Abstract
Caerulein was first purified and identified in the Australian frog Hyla caerulea in 1967 and has been detected in several frog species. Caerulein is a decapeptide that contains the C-terminal four amino-acid sequence (Trp-Met-Asp-Phe-NH2) that is conserved in vertebrate gastrin and CCK. In addition, caerulein possesses a sulfated tyrosine at the seventh residue from the C-terminus. Caerulein is synthesized in the skin of frogs. Caerulein is processed from the precursor, which also contains an antimicrobial peptide called caerulein precursor fragment (CPF). Caerulein can activate gastrin and CCK signaling through CCK1R and CCK2R, suggesting that caerulein and CRF may function as a defensive peptide against microbes and predators.
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