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VIP and PACAP

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  1. Biosynthesis of cardiac natriuretic peptides

    Research output: Contribution to journalJournal articleResearchpeer-review

  2. Cell-specific precursor processing

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  3. Posttranslational processing of progastrin

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  1. Circadian variations in plasma concentrations of cholecystokinin and gastrin in man

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  2. Evaluation of Serum Insulin-like Factor 3 Quantification by LC-MS/MS as a Biomarker of Leydig Cell Function

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  3. Spatiotemporal expression pattern of PERIOD 1 and PERIOD 2 in the mouse SCN is dependent on VIP receptor 2 signaling

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  4. Calcitonin-gene related peptide and disease activity in cluster headache

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Vasoactive intestinal polypeptide (VIP) is derived from a 170 amino acid precursor which in addition is processed to preproVIP 22-79, PHI, preproVIP 111-122 and preproVIP 156-170. All preproVIP-derived peptides have been shown in normal tissue and VIP-producing cell lines and elevated quantities occur in plasma and tumour tissues from patients with VIP-producing tumours. In some tissues the dibasic cleavage site after PHI is uncleaved resulting in a C-terminally extended form, PHV. PHI and VIP are present in a 1:1 molar ratio in large dense core vesicles and released in roughly equimolar amounts. Carboxyamidation of VIP and PHI is not critical and glycine-extended forms of both peptides have been demonstrated. Pituitary adenylate cyclase activating polypeptide (PACAP) is derived from a 170 amino acid long precursor, which gives rise to PACAP 38, PACAP 27 and PACAP related peptide (PRP). All peptides are present in tissue, the dominating form being PACAP 38. Prohormone convertase (PC) 1 and 2 seem to be involved in the processing of PACAP, except in the testes and ovary, where the PACAP precursor is substrate for PC4.
Original languageEnglish
Book seriesResults and Problems in Cell Differentiation
Volume50
Pages (from-to)221-34
Number of pages14
ISSN0080-1844
DOIs
Publication statusPublished - 1 Jan 2010

    Research areas

  • Amino Acids, Animals, Female, Gene Expression Regulation, Gene Expression Regulation, Neoplastic, Glycine, Humans, Male, Models, Biological, Peptide Hormones, Peptides, Pituitary Adenylate Cyclase-Activating Polypeptide, Protein Structure, Tertiary, Vasoactive Intestinal Peptide

ID: 32716626