Plasma and intestinal concentrations of GIP and GLP-1 (7-36) amide during suckling and after weaning in pigs. 1995

J M Knapper, and L M Morgan, and J M Fletcher, and V Marks
School of Biological Sciences, University of Surrey, Guildford, United Kingdom.

Plasma concentrations of glucose dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1(7-36)amide (GLP-1[7-36]amide) were measured after milk ingestion in 15-18 day old piglets and after weaning diet ingestion in 33 day old piglets weaned at 21 days. Intestinal concentrations of these two hormones were also measured in unsuckled piglets of less than 24 h of age, and piglets whose ages corresponded with those used for plasma measurements. Suckling piglets showed a moderate glycaemic and insulinaemic response to milk ingestion. Plasma GIP and GLP-1(7-36)amide levels were significantly elevated at 1 and 3-h post-prandially. Weaned piglets showed a much more marked glucose and insulin response to meal ingestion. Plasma GIP and GLP-1(7-36)amide levels were again significantly elevated at 1 and 3 h in these animals. The mean plasma GIP response was greater in the weaned animals compared with the suckling animals at the time points investigated. The plasma GLP-1(7-36)amide response in contrast was significantly greater at 1 h in the suckling animals. In comparison, GIP concentrations in acid ethanol extracts of the small intestine were significantly higher during suckling and GLP-1(7-36)amide concentrations significantly higher after weaning. The circulating levels of both hormones seen during suckling and after weaning were far higher than those previously reported in humans. We conclude that both milk ingestion and the weaning diet are capable of stimulating GIP and GLP-1(7-36)amide in piglets and suggest that the levels of both hormones seen in this study may be important in adipose tissue metabolism at this time.

UI MeSH Term Description Entries
D007328 Insulin A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1). Iletin,Insulin A Chain,Insulin B Chain,Insulin, Regular,Novolin,Sodium Insulin,Soluble Insulin,Chain, Insulin B,Insulin, Sodium,Insulin, Soluble,Regular Insulin
D007413 Intestinal Mucosa Lining of the INTESTINES, consisting of an inner EPITHELIUM, a middle LAMINA PROPRIA, and an outer MUSCULARIS MUCOSAE. In the SMALL INTESTINE, the mucosa is characterized by a series of folds and abundance of absorptive cells (ENTEROCYTES) with MICROVILLI. Intestinal Epithelium,Intestinal Glands,Epithelium, Intestinal,Gland, Intestinal,Glands, Intestinal,Intestinal Gland,Mucosa, Intestinal
D008892 Milk The off-white liquid secreted by the mammary glands of humans and other mammals. It contains proteins, sugar, lipids, vitamins, and minerals. Cow Milk,Cow's Milk,Milk, Cow,Milk, Cow's
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D001786 Blood Glucose Glucose in blood. Blood Sugar,Glucose, Blood,Sugar, Blood
D004763 Glucagon-Like Peptides Peptides derived from proglucagon which is also the precursor of pancreatic GLUCAGON. Despite expression of proglucagon in multiple tissues, the major production site of glucagon-like peptides (GLPs) is the INTESTINAL L CELLS. GLPs include glucagon-like peptide 1, glucagon-like peptide 2, and the various truncated forms. Enteroglucagon,Enteroglucagons,Glucagon-Like Peptide,Glucagon-Like Polypeptide,Gut Glucagon,Glucagon-Like Polypeptides,Glucagon Like Peptide,Glucagon Like Peptides,Glucagon Like Polypeptide,Glucagon Like Polypeptides,Glucagon, Gut,Peptide, Glucagon-Like,Polypeptide, Glucagon-Like
D005502 Food Substances taken in by the body to provide nourishment. Foods
D005749 Gastric Inhibitory Polypeptide A gastrointestinal peptide hormone of about 43-amino acids. It is found to be a potent stimulator of INSULIN secretion and a relatively poor inhibitor of GASTRIC ACID secretion. Glucose-Dependent Insulinotropic Peptide,Gastric-Inhibitory Polypeptide,Glucose Dependent Insulinotropic Peptide,Glucose-Dependent Insulin-Releasing Peptide,Glucose Dependent Insulin Releasing Peptide,Inhibitory Polypeptide, Gastric,Insulin-Releasing Peptide, Glucose-Dependent,Insulinotropic Peptide, Glucose-Dependent,Peptide, Glucose-Dependent Insulin-Releasing,Peptide, Glucose-Dependent Insulinotropic,Polypeptide, Gastric Inhibitory,Polypeptide, Gastric-Inhibitory
D005934 Glucagon A 29-amino acid pancreatic peptide derived from proglucagon which is also the precursor of intestinal GLUCAGON-LIKE PEPTIDES. Glucagon is secreted by PANCREATIC ALPHA CELLS and plays an important role in regulation of BLOOD GLUCOSE concentration, ketone metabolism, and several other biochemical and physiological processes. (From Gilman et al., Goodman and Gilman's The Pharmacological Basis of Therapeutics, 9th ed, p1511) Glucagon (1-29),Glukagon,HG-Factor,Hyperglycemic-Glycogenolytic Factor,Proglucagon (33-61),HG Factor,Hyperglycemic Glycogenolytic Factor
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

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