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

VIP and PACAP

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

APA

CBE

MLA

Vancouver

Author

Bibtex

@article{5d8783355d46417fb921758052e862c4,
title = "VIP and PACAP",
abstract = "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.",
keywords = "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",
author = "Jan Fahrenkrug",
year = "2010",
month = "1",
day = "1",
doi = "10.1007/400_2009_24",
language = "English",
volume = "50",
pages = "221--34",
journal = "Results and Problems in Cell Differentiation",
issn = "0080-1844",
publisher = "Springer New York LLC",

}

RIS

TY - JOUR

T1 - VIP and PACAP

AU - Fahrenkrug, Jan

PY - 2010/1/1

Y1 - 2010/1/1

N2 - 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.

AB - 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.

KW - Amino Acids

KW - Animals

KW - Female

KW - Gene Expression Regulation

KW - Gene Expression Regulation, Neoplastic

KW - Glycine

KW - Humans

KW - Male

KW - Models, Biological

KW - Peptide Hormones

KW - Peptides

KW - Pituitary Adenylate Cyclase-Activating Polypeptide

KW - Protein Structure, Tertiary

KW - Vasoactive Intestinal Peptide

U2 - 10.1007/400_2009_24

DO - 10.1007/400_2009_24

M3 - Journal article

VL - 50

SP - 221

EP - 234

JO - Results and Problems in Cell Differentiation

JF - Results and Problems in Cell Differentiation

SN - 0080-1844

ER -

ID: 32716626