Glucagon-like peptide-1-(7-36)amide is transformed to glucagon-like peptide-1-(9-36)amide by dipeptidyl peptidase IV in the capillaries supplying the L cells of the porcine intestine

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

Glucagon-like peptide-1-(7-36)amide is transformed to glucagon-like peptide-1-(9-36)amide by dipeptidyl peptidase IV in the capillaries supplying the L cells of the porcine intestine. / Hansen, L; Deacon, C F; Orskov, C; Holst, J J.

In: Molecular Endocrinology, Vol. 140, No. 11, 11.1999, p. 5356-63.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Hansen, L, Deacon, CF, Orskov, C & Holst, JJ 1999, 'Glucagon-like peptide-1-(7-36)amide is transformed to glucagon-like peptide-1-(9-36)amide by dipeptidyl peptidase IV in the capillaries supplying the L cells of the porcine intestine', Molecular Endocrinology, vol. 140, no. 11, pp. 5356-63. https://doi.org/10.1210/endo.140.11.7143

APA

Hansen, L., Deacon, C. F., Orskov, C., & Holst, J. J. (1999). Glucagon-like peptide-1-(7-36)amide is transformed to glucagon-like peptide-1-(9-36)amide by dipeptidyl peptidase IV in the capillaries supplying the L cells of the porcine intestine. Molecular Endocrinology, 140(11), 5356-63. https://doi.org/10.1210/endo.140.11.7143

Vancouver

Hansen L, Deacon CF, Orskov C, Holst JJ. Glucagon-like peptide-1-(7-36)amide is transformed to glucagon-like peptide-1-(9-36)amide by dipeptidyl peptidase IV in the capillaries supplying the L cells of the porcine intestine. Molecular Endocrinology. 1999 Nov;140(11):5356-63. https://doi.org/10.1210/endo.140.11.7143

Author

Hansen, L ; Deacon, C F ; Orskov, C ; Holst, J J. / Glucagon-like peptide-1-(7-36)amide is transformed to glucagon-like peptide-1-(9-36)amide by dipeptidyl peptidase IV in the capillaries supplying the L cells of the porcine intestine. In: Molecular Endocrinology. 1999 ; Vol. 140, No. 11. pp. 5356-63.

Bibtex

@article{6d2acd90cd1548ef8ff7ea66690ee26c,
title = "Glucagon-like peptide-1-(7-36)amide is transformed to glucagon-like peptide-1-(9-36)amide by dipeptidyl peptidase IV in the capillaries supplying the L cells of the porcine intestine",
abstract = "The insulinotropic hormone glucagon-like peptide-1 (GLP-1) is stored in the intestinal L cell in an active form, GLP-1-(7-36)amide, but more than half of the endogenous peptide circulates in an inactive, N-terminally truncated form, GLP-1-(9-36)amide. This study examined the GLP-1 newly secreted from the porcine ileum, in vitro (isolated perfused preparation) and in vivo (anesthetized pig), to determine where this conversion occurs. Although the GLP-1 extractable from the porcine ileum is predominantly the intact peptide (94.6+/-1.7{\%}), a large proportion of the GLP-1 that is secreted has already been degraded to the truncated form both in vitro (53.8+/-0.9{\%} intact) and in vivo (32.9+/-10.8{\%} intact). In the presence of a specific dipeptidyl peptidase IV (DPP IV) inhibitor (valine-pyrrolidide), the proportion of intact GLP-1 released from the perfused ileum was increased under both basal (99{\%} intact; P < 0.05) and stimulated (86-101{\%} intact; P < 0.05) conditions. Immunohistochemical and histochemical studies revealed specific DPP IV staining in the brush border epithelium as well as in the capillary endothelium. Double staining showed juxtapositioning of DPP IV-positive capillaries and GLP-1-containing L cells. From these results, we suggest that GLP-1 is degraded as it enters the DPP IV containing blood vessels draining the intestinal mucosa.",
keywords = "Animals, Capillaries/enzymology, Chromatography, High Pressure Liquid, Dipeptidyl Peptidase 4/metabolism, Endothelium, Vascular/enzymology, Epithelium/enzymology, Glucagon, Glucagon-Like Peptide 1, Glucagon-Like Peptides, Histocytochemistry, Immunohistochemistry, Intestinal Mucosa/blood supply, Microvilli/enzymology, Peptide Fragments/metabolism, Peptides/secretion, Swine",
author = "L Hansen and Deacon, {C F} and C Orskov and Holst, {J J}",
year = "1999",
month = "11",
doi = "10.1210/endo.140.11.7143",
language = "English",
volume = "140",
pages = "5356--63",
journal = "Molecular Endocrinology",
issn = "0888-8809",
publisher = "Oxford University Press",
number = "11",

}

RIS

TY - JOUR

T1 - Glucagon-like peptide-1-(7-36)amide is transformed to glucagon-like peptide-1-(9-36)amide by dipeptidyl peptidase IV in the capillaries supplying the L cells of the porcine intestine

AU - Hansen, L

AU - Deacon, C F

AU - Orskov, C

AU - Holst, J J

PY - 1999/11

Y1 - 1999/11

N2 - The insulinotropic hormone glucagon-like peptide-1 (GLP-1) is stored in the intestinal L cell in an active form, GLP-1-(7-36)amide, but more than half of the endogenous peptide circulates in an inactive, N-terminally truncated form, GLP-1-(9-36)amide. This study examined the GLP-1 newly secreted from the porcine ileum, in vitro (isolated perfused preparation) and in vivo (anesthetized pig), to determine where this conversion occurs. Although the GLP-1 extractable from the porcine ileum is predominantly the intact peptide (94.6+/-1.7%), a large proportion of the GLP-1 that is secreted has already been degraded to the truncated form both in vitro (53.8+/-0.9% intact) and in vivo (32.9+/-10.8% intact). In the presence of a specific dipeptidyl peptidase IV (DPP IV) inhibitor (valine-pyrrolidide), the proportion of intact GLP-1 released from the perfused ileum was increased under both basal (99% intact; P < 0.05) and stimulated (86-101% intact; P < 0.05) conditions. Immunohistochemical and histochemical studies revealed specific DPP IV staining in the brush border epithelium as well as in the capillary endothelium. Double staining showed juxtapositioning of DPP IV-positive capillaries and GLP-1-containing L cells. From these results, we suggest that GLP-1 is degraded as it enters the DPP IV containing blood vessels draining the intestinal mucosa.

AB - The insulinotropic hormone glucagon-like peptide-1 (GLP-1) is stored in the intestinal L cell in an active form, GLP-1-(7-36)amide, but more than half of the endogenous peptide circulates in an inactive, N-terminally truncated form, GLP-1-(9-36)amide. This study examined the GLP-1 newly secreted from the porcine ileum, in vitro (isolated perfused preparation) and in vivo (anesthetized pig), to determine where this conversion occurs. Although the GLP-1 extractable from the porcine ileum is predominantly the intact peptide (94.6+/-1.7%), a large proportion of the GLP-1 that is secreted has already been degraded to the truncated form both in vitro (53.8+/-0.9% intact) and in vivo (32.9+/-10.8% intact). In the presence of a specific dipeptidyl peptidase IV (DPP IV) inhibitor (valine-pyrrolidide), the proportion of intact GLP-1 released from the perfused ileum was increased under both basal (99% intact; P < 0.05) and stimulated (86-101% intact; P < 0.05) conditions. Immunohistochemical and histochemical studies revealed specific DPP IV staining in the brush border epithelium as well as in the capillary endothelium. Double staining showed juxtapositioning of DPP IV-positive capillaries and GLP-1-containing L cells. From these results, we suggest that GLP-1 is degraded as it enters the DPP IV containing blood vessels draining the intestinal mucosa.

KW - Animals

KW - Capillaries/enzymology

KW - Chromatography, High Pressure Liquid

KW - Dipeptidyl Peptidase 4/metabolism

KW - Endothelium, Vascular/enzymology

KW - Epithelium/enzymology

KW - Glucagon

KW - Glucagon-Like Peptide 1

KW - Glucagon-Like Peptides

KW - Histocytochemistry

KW - Immunohistochemistry

KW - Intestinal Mucosa/blood supply

KW - Microvilli/enzymology

KW - Peptide Fragments/metabolism

KW - Peptides/secretion

KW - Swine

U2 - 10.1210/endo.140.11.7143

DO - 10.1210/endo.140.11.7143

M3 - Journal article

C2 - 10537167

VL - 140

SP - 5356

EP - 5363

JO - Molecular Endocrinology

JF - Molecular Endocrinology

SN - 0888-8809

IS - 11

ER -

ID: 194815184