kinase C in cultured mesangial cells. J. Biol. Chem. 266:21037-21043.
6. Suh, B. C., Lee, C. O., and Kim, K. T. 1995. Signal flows from two phospholipase C-linked receptors are independent in PC-12 cells. J. Neurochem. 64:1071-1079.
7. 2+ entry by tyrosine kinase inhibitors. J. Biol. Chem. 268:9945-9948.
8. 2 bradykinin receptor. Proc. Natl. Acad. Sci. USA 88:7724-7728.
9. 1 bradykinin receptor. J. Biol. Chem. 269:21583-21586.
10. 2 bradykinin receptor expressed by PC12 pheochromocytoma cells. Proc. Natl. Acad. Sci. USA 91: 4412-4416.
11. Morel, A., O'Carroll, A.-M., Brownstein, M. J., and Lolait, S. J. 1992. Molecular cloning and expression of a rat Via arginine vasopressin receptor. Nature 356:356-526.
12. Briley, E. M., Lolait, S. J., Axelrod, J., and Felder, C. C. 1994. The cloned vasopressin Via receptor stimulates phospholipase A2, phospholipase C, and phospholipase D through activation of receptor-operated calcium channels. Neuropeptides 27:63-74.
13. Lolait, S. J., O'Carroll, A. M., Mahan, L. C., Felder, C. C., Button, D. C., Young, W. S. 3rd., Mezey, E., and Brownstein, W. J. 1995. Extrapituitary expression of the rat V1b vasopressin receptor gene. Proc. Natl. Acad. Sci. USA 92:6783-6787.
14. Ostrowski, N. L., Lolait, S. J., and Young, W. S. 3rd 1994. Cellular localization of vasopressin V1a receptor messenger ribonucleic acid in adult male rat brain. Endocrinology 135:1511-1528.
15. Lolait, S. J., O'Carroll, A.-M., McBride, O. W., Konig, M., Morel, A., and Brownstein, M. J. 1992. Cloning and characterization of a vasopressin V2 receptor; chromosomal localization of gene suggests link to hereditary nephrogenic diabetes insipidus. Nature 357:336-339.
16. Sisodia, S. S., Koo, E. H., Beyreuther, K., Unterbeck, A., and Price, D. L. 1990. Evidence that β-amyloid protein of Alzheimer's disease is not derived by normal processing. Science 248:492-495.
17. Hung, A. Y., Haass, C., Nitsch, R. M., Qiao Qiu, W., Citron, M., Wurtman, R. J., Growdon, J. H., and Selkoe, D. J. 1993. Activation of protein kinase C inhibits cellular production of the amyloid β-protein. J. Biol. Chem. 268:22959-22962.
18. Gabuzda, D., Busciglio, J., and Yankner, B. A. 1993. Inhibition of β-amyloid production by activation of protein kinase C. J. Neurochem. 61:2326-2329.
19. Wolf, B. A., Wertkin, A. M., Jolly, Y. C., Yasuda, R. P., Wolfe, B. B., Konrad, R. J., Manning, D., Ravi, S., Williamson, J. R., and Lee, V. M. Y. 1995. Muscarinic regulation of Alzheimer's disease amyloid precursor protein secretion and amyloid beta-protein production in human neuronal NT2N cells. J. Biol. Chem. 270:4916-4922.
20. Farber, S. A., Nitsch, R. M., Schulz, J. G., and Wurtman, R. J. 1995. Regulated secretion of β-amyloid precursor protein in rat brain. J. Neurosci. 15:7442-7450.
21. Nitsch, R. M. and Growdon, J. H. 1994. Role of neurotransmission in the regulation of amyloid β-protein precursor processing. Biochem. Pharmacol. 47:1275-1284.
22. Nitsch, R. M., Slack, B. E., Wurtman, R. J., and Growdon, J. H. 1992. Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors. Science 258:304-307.
23. Nitsch, R. M., Deng, M., Growdon, J. H., and Wurtman, R. J. 1996. Serotonin 5-HT2a and 5-HT2c receptors stimulate amyloid precursor protein ectodomain secretion. J. Biol. Chem. 271:4188-4194.
24. Nitsch, R. M., Deng, A., Wurtman, R. J., and Growdon, J. H. 1997. Metabotropic glutamate receptor subtype mGluR1α stimulates the secretion of the amyloid beta protein precursor ectodomain. J. Neurochem. in press.
25. Nitsch, R. M., Farber, S. A., Growdon, J. H., and Wurtman, R. J. 1993. Release of amyloid β-protein precursor derivatives from hippocampal slices by electrical depolarization. Proc. Natl. Acad. Sci. USA 90:5191-5193.
26. Lee, R. K. K., Wurtman, R. J., Slack, B. E., Cox, A. J., and Nitsch, R. M. 1995. Amyloid precursor protein processing is stimulated by metabotropic glutamate receptors. Proc. Natl. Acad. Sci. USA 92:8083-8087.
27. Emmerling, M. R., Moore, C. J., Doyle, P. D., Carroll, R. T., and Davis, R. E. 1993. Phospholipase A2 activation influences the processing and secretion of the amyloid precursor protein. Biochem. Biophys. Res. Commun. 197:292-297.
28. Slack, B. E., Breu, J., Petryniak, M. A., Srivastava, K., and Wurtman, R. J. 1995. Tyrosine phosphorylation-dependent stimulation of amyloid precursor protein secretion by the m3 muscarinic aceltylcholine receptor. J. Biol. Chem. 270:8337-8344.
29. Slunt, H. H., Thinakaran, G., Von Koch, C., Lo, A. C. Y., Tanzi, R. E., and Sisodia, S. S. 1994. Expression of a ubiquitous, cross-reactive homologue of the mouse beta-amyloid precursor protein (APP). J. Biol. Chem. 269:2637-2644.
30. Xu, H., Greengard, P., and Gandy, S. 1995. Regulated formation of Golgi secretory vesicles containing Alzheimer beta-amyloid precursor protein. J. Biol. Chem. 270:23243-23245.
31. Milward, E. A., Papadopoulos, R., Fuller, S. J., Moir, R. D., Small, D., Beyreuther, K., and Masters, C. L. 1992. The amyloid protein precursor of Alzheimer's disease is a mediator of the effects of nerve growth factor on neunte outgrowth. Neuron 9:129-137.
32. Zheng, H., Jiang, M. H., Trumbauer, M. E., Sirinathsinghji, D. J. S., Hopkins, R., Smith, D. W., Heavens, R. P., Dawson, G. R., Boyce, S., Conner, M. W., Stevens, K. A., Slunt, H. H., Sisodia, S. S., Chen, H. Y., and Van der Ploeg, L. H. T. 1995. Betaamyloid precursor protein-deficient mice show reactive gliosis and decreased locomotor activity. Cell 81:525-531.
33. Goate, A. Chartier-Harlin, M.-C. Mullan, M. Broen, J. Crawford, F. Fidani, L. Giuffra, L. Hayes, A. Irving, N. James, L. Mant, R. Newton, P. Rooke, K. Roques, P. Talbot, C. Pericak-Vance, M. Roses, A. Williamson, R. Rossor, M. Owen, M., and Hardy, J. 1991. Segregation of a missense mutation in the amyloid precursor gene with familial Alzheimer's disease. Nature 349:704-706.
34. Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W., Larson, E., Levy-Lahad, E., Viitanan, M., Peskind, E., Poorkaj, P., Schellenberg, G., Tanzi, R., Wasco, W., Lannfelt, L., Selkoe, D., and Younkin, S. 1996. Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nature Med. 2:850-852.