Establishment of novel specific assay for short‐form glucose‐dependent insulinotropic polypeptide and evaluation of its secretion in nondiabetic subjects

Autor: Tsuyoshi Yanagimachi, Nobuhiro Maruyama, Hidemitsu Sakagami, Yukihiro Fujita, Ryoichi Bessho, Jun Honjo, Hiroki Yokoyama, Yasutaka Takeda, Masakazu Haneda
Jazyk: angličtina
Rok vydání: 2020
Předmět:
Adult
Blood Glucose
Male
medicine.medical_specialty
endocrine system
Physiology
Alpha (ethology)
Enzyme-Linked Immunosorbent Assay
Gastric Inhibitory Polypeptide
030204 cardiovascular system & hematology
Carbohydrate metabolism
oral glucose tolerance test
cookie meal test
Glucagon
lcsh:Physiology
03 medical and health sciences
0302 clinical medicine
In vivo
Physiology (medical)
Internal medicine
medicine
Metabolism and Regulation
Animals
Humans
Insulin
Secretion
Rats
Wistar
Original Research
Aged
geography
geography.geographical_feature_category
biology
lcsh:QP1-981
Chemistry
DPP‐4 inhibitor
Glucose Tolerance Test
Middle Aged
Islet
In vitro
Peptide Fragments
GIP (1–30)
Endocrinology
biology.protein
ELISA
Female
Endocrine and Metabolic Conditons
Disorders and Treatments
Antibody
030217 neurology & neurosurgery
hormones
hormone substitutes
and hormone antagonists
Zdroj: Physiological Reports
Physiological Reports, Vol 8, Iss 11, Pp n/a-n/a (2020)
ISSN: 2051-817X
Popis: The short‐form glucose‐dependent insulinotropic polypeptide (GIP) (1–30) is released from islet alpha cells and promotes insulin secretion in a paracrine manner in vitro. However, it is not well elucidated how GIP (1–30) is involved in glucose metabolism in vivo, since a specific assay system for GIP (1–30) has not yet been established. We first developed a sandwich enzyme‐linked immunosorbent assay (ELISA) specific for GIP (1–30) by combining a novel antibody specific to the GIP (1–30) C terminus with the common antibody against GIP N terminus. Then, we explored cross‐reactivities with incretins and glucagon‐related peptides in this ELISA. GIP (1–30) amide, but not GIP (1–42), GLP‐1, or glucagon increased absorbance in a dose‐dependent manner. We next measured plasma GIP (1–30) concentrations in nondiabetic participants (ND) during a 75‐g oral glucose tolerance test or cookie meal test (carbohydrates 75 g, lipids 28.5 g, proteins 8.5 g). Both glucose and cookie load increased GIP (1–30) concentrations in ND, but the increases were much lower than those of GIP (1–42). Furthermore, the DPP‐4 inhibitor significantly increased GIP (1–30) concentrations similarly to GIP (1–42) in ND. In conclusion, we for the first time developed an ELISA specific for GIP (1–30) and revealed its secretion in ND.
For the first time, we established a novel ELISA specific for GIP (1–30). GIP (1–30) secretion is promoted by oral glucose and mix meal load in nondiabetics. DPP‐4 inhibitors increased peripheral blood GIP (1–30) levels.
Databáze: OpenAIRE
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