Multiple bradykinin-related peptides from the skin of the frog, Rana temporaria

J. Michael Conlon; Ulrika Aronsson

doi:10.1016/S0196-9781(96)00339-7

Multiple bradykinin-related peptides from the skin of the frog, Rana temporaria

J. Michael Conlon, Ulrika Aronsson

Research output: Contribution to journal › Article › peer-review

63 Citations (Scopus)

Abstract

The skin of the European common frog, Rana temporaria, contains a very high concentration of bradykinin (BK) but the mode of biosynthesis of the peptide is unknown. In addition to BK, we have isolated from an extract of R. temporaria skin the metabolites [des-Arg⁹] BK and [hydroxyprolyl³] BK. Peptides were also isolated that represent partially processed intermediates in the biosynthetic pathway to BK and comprise BK extended from its N- terminus by -Gly-Val-Ile-Pro-Leu-Leu and three peptides comprising BK extended from its C terminus by -Ile-Ala, by -Ile-Ala-Pro-Ala-Ser-Thr-Leu, and by -Ile-Ala-Pro-Ala-Ser-Ile-Leu. The isolation of two C-terminally extended BK-containing peptides differing by a single amino substitution indicates that the biosynthetic precursor of frog skin BK may contain more than one copy of the BK sequence and/or more than one gene encoding BK is expressed. The structures of the biosynthetic intermediates suggest that BK in frog skin is generated by the action of cellular endoproteinase(s) cleaving at the site of monobasic residues rather than by the action of the kallikrein-kinin system.

Original language	English
Pages (from-to)	361-365
Number of pages	5
Journal	Peptides
Volume	18
Issue number	3
DOIs	https://doi.org/10.1016/S0196-9781(96)00339-7
Publication status	Published - 1997
Externally published	Yes

Keywords

Bradykinin
Frog skin
Posttranslational processing

ASJC Scopus subject areas

Biochemistry
Physiology
Endocrinology
Cellular and Molecular Neuroscience

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10.1016/S0196-9781(96)00339-7

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title = "Multiple bradykinin-related peptides from the skin of the frog, Rana temporaria",

abstract = "The skin of the European common frog, Rana temporaria, contains a very high concentration of bradykinin (BK) but the mode of biosynthesis of the peptide is unknown. In addition to BK, we have isolated from an extract of R. temporaria skin the metabolites [des-Arg9] BK and [hydroxyprolyl3] BK. Peptides were also isolated that represent partially processed intermediates in the biosynthetic pathway to BK and comprise BK extended from its N- terminus by -Gly-Val-Ile-Pro-Leu-Leu and three peptides comprising BK extended from its C terminus by -Ile-Ala, by -Ile-Ala-Pro-Ala-Ser-Thr-Leu, and by -Ile-Ala-Pro-Ala-Ser-Ile-Leu. The isolation of two C-terminally extended BK-containing peptides differing by a single amino substitution indicates that the biosynthetic precursor of frog skin BK may contain more than one copy of the BK sequence and/or more than one gene encoding BK is expressed. The structures of the biosynthetic intermediates suggest that BK in frog skin is generated by the action of cellular endoproteinase(s) cleaving at the site of monobasic residues rather than by the action of the kallikrein-kinin system.",

keywords = "Bradykinin, Frog skin, Posttranslational processing",

author = "Conlon, {J. Michael} and Ulrika Aronsson",

note = "Funding Information: This work was supported by the National Science Foundation (Grant IBN 9418819) and the Wenner-Gren Center Foundation.",

year = "1997",

doi = "10.1016/S0196-9781(96)00339-7",

language = "English",

volume = "18",

pages = "361--365",

journal = "Peptides",

issn = "0196-9781",

publisher = "Elsevier Inc.",

number = "3",

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T1 - Multiple bradykinin-related peptides from the skin of the frog, Rana temporaria

AU - Conlon, J. Michael

AU - Aronsson, Ulrika

N1 - Funding Information: This work was supported by the National Science Foundation (Grant IBN 9418819) and the Wenner-Gren Center Foundation.

PY - 1997

Y1 - 1997

N2 - The skin of the European common frog, Rana temporaria, contains a very high concentration of bradykinin (BK) but the mode of biosynthesis of the peptide is unknown. In addition to BK, we have isolated from an extract of R. temporaria skin the metabolites [des-Arg9] BK and [hydroxyprolyl3] BK. Peptides were also isolated that represent partially processed intermediates in the biosynthetic pathway to BK and comprise BK extended from its N- terminus by -Gly-Val-Ile-Pro-Leu-Leu and three peptides comprising BK extended from its C terminus by -Ile-Ala, by -Ile-Ala-Pro-Ala-Ser-Thr-Leu, and by -Ile-Ala-Pro-Ala-Ser-Ile-Leu. The isolation of two C-terminally extended BK-containing peptides differing by a single amino substitution indicates that the biosynthetic precursor of frog skin BK may contain more than one copy of the BK sequence and/or more than one gene encoding BK is expressed. The structures of the biosynthetic intermediates suggest that BK in frog skin is generated by the action of cellular endoproteinase(s) cleaving at the site of monobasic residues rather than by the action of the kallikrein-kinin system.

AB - The skin of the European common frog, Rana temporaria, contains a very high concentration of bradykinin (BK) but the mode of biosynthesis of the peptide is unknown. In addition to BK, we have isolated from an extract of R. temporaria skin the metabolites [des-Arg9] BK and [hydroxyprolyl3] BK. Peptides were also isolated that represent partially processed intermediates in the biosynthetic pathway to BK and comprise BK extended from its N- terminus by -Gly-Val-Ile-Pro-Leu-Leu and three peptides comprising BK extended from its C terminus by -Ile-Ala, by -Ile-Ala-Pro-Ala-Ser-Thr-Leu, and by -Ile-Ala-Pro-Ala-Ser-Ile-Leu. The isolation of two C-terminally extended BK-containing peptides differing by a single amino substitution indicates that the biosynthetic precursor of frog skin BK may contain more than one copy of the BK sequence and/or more than one gene encoding BK is expressed. The structures of the biosynthetic intermediates suggest that BK in frog skin is generated by the action of cellular endoproteinase(s) cleaving at the site of monobasic residues rather than by the action of the kallikrein-kinin system.

KW - Bradykinin

KW - Frog skin

KW - Posttranslational processing

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Multiple bradykinin-related peptides from the skin of the frog, Rana temporaria

Abstract

Keywords

ASJC Scopus subject areas

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