p19 detected in the rat retina and pineal gland is a guanylyl cyclase-activating protein (GCAP).

• Authors: Agnieszka Dejda , Izabela Matczak , Wojciech A Gorczyca
• Languages of publication: EN

Abstracts

EN

The Ca2+-dependent activation of retina-specific guanylyl cyclase (retGC) is mediated by guanylyl cyclase-activating proteins (GCAPs). Here we report for the first time detection of a 19 kDa protein (p19) with GCAP properties in extracts of rat retina and pineal gland. Both extracts stimulate synthesis of cGMP in rod outer segment (ROS) membranes at low (30 nM) but not at high (1 mM) concentrations of Ca2+. At low Ca2+, immunoaffinity purified p19 activates guanylyl cyclase(s) in bovine ROS and rat retinal membranes. Moreover, p19 is recognized by antibodies against bovine GCAP1 and, similarly to other GCAPs, exhibits a Ca2+-dependent electrophoretic mobility shift.

Keywords

EN

pineal gland; rat; guanylyl cyclase; calcium-binding proteins; guanylyl cyclase-activating proteins; retina

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2002
• Volume: 49
• Issue: 4
• Pages: 899-905

Dates

published

2002

received

2002-11-19

revised

2002-11-30

accepted

2002-12-2

Contributors

author

Agnieszka Dejda

• Department of Biogenic Amines, Polish Academy of Sciences, Łódź, Poland

author

Izabela Matczak

• Department of Biogenic Amines, Polish Academy of Sciences, Łódź, Poland

author

Wojciech A Gorczyca

• Laboratory of Signaling Proteins, L. Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław, Poland

References

• Burgoyne RD, Weiss JL. (2001) The neuronal calcium sensor family of Ca2+-binding proteins. Biochem J.; 353: 1-12.
• Cuenca N, Lopez S, Howes K, Kolb H. (1998) The localization of guanylyl-cyclase-activating proteins in the mammalian retina. Invest Ophthalmol Vis Sci.; 39: 1243-50.
• Dizhoor AM, Lowe DG, Olshevskaya EV, Laura RP, Hurley JB. (1994) The human photoreceptor membrane guanylyl cyclase, RetGC, is present in outer segments and is regulated by calcium and a soluble activator. Neuron.; 12: 1345-52.
• Dizhoor AM, Olshevskaya EV, Henzel WJ, Wong S, Stults JT, Ankoudinova I, Hurley JM. (1995) Cloning, sequencing, and expressing of a 24-kDa Ca2+-binding protein activating photoreceptor guanylyl cyclase. J Biol Chem.; 270: 25200-6.
• Falcon J. (1999) Cellular circadian clocks in the pineal. Prog Neurobiol.; 58: 121-62.
• Frins S, Bonigk W, Muller F, Kellner R, Koch KW. (1996) Functional characterization of a guanylyl cyclase-activating protein from vertebrate rods. J Biol Chem.; 271: 8022-7.
• Gorczyca WA. (1999) Role of calcium ions in vertebrate phototransduction. Pol J Pharmacol.; 51: 167-72.
• Gorczyca WA. (2000) Use of nucleoside a-phosphorothioates in studies of photoreceptor guanylyl cyclase: purification of guanylyl cyclase-activating proteins. Methods Enzymol.; 315: 689-707.
• Gorczyca WA, Sokal I. (2002) GCAPs: Ca2+-sensitive regulators of retGC. In: Photoreceptors and calcium. Baehr W, Palczewski K, edn, Kluwer Academic Publishers (in press).
• Gorczyca WA, Gray-Keller MP, Detwiler PB, Palczewski K. (1994) Purification and physiological evaluation of guanylate cyclase activating protein from retinal rods. Proc Natl Acad Sci U S A.; 91: 4014-18.
• Gorczyca WA, Polans AS, Surgucheva I, Subbaraya I, Baehr W, Palczewski K. (1995) Guanylyl cyclase-activating protein: a calcium-sensitive regulator of phototransduction. J Biol Chem.; 270: 22029-36.
• Haeseleer F, Sokal I, Li N, Pettenati M, Rao N, Bronson D, Wechter R, Baehr W, Palczewski K. (1999) Molecular characterization of a third member of the guanylyl cyclase-activating protein subfamily. J Biol Chem.; 274: 6526-35.
• Koch K-W, Stryer L. (1988) Highly cooperative feedback control of retinal rod guanylate cyclase by calcium ions. Nature.; 334: 64-6.
• Lolley RN, Racz E. (1982) Calcium modulation of cyclic GMP synthesis in rat visual cells. Vision Res.; 22: 1481-86.
• McDowell JH. (1993) Preparing rod outer segment membranes, regenerating rhodopsin, and determining rhodopsin concentration. Methods Neurosci.; 15: 23-30.
• Meissl H. (1997) Photic regulation of pineal function. Analogies between retinal and pineal photoreception. Biol Cell.; 89: 549-54.
• Palczewski K, Subbaraya I, Gorczyca WA, Helekar BS, Ruiz CC, Ohguro H, Huang J, Zhao X, Crabb JW, Johnson RS, Walsh KA, Gray-Keller MP, Detwiler PB, Baehr W. (1994) Molecular cloning and characterization of retinal guanylyl cyclase-activating protein. Neuron.; 13: 395-404.
• Palczewski K, Polans AS, Baehr W, Ames JB. (2000) Ca2+-binding proteins in the retina: structure, function, and the etiology of human visual diseases. BioEssays.; 22: 337-50.
• Schoenmakers TJ, Visser GJ, Flik G, Theuvenet AP. (1992) CHELATOR: an improved method for computing metal ion concentrations in physiological solutions. Biotechniques.; 12: 870-9.
• Semple-Rowland SL, Larkin P, Bronson JD, Nykamp K, Streit WJ, Baehr W. (1999) Characterization of the chicken GCAP gene array and analyses of GCAP1, GCAP2, and GC1 gene expression in normal and rd chicken pineal. Mol. Vis.; 5: 14.
• Tosini G, Doyle S, Geusz M, Menaker M. (2000) Induction of photosensitivity in neonatal rat pineal gland. Proc Natl Acad Sci U S A.; 97: 11540-4.
• Venkataraman V, Duda T, Sharma RK. (1998) The alpha2D/A-adrenergic receptor-linked membrane guanylate cyclase: a new signal transduction system in the pineal gland. FEBS Lett.; 427: 69-73.
• Venkataraman V, Nagele R, Duda T, Sharma RK. (2000) Rod outer segment membrane guanylate cyclase type 1-linked stimulatory and inhibitory calcium signaling systems in the pineal gland: biochemical, molecular, and immunohistochemical evidence. Biochemistry.; 39: 6042-52.
• Zawilska JB, Rosiak J, Senderecka M, Nowak JZ. (1997) Suppresive effect of NMDA receptor antagonist MK-801 on nocturnal serotonin N-acetyltransferase activity in the rat pineal gland. Pol J Pharmacol.; 49: 479-83.