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OPNP  -  opsin, pineal

Gallus gallus

Synonyms: OPN1LW, protan)
 
 
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Disease relevance of OPN1LW

 

High impact information on OPN1LW

 

Biological context of OPN1LW

  • The addition of egg phosphatidylcholine to P-opsin had little effect on the activation kinetics; however, the intrinsic rate of decay in the absence of transducin was accelerated [5].
  • The deduced pigeon P-opsin lacks a potential N-glycosylation site in the N-terminus, but has multiple phosphorylation sites in the C-terminus, which are opposite from the characteristics of the chicken P-opsin [6].
  • Thus, whereas the daily rhythm of pinopsin gene expression is dually regulated by light plus the intrapineal circadian oscillator, that of melanopsin appears to depend solely on the oscillator [7].
  • The high level of identity with opsins in both the transmembrane regions, where the chromophore binding site is located, and the intracellular loops, where the G-proteins interact, suggests that both melanopsin and pinopsin should be able to generate a stable photopigment, capable of triggering a transduction cascade mediated by G-proteins [8].
  • A light-responsive element was found in the promoter region of the Pinopsin gene, and the element included a CACGTG E-box, suggesting a novel role of the E-box as a point of convergence of light and circadian signals [9].
 

Anatomical context of OPN1LW

  • To study the function of this protein, an epitope-tagged P-opsin was stably expressed in an embryonic chicken pineal cell line [5].
  • These cCRY4 features strikingly contrast with those of the chick pineal photoreceptor pinopsin, suggesting a possible temporal and/or spatial duplicity of the pineal photoreceptive system, the opsin- and CRY-based mechanisms [10].
  • In Western blot analysis, the antibody stained a single band of 42-kDa protein in a detergent-extract of chicken pineal membranes, suggesting that pinopsin (calculated molecular weight, 38187) might be glycosylated and/or palmitoylated [11].
 

Associations of OPN1LW with chemical compounds

  • P-opsin is a seven-membrane spanning, G protein-linked receptor with a Schiff-base lysine in the seventh membrane span and a Schiff-base counterion in the third membrane span [4].
  • The pineal gland expresses a unique member of the opsin family (P-opsin; Max, M., McKinnon, P. J., Seidenman, K. J., Barrett, R. K., Applebury, M. L., Takahashi, J. S., and Margolskee, R. F. (1995) Science 267, 1502-1506) that may play a role in circadian entrainment and photo-regulation of melatonin synthesis [5].
  • P-opsin bleached slowly in the dark (t1/2 = 2 h) in the presence of 50 mM hydroxylamine [5].
  • Purified P-opsin in dodecyl maltoside activated rod transducin in a light-dependent manner, catalyzing the exchange of more than 300 mol of GTPgammaS (guanosine 5'-O-(3-thiotriphosphate))/mol of P-opsin [5].
  • Pinopsin mRNA levels are significantly elevated in the pineal glands of chickens carrying a null mutation in guanylate cyclase-1 [12].
 

Other interactions of OPN1LW

 

Analytical, diagnostic and therapeutic context of OPN1LW

  • In this paper, the localization of alpha-subunits of G-proteins, rod transducin (Gt1) and Gq/11, was examined by immunoelectron microscopy to investigate whether these G-proteins colocalize with pinopsin in the outer segments [15].
  • In the present study, we investigated the amino acid residue(s) contributing to this unique property of pinopsin by using site-directed mutagenesis to pinopsin-specific structural features, (i) Ser171, (ii) Asn184, and (iii) the second extracellular loop two-amino acids shorter than that of cone visual pigments [16].
  • Subsequently, using RT-PCR and RPA analysis, we verified the expression of ruin lizard melanopsin and pinopsin in directly photosensitive organs, such as the lateral eye, brain, pineal gland and parietal eye [8].
  • For the immunocytochemistry, we raised antibodies in rabbits against a 14 amino acids containing part of the chicken pinopsin molecule [2].

References

  1. Rod-type transducin alpha-subunit mediates a phototransduction pathway in the chicken pineal gland. Kasahara, T., Okano, T., Yoshikawa, T., Yamazaki, K., Fukada, Y. J. Neurochem. (2000) [Pubmed]
  2. Immunoreactive pinopsin in pineal and retinal photoreceptors of various vertebrates. Fejér, Z., Szél, A., Röhlich, P., Görcs, T., Manzano e Silva, M.J., Vígh, B. Acta. Biol. Hung. (1997) [Pubmed]
  3. Pinopsin is a chicken pineal photoreceptive molecule. Okano, T., Yoshizawa, T., Fukada, Y. Nature (1994) [Pubmed]
  4. Pineal opsin: a nonvisual opsin expressed in chick pineal. Max, M., McKinnon, P.J., Seidenman, K.J., Barrett, R.K., Applebury, M.L., Takahashi, J.S., Margolskee, R.F. Science (1995) [Pubmed]
  5. Light-dependent activation of rod transducin by pineal opsin. Max, M., Surya, A., Takahashi, J.S., Margolskee, R.F., Knox, B.E. J. Biol. Chem. (1998) [Pubmed]
  6. Molecular characterization of the pigeon P-opsin gene. Kawamura, S., Yokoyama, S. Gene (1996) [Pubmed]
  7. Circadian gene expression patterns of melanopsin and pinopsin in the chick pineal gland. Holthues, H., Engel, L., Spessert, R., Vollrath, L. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  8. Isolation and characterization of melanopsin and pinopsin expression within photoreceptive sites of reptiles. Frigato, E., Vallone, D., Bertolucci, C., Foulkes, N.S. Naturwissenschaften (2006) [Pubmed]
  9. Chicktacking pineal clock. Okano, T., Fukada, Y. J. Biochem. (2003) [Pubmed]
  10. Molecular cloning, mRNA expression, and immunocytochemical localization of a putative blue-light photoreceptor CRY4 in the chicken pineal gland. Kubo, Y., Akiyama, M., Fukada, Y., Okano, T. J. Neurochem. (2006) [Pubmed]
  11. Immunocytochemical identification of pinopsin in pineal glands of chicken and pigeon. Okano, T., Takanaka, Y., Nakamura, A., Hirunagi, K., Adachi, A., Ebihara, S., Fukada, Y. Brain Res. Mol. Brain Res. (1997) [Pubmed]
  12. Pinopsin mRNA levels are significantly elevated in the pineal glands of chickens carrying a null mutation in guanylate cyclase-1. Semple-Rowland, S.L., Tepedino, M., Coleman, J.E. Brain Res. Mol. Brain Res. (2001) [Pubmed]
  13. Chimeric nature of pinopsin between rod and cone visual pigments. Nakamura, A., Kojima, D., Imai, H., Terakita, A., Okano, T., Shichida, Y., Fukada, Y. Biochemistry (1999) [Pubmed]
  14. Light-dependent expression of pinopsin gene in chicken pineal gland. Takanaka, Y., Okano, T., Iigo, M., Fukada, Y. J. Neurochem. (1998) [Pubmed]
  15. Colocalization of pinopsin with two types of G-protein alpha-subunits in the chicken pineal gland. Matsushita, A., Yoshikawa, T., Okano, T., Kasahara, T., Fukada, Y. Cell Tissue Res. (2000) [Pubmed]
  16. Regulatory mechanism for the stability of the meta II intermediate of pinopsin. Nakamura, A., Kojima, D., Okano, T., Imai, H., Terakita, A., Shichida, Y., Fukada, Y. J. Biochem. (2001) [Pubmed]
 
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