Abstract
Guanylin, a 15-amino acid peptide homologue of bacterial heat-stable enterotoxins, is an endogenous activator of guanylate cyclase C (GC-C). We isolated two novel guanylin molecules from rat intestinal mucosa. They contained guanylin-15 at their C-termini and were identified as guanylin-94 and guanylin-16 by amino acid sequencing and mass spectrometry. Guanylin-94 and guanylin-16 in total account for 85% of guanylin molecules in both the small and large intestine, guanylin-15 being a minor component. Rat guanylin-94 and guanylin-16 did not increase cyclic GMP production in T84 cells. Identification of the post-translational processing products of guanylin should provide a better understanding of the biosynthesis of the peptide.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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1-Methyl-3-isobutylxanthine / pharmacology
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Amino Acid Sequence
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Animals
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Cell Line
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Chromatography, Gel
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Chromatography, High Pressure Liquid
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Colon
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Cyclic GMP / metabolism*
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Gastrointestinal Hormones*
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Ileum
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Intercellular Signaling Peptides and Proteins
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Intestinal Mucosa / chemistry
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Kinetics
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Male
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Mass Spectrometry
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Molecular Sequence Data
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Natriuretic Peptides
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Peptides / chemistry
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Peptides / isolation & purification
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Peptides / metabolism
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Peptides / pharmacology*
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Protein Processing, Post-Translational
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Rats
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Rats, Sprague-Dawley
Substances
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Gastrointestinal Hormones
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Intercellular Signaling Peptides and Proteins
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Natriuretic Peptides
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Peptides
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guanylin 16
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guanylin 94
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guanylin
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Cyclic GMP
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1-Methyl-3-isobutylxanthine