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Cloning of an unusual natriuretic peptide from the South American coral snake Micrurus corallinus.
Eur J Biochem. 1997 Nov 15; 250(1):144-9.EJ

Abstract

In the course of cloning abundant cDNAs from the South American coral snake Micrurus corallinus venom gland, we characterized a cDNA coding for a putative natriuretic peptide. All the natural natriuretic peptides described so far, possess a ring structure composed of 17 amino acids formed through an S-S bridge which is extended at the N-terminus by few to several amino acids and may be extended at the C-terminus, usually 4-7 amino acids. In contrast, the M. corallinus natriuretic peptide presents several distinct features: (a) the proform of the deduced natriuretic peptide displays an unusual C-terminus extension. This implies that the mature peptide has a long C-terminal tail or it is further extensively processed to result in the mature natriuretic peptide with the expected 4-7 amino-acid extension. (b) the deduced natriuretic peptide presents an unusual internal Cys within the ring structure. This raises the possibility of natriuretic peptides with a smaller ring structure. (c) the putative natriuretic peptide is flanked by two homologous peptides of unknown function. In addition, an analogous peptide was synthesized and assayed on perfused rat kidney, showing a dose-dependent response in urinary volume and sodium excretion. Moreover, northern-blot studies showed that M. corallinus natriuretic peptide transcripts were highly expressed in venom glands, but they were not detectable in other tissues like heart and brain, suggesting a main role for this M. corallinus natriuretic peptide in the venom gland or in the envenomation by this coral snake's bite.

Authors+Show Affiliations

Centro de Biotecnologia, Instituto Butantan, São Paulo, Brazil.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

9432002

Citation

Ho, P L., et al. "Cloning of an Unusual Natriuretic Peptide From the South American Coral Snake Micrurus Corallinus." European Journal of Biochemistry, vol. 250, no. 1, 1997, pp. 144-9.
Ho PL, Soares MB, Maack T, et al. Cloning of an unusual natriuretic peptide from the South American coral snake Micrurus corallinus. Eur J Biochem. 1997;250(1):144-9.
Ho, P. L., Soares, M. B., Maack, T., Gimenez, I., Puorto, G., Furtado, M. F., & Raw, I. (1997). Cloning of an unusual natriuretic peptide from the South American coral snake Micrurus corallinus. European Journal of Biochemistry, 250(1), 144-9.
Ho PL, et al. Cloning of an Unusual Natriuretic Peptide From the South American Coral Snake Micrurus Corallinus. Eur J Biochem. 1997 Nov 15;250(1):144-9. PubMed PMID: 9432002.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cloning of an unusual natriuretic peptide from the South American coral snake Micrurus corallinus. AU - Ho,P L, AU - Soares,M B, AU - Maack,T, AU - Gimenez,I, AU - Puorto,G, AU - Furtado,M F, AU - Raw,I, PY - 1998/2/7/pubmed PY - 1998/2/7/medline PY - 1998/2/7/entrez SP - 144 EP - 9 JF - European journal of biochemistry JO - Eur. J. Biochem. VL - 250 IS - 1 N2 - In the course of cloning abundant cDNAs from the South American coral snake Micrurus corallinus venom gland, we characterized a cDNA coding for a putative natriuretic peptide. All the natural natriuretic peptides described so far, possess a ring structure composed of 17 amino acids formed through an S-S bridge which is extended at the N-terminus by few to several amino acids and may be extended at the C-terminus, usually 4-7 amino acids. In contrast, the M. corallinus natriuretic peptide presents several distinct features: (a) the proform of the deduced natriuretic peptide displays an unusual C-terminus extension. This implies that the mature peptide has a long C-terminal tail or it is further extensively processed to result in the mature natriuretic peptide with the expected 4-7 amino-acid extension. (b) the deduced natriuretic peptide presents an unusual internal Cys within the ring structure. This raises the possibility of natriuretic peptides with a smaller ring structure. (c) the putative natriuretic peptide is flanked by two homologous peptides of unknown function. In addition, an analogous peptide was synthesized and assayed on perfused rat kidney, showing a dose-dependent response in urinary volume and sodium excretion. Moreover, northern-blot studies showed that M. corallinus natriuretic peptide transcripts were highly expressed in venom glands, but they were not detectable in other tissues like heart and brain, suggesting a main role for this M. corallinus natriuretic peptide in the venom gland or in the envenomation by this coral snake's bite. SN - 0014-2956 UR - https://www.unboundmedicine.com/medline/citation/9432002/Cloning_of_an_unusual_natriuretic_peptide_from_the_South_American_coral_snake_Micrurus_corallinus_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0014-2956&date=1997&volume=250&issue=1&spage=144 DB - PRIME DP - Unbound Medicine ER -