Abstract:
:Uroguanylin, a member of the guanylin peptide family, is a novel peptide regulator for intestinal salt and water transport. A cDNA encoding a precursor for rat uroguanylin was cloned from a rat jejunum cDNA library and sequenced. The precursor was 106 amino acids long and included a 21 residue putative signal peptide at the N-terminus. Rat uroguanylin consisted of 15 amino acids similar to, but distinct from human uroguanylin; the C-terminal leucine residue was deleted and 3 residues were substituted compared to those in the human peptide. Synthetic rat uroguanylin-15 dose-dependently increased the cyclic GMP level in cultured T84 cells. RNA blot analysis showed that rat uroguanylin mRNA is expressed not only in the gastrointestinal tract but also in the lung, pancreas and kidney. Evidence for uroguanylin expression in extra-gastrointestinal tissues indicates the possible existence of a novel system for water and electrolyte homeostasis, and a more global effect of uroguanylin on epithelial cell function.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Miyazato M,Nakazato M,Matsukura S,Kangawa K,Matsuo Hdoi
10.1016/s0014-5793(96)01235-5subject
Has Abstractpub_date
1996-12-02 00:00:00pages
170-4issue
2-3eissn
0014-5793issn
1873-3468pii
S0014-5793(96)01235-5journal_volume
398pub_type
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