Dipeptidyl Peptidase IV (DPIV/CD26) Degradation of Glucagon

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Dipeptidyl peptidase IV (DPIV/CD26) degradation of glucagon. Characterization of glucagon degradation products and DPIV-resistant analogs.

Over the past decade, numerous studies have been targeted at defining structure-activity relationships of glucagon. Recently, we have found that glucagon(1-29) is hydrolyzed by dipeptidyl peptidase IV (DPIV) to produce glucagon(3-29) and glucagon(5-29); in human serum, [pyroglutamyl (pGlu)(3)]glucagon(3-29) is formed from glucagon(3-29), and this prevents further hydrolysis of glucagon by DPIV ...

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Metabolism of glucagon by dipeptidyl peptidase IV (CD26).

Glucagon is a 29-amino acid polypeptide released from pancreatic islet alpha-cells that acts to maintain euglycemia by stimulating hepatic glycogenolysis and gluconeogenesis. Despite its importance, there remains controversy about the mechanisms responsible for glucagon clearance in the body. In the current study, enzymatic metabolism of glucagon was assessed using sensitive mass spectrometric ...

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Tackling dipeptidyl peptidase IV in neurological disorders

Dipeptidyl peptidase IV (DPP-IV) is a serine protease best known for its role in inactivating glucagon-like peptide-1 (GLP-1), pituitary adenylate cyclase-activating polypeptide (PACAP) and glucose-dependent insulinotropic peptide (GIP), three stimulators of pancreatic insulin secretion with beneficial effects on glucose disposal. Owing to the relationship between DPP-IV and these peptides, inh...

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Dipeptidyl Peptidase IV and Incident Diabetes

OBJECTIVE Dipeptidyl peptidase IV (DPP-IV) is not only important in beta-cell function but also has proinflammatory actions. We aimed to investigate whether it could act as a link between low-grade chronic inflammation and diabetes. RESEARCH DESIGN AND METHODS Using a case-cohort design, we followed 546 middle-aged individuals who developed diabetes and 538 who did not over approximately 9 ye...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 2000

ISSN: 0021-9258

DOI: 10.1074/jbc.275.6.3827