Research
Print page Print page
Switch language
The Capital Region of Denmark - a part of Copenhagen University Hospital
Published

Procholecystokinin expression and processing in cardiac myocytes

Research output: Contribution to journalReviewResearchpeer-review

  1. Serum proatrial natriuretic peptide concentrations during oral glucose-induced acute hyperinsulinemia in lean and obese men

    Research output: Contribution to journalJournal articleResearchpeer-review

  2. Cardiac procholecystokinin expression during haemodynamic changes in the mammalian heart

    Research output: Contribution to journalJournal articleResearchpeer-review

  1. Copeptin, a surrogate marker for arginine vasopressin secretion, is positively associated with glucagon

    Research output: Contribution to journalJournal articleResearchpeer-review

  2. Hypovolemia and reduced hemoglobin mass in patients with heart failure and preserved ejection fraction

    Research output: Contribution to journalJournal articleResearchpeer-review

  3. Transcriptome analysis in patients with temporal lobe epilepsy

    Research output: Contribution to journalJournal articleResearchpeer-review

  4. Cardiac dysfunction in cirrhosis: a 2-yr longitudinal follow-up study using advanced cardiac imaging

    Research output: Contribution to journalJournal articleResearchpeer-review

View graph of relations

The mammalian heart is by now an established endocrine organ whose myocytes in a regulated manner release atrial and ventricular natriuretic peptides (ANP and BNP). But like other hormone-producing cells in classic endocrine organs, the cardiac myocytes also express genes of additional peptide hormones. One such hormone gene is that of the well-known pleiotropic gut-brain peptide system, cholecystokinin (CCK), which is expressed at mRNA and protein levels in both atrial and ventricular cardiac myocytes. The posttranslational processing of proCCK in the myocytes, however, deviates substantially from that of other CCK-producing cells. Hence, the predominant cardiac proCCK product is devoid of the N-terminal 1-24 fragment, and besides O-sulfated at three C-terminal tyrosyl residues (Y76, Y90, and Y92). Moreover, carboxyamidated CCK peptides are present only in very low trace amounts (≤0.1%) in comparison with the truncated and triple-sulfated proCCK fragment. The present review first summarizes present knowledge about the wide-spread expression of the CCK system in mammals, and then discusses the possible function and biomarker role of the specific cardiac proCCK variant. The review concludes that the many unsettled questions about the specific cardiac expression cascade as well as the functional and diagnostic roles of cardiac CCK are worth pursuing.

Original languageEnglish
JournalPeptides
Volume111
Pages (from-to)71-76
Number of pages6
ISSN0196-9781
DOIs
Publication statusPublished - Jan 2019

ID: 56445370