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Unsulfated cholecystokinin: An overlooked hormone?

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@article{2305ca6f0d1a47069946e4707c4e8c6a,
title = "Unsulfated cholecystokinin: An overlooked hormone?",
abstract = "Tyrosyl O-sulfation is a common posttranslational derivatization of proteins that may also modify regulatory peptides. Among these are members of the cholecystokinin (CCK)/gastrin family. While sulfation of gastrin peptides is without effect on the bioactivity, O-sulfation is crucial for the cholecystokinetic activity (i.e. gallbladder emptying) of CCK peptides. Accordingly, the purification of CCK as a sulfated peptide was originally monitored by its gallbladder emptying effect. Since then, the dogma has prevailed that CCK peptides are always sulfated. The dogma is correct in a semantic context since the gallbladder expresses only the CCK-A receptor that requires sulfation of the ligand. CCK peptides, however, are also ligands for the CCK-B receptors that do not require ligand sulfation. Consequently, unsulfated CCK peptides may act via CCK-B receptors. Since in vivo occurrence of unsulfated products of proCCK with an intact α-amidated C-terminal tetrapeptide sequence (-Trp-Met-Asp-PheNH(2)) has been reported, it is likely that unsulfated CCK peptides constitute a separate hormone system that acts via CCK-B receptors. This review discusses the occurrence, molecular forms, and possible physiological as well as pathophysiological significance of unsulfated CCK peptides.",
keywords = "Amino Acid Sequence, Animals, Cholecystokinin, Gene Expression, Humans, Molecular Sequence Data, Organ Specificity, Protein Isoforms, Protein Processing, Post-Translational, Receptors, Cholecystokinin, Signal Transduction, Tyrosine",
author = "Rehfeld, {Jens F} and Mikkel Agersnap",
note = "Copyright {\circledC} 2011 Elsevier B.V. All rights reserved.",
year = "2012",
doi = "10.1016/j.regpep.2011.09.009",
language = "English",
volume = "173",
pages = "1--5",
journal = "Regulatory Peptides",
issn = "0167-0115",
publisher = "Elsevier BV",
number = "1-3",

}

RIS

TY - JOUR

T1 - Unsulfated cholecystokinin

T2 - An overlooked hormone?

AU - Rehfeld, Jens F

AU - Agersnap, Mikkel

N1 - Copyright © 2011 Elsevier B.V. All rights reserved.

PY - 2012

Y1 - 2012

N2 - Tyrosyl O-sulfation is a common posttranslational derivatization of proteins that may also modify regulatory peptides. Among these are members of the cholecystokinin (CCK)/gastrin family. While sulfation of gastrin peptides is without effect on the bioactivity, O-sulfation is crucial for the cholecystokinetic activity (i.e. gallbladder emptying) of CCK peptides. Accordingly, the purification of CCK as a sulfated peptide was originally monitored by its gallbladder emptying effect. Since then, the dogma has prevailed that CCK peptides are always sulfated. The dogma is correct in a semantic context since the gallbladder expresses only the CCK-A receptor that requires sulfation of the ligand. CCK peptides, however, are also ligands for the CCK-B receptors that do not require ligand sulfation. Consequently, unsulfated CCK peptides may act via CCK-B receptors. Since in vivo occurrence of unsulfated products of proCCK with an intact α-amidated C-terminal tetrapeptide sequence (-Trp-Met-Asp-PheNH(2)) has been reported, it is likely that unsulfated CCK peptides constitute a separate hormone system that acts via CCK-B receptors. This review discusses the occurrence, molecular forms, and possible physiological as well as pathophysiological significance of unsulfated CCK peptides.

AB - Tyrosyl O-sulfation is a common posttranslational derivatization of proteins that may also modify regulatory peptides. Among these are members of the cholecystokinin (CCK)/gastrin family. While sulfation of gastrin peptides is without effect on the bioactivity, O-sulfation is crucial for the cholecystokinetic activity (i.e. gallbladder emptying) of CCK peptides. Accordingly, the purification of CCK as a sulfated peptide was originally monitored by its gallbladder emptying effect. Since then, the dogma has prevailed that CCK peptides are always sulfated. The dogma is correct in a semantic context since the gallbladder expresses only the CCK-A receptor that requires sulfation of the ligand. CCK peptides, however, are also ligands for the CCK-B receptors that do not require ligand sulfation. Consequently, unsulfated CCK peptides may act via CCK-B receptors. Since in vivo occurrence of unsulfated products of proCCK with an intact α-amidated C-terminal tetrapeptide sequence (-Trp-Met-Asp-PheNH(2)) has been reported, it is likely that unsulfated CCK peptides constitute a separate hormone system that acts via CCK-B receptors. This review discusses the occurrence, molecular forms, and possible physiological as well as pathophysiological significance of unsulfated CCK peptides.

KW - Amino Acid Sequence

KW - Animals

KW - Cholecystokinin

KW - Gene Expression

KW - Humans

KW - Molecular Sequence Data

KW - Organ Specificity

KW - Protein Isoforms

KW - Protein Processing, Post-Translational

KW - Receptors, Cholecystokinin

KW - Signal Transduction

KW - Tyrosine

U2 - 10.1016/j.regpep.2011.09.009

DO - 10.1016/j.regpep.2011.09.009

M3 - Journal article

VL - 173

SP - 1

EP - 5

JO - Regulatory Peptides

JF - Regulatory Peptides

SN - 0167-0115

IS - 1-3

ER -

ID: 36789524