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PubMed2005

The discovery of glucagon-like peptide 1.

The discovery of glucagon-like peptide 1 (GLP-1) began more than two decades ago with the observations that anglerfish islet proglucagon messenger RNAs (mRNAs) contained coding sequences for two glucagon-related peptides arranged in tandem. Subsequent analyses revealed that mammalian proglucagon mRNAs encoded a precursor containing the sequence of pancreatic glucagon, intestinal glicentin and two glucagon-related peptides termed GLP-1 and GLP-2. Multidisciplinary approaches were then required to define the structure of biologically active GLP-1 7-36 amide and its role as an incretin, satiety hormone and, most recently, a neuroprotective peptide. This historial perspective outlines the use of traditional recombinant DNA approaches to derive the GLP-1 sequence and highlights the challenges and combination of clinical and basic science approaches required to define the physiology and pathophysiology of bioactive peptides discovered through genomics.

Animals↗
PubMed1987

Neoplastic endocrine cells in carcinomas of the small intestine: histochemical and immunohistochemical studies of 24 tumors.

Endocrine cells in 24 primary carcinomas and in the nonneoplastic mucosa of the small intestine were investigated histochemically and immunohistochemically with antisera against serotonin and 10 kinds of peptide hormones. Argyrophil-positive endocrine cells were found in four of eight duodenal, all of eight jejunal, and six of eight ileal carcinomas. The density of the positive cells was higher in the ileal tumors than in the duodenal and jejunal ones. Immunoreactive endocrine cells were detected in three duodenal, six jejunal, and five ileal carcinomas. Immunoreactive serotonin cells were present most frequently and most densely without respect to the site of origin of the carcinomas. In general, the population of endocrine cells among the tumor cells was higher in the ileal carcinomas than in the duodenal and jejunal ones. The ileal carcinomas frequently and densely demonstrated somatostatin, peptide YY, neurotensin, glucagon, and glicentin cells in addition to serotonin cells. The kinds of endocrine cells and the relative frequency of each kind of endocrine cell in carcinomas of the small intestine were similar to those in the nonneoplastic mucosa from which the carcinomas originated. This is the first systematic immunohistochemical study on endocrine cells in carcinoma of the small intestine.

Adult↗
PubMed1997

Distribution of glucagon-like peptide-1 and other preproglucagon-derived peptides in the rat hypothalamus and brainstem.

Central administration of the preproglucagon-derived peptide glucagon-like peptide-1 significantly inhibits ingestion of food and water, and glucagon-like peptide-1 binding sites are present in a multitude of central areas involved in the regulation of ingestional behaviour. To evaluate further the neuroanatomical organization of central glucagon-like peptide-1 containing neuronal circuits with potential implications on ingestional behaviour, we carried out a series of experiments in the rat demonstrating the topographical sites of synthesis and processing of the preproglucagon precursor followed by a chromatographic analysis of the processed fragments. In situ hybridization histochemistry revealed that preproglucagon encoding messenger RNA was expressed in a single population of neurons in the caudal portion of the nucleus of the solitary tract. Gel chromatographic analysis of hypothalamic and brainstem tissue extracts revealed that the preproglucagon precursor is processed in a fashion similar to that seen in the small intestine, preferentially giving rise to glicentin, glucagon-like peptide-1 and glucagon-like peptide-2. This single brain site of glucagon-like peptide-1 synthesis was subsequently confirmed by immunohistochemical demonstration of glucagon-like peptide-1-immunoreactive perikarya in the central and caudal parts of the nucleus of the solitary tract. Numerous sites containing glucagon-like peptide-1 immunoreactive fibres were, however, discovered in the forebrain including hypothalamic, thalamic and cortical areas. The densest innervation by glucagon-like peptide-1 immunoreactive nerve fibres was seen in the hypothalamic dorsomedial and paraventricular nuclei, but numerous glucagon-like peptide-1 immunoreactive fibres were also seen throughout the periventricular strata of the third ventricle. Dual-labelling immunohistochemistry for tyrosine hydroxylase and glucagon-like peptide-1 gave no evidence for co-localization of catecholamines and glucagon-like peptide-1 in neurons of the lower brainstem. To identify neurons of the nucleus of the solitary tract that project to the hypothalamic paraventricular nucleus, the retrograde tracer FluoroGold was injected into this hypothalamic target and dual immunocytochemical identification of glucagon-like peptide-1 and tyrosine hydroxylase-positive neurons was performed on brainstem sections containing retrogradely labelled perikarya. From this experiment it was seen that many of the retrogradely labelled neurons in the central portion of the nucleus of the solitary tract are catecholaminergic, while none is glucagon-like peptide-1 immunoreactive. In contrast, most of the retrogradely labelled neurons of the caudal portion of the nucleus of the solitary tract contain glucagon-like peptide-1. These observations further substantiate that glucagon-like peptide-1 neurons of the solitary tract constitute a distinct non-catecholaminergic cell group which projects to many targets, one of which is the hypothalamic paraventricular nucleus.

Animals↗
PubMed1994

Purification and sequence of rat oxyntomodulin.

Structural information about rat enteroglucagon, intestinal peptides containing the pancreatic glucagon sequence, has been based previously on cDNA, immunologic, and chromatographic data. Our interests in testing the physiological actions of synthetic enteroglucagon peptides in rats required that we identify precisely the forms present in vivo. From knowledge of the proglucagon gene sequence, we synthesized an enteroglucagon C-terminal octapeptide common to both proposed enteroglucagon forms, glicentin and oxyntomodulin, but sharing no sequence overlap with glucagon. We then developed a radioimmunoassay using antibodies raised against the octapeptide that was specific for enteroglucagon peptides without cross-reacting with glucagon. Rat intestine was extracted, and one presumptive enteroglucagon form was purified by following the enteroglucagon C-terminal octapeptide-like immunoreactivity through several HPLC purification steps. Structural characterization of the material by amino acid composition, microsequence, and mass spectral analyses identified the peptide as rat oxyntomodulin. The 37-residue peptide consists of pancreatic glucagon plus the C-terminal extension, Lys-Arg-Asn-Arg-Asn-Asn-Ile-Ala. This now permits synthesis of an unambiguous duplicate of endogenous rat oxyntomodulin for physiological studies.

Amino Acid Sequence↗
PubMed1995

Processing of mouse proglucagon by recombinant prohormone convertase 1 and immunopurified prohormone convertase 2 in vitro.

The mouse tumor cell line alpha TC1-6 was used as a model system to examine the post-translational processing of proglucagon. Determination of the mouse preproglucagon cDNA sequence and comparison with the published sequences of rat and human preproglucagons revealed nucleic acid homologies of 89.1 and 84%, respectively, and amino acid homologies of 94 and 89.4%, respectively. Immunohistochemical analyses with antibodies directed against PC2 and glucagon colocalized both the enzyme and substrate within the same secretory granules. PC1 was also immunolocalized in secretory granules. Cells were metabolically labeled with [3H]tryptophan, and extracts were analyzed by reverse-phase high pressure liquid chromatography. Radioactive peptides with retention times identical to those of synthetic peptide standards were recovered and subjected to peptide mapping to verify their identities. To determine the potential role of PC1 and PC2 in proglucagon processing, 3H-labeled proglucagon was incubated in vitro with recombinant PC1 and/or immunopurified PC2. Both enzymes cleaved proglucagon to yield the major proglucagon fragment, glicentin, and oxyntomodulin, whereas only PC1 released glucagon-like peptide-I from the major proglucagon fragment. Neither PC1 nor PC2 processed glucagon from proglucagon in vitro. These results suggest a potential role for PC1 and/or PC2 in cleaving several of the normal products, excluding glucagon, from the mouse proglucagon precursor.

Amino Acid Sequence↗
PubMed1998

Regulatory roles of the P domain of the subtilisin-like prohormone convertases.

A unique feature of the eukaryotic subtilisin-like proprotein convertases (SPCs) is the presence of an additional highly conserved sequence of approximately 150 residues (P domain) located immediately downstream of the catalytic domain. To study the function of this region, which is required for the production of enzymatically active convertases, we have expressed and characterized various P domain-related mutants and chimeras in HEK293 cells and alpha-TC1-6 cells. In a series of C-terminal truncations of PC3 (also known as PC1 or SPC3), PC3-Thr594 was identified as the shortest active form, thereby defining the functional C-terminal boundary of the P domain. Substitutions at Thr594 and nearby sites indicated that residues 592-594 are crucial for activity. Chimeric SPC proteins with interchanged P domains demonstrated dramatic changes in several properties. Compared with truncated wild-type PC3 (PC3-Asp616), both PC3/PC2Pd and PC3/FurPd had elevated activity on several synthetic substrates as well as reduced calcium ion dependence, whereas Fur/PC2Pd was only slightly decreased in activity as compared with truncated furin (Fur-Glu583). Of the three active SPC chimeras tested, all had more alkaline pH optima. When PC3/PC2Pd was expressed in alpha-TC1-6 cells, it accelerated the processing of proglucagon into glicentin and major proglucagon fragment and cleaved major proglucagon fragment to release GLP-1 and tGLP-1, similar to wild-type PC3. Thus, P domain exchanges generated fully active chimeric proteases in several instances but not in all (e.g. PC2/PC3Pd was inactive). The observed property changes indicate a role for the P domain in regulating the stability, calcium dependence, and pH dependence of the convertases.

Animals↗
PubMed2004

Altered proglucagon processing in an alpha-cell line derived from prohormone convertase 2 null mouse islets.

The endoproteolytic processing of proproteins in the secretory pathway depends on the expression of selected members of a family of subtilisin-like endoproteases known as the prohormone convertases (PCs). The main PC family members expressed in mammalian neuroendocrine cells are PC2 and PC1/3. The differential processing of proglucagon in pancreatic alpha-cells and intestinal L cells leads to production of distinct hormonal products with opposing physiological effects from the same precursor. Here we describe the establishment and characterization of a novel alpha-cell line (alphaTC-DeltaPC2) derived from PC2 homozygous null animals. The alphaTC-DeltaPC2 cells are shown to be similar to the well characterized alphaTC1-6 cell line in both morphology and overall gene expression. However, the absence of PC2 activity in alphaTC-DeltaPC2 leads to a complete block in the production of mature glucagon. Surprisingly, alphaTC-DeltaPC2 cells are able to efficiently cleave the interdomain site in proglucagon (KR 70-71). Further analysis reveals that alphaTC-DeltaPC2 cells, unlike alphaTC1-6 cells, express low levels of PC1/3 that lead to the generation of glicentin as well as low amounts of oxyntomodulin, GLP-1, truncated GLP-1, and N-terminally extended GLP-2. We conclude that alphaTC-DeltaPC2 cells provide additional evidence for PC2 as the major convertase in alpha-cells leading to mature glucagon production and provide a robust model for further analysis of the mechanisms of proprotein processing by the prohormone convertases.

Animals↗
PubMed2000

Deficiency of the intestinal growth factor, glucagon-like peptide 2, in the colon of SCID mice with inflammatory bowel disease induced by transplantation of CD4+ T cells.

BACKGROUND: Glucagon-like peptide 2 (GLP-2) is produced in endocrine L-cells of the intestinal mucosa. Recently, GLP-2 was found to stimulate intestinal mucosal growth. Our objective was to study the content of GLP-2 in the large intestine in a murine model of T-cell-induced inflammatory bowel disease. METHODS: Inflammation was induced by adoptive transfer of CD4+ blast T cells from BALB/c mice to SCID mice. The amount of GLP-2 (1-33) was measured with a specific, NH2-terminally directed radioimmunoassay in tissue extracts from the large intestine of transplanted mice developing colitis and from BALB/c and SCID control mice. RESULTS: In the middle and descending colon segments showing the most severe signs of inflammatory lesions in the CD4+ T-cell-transplanted mice, the amount of GLP-2 was significantly lower than in similar colon segments in both untransplanted SCID mice and normal BALB/c mice (P = 0.0013 and 0.0033). In the descending colon the amount of GLP-2 was 6.7 +/- 1.0 pmol/g protein in the CD4+ transplanted mice compared with 68.4 +/- 20.3 and 42.7 +/- 4.3 in the two groups of control mice. Similar findings were made with regard to the contents of the two other proglucagon-derived intestinal peptides, glicentin and GLP-1. CONCLUSION: The amount of GLP-2 is markedly reduced in the colon of mice with a T-cell-induced inflammatory bowel disease histopathologically resembling both Crohn disease and ulcerative colitis. This observation may provide a pathophysiologic rationale for administration of GLP-2 as a trophic factor in inflammatory bowel disease.

Animals↗
PubMed1986

Evidence of hybrid cell of thyroid follicular cell and carcinoid cell in strumal carcinoid.

A strumal carcinoid associated with mature cystic teratoma of the ovary in a 59-year-old was investigated immunohistochemically and electron microscopically. Histologically it was composed largely of trabecular and partly of insular carcinoid and individual thyroid follicles. Intensive argyrophilia was shown in both the cells of carcinoid tumor and follicular structure. Thyroglobulin was strongly positive in the follicular lining epithelium and weakly positive in the carcinoid cells adjacent to the follicular area. Immunoreactive cells for somatostatin and prostatic acid phosphatase were strongly detected in the carcinoid area and gradually blended to the follicular epithelium. Methionine-enkephalin, glicentin, and pancreatic polypeptide were focally detected in the carcinoid area. Whereas calcitonin-positive cells were sparsely observed in the follicular area, carcinoembryonic antigen and serotonin were absolutely negative. Electron microscopic findings revealed abundant neurosecretory granules, microfilaments, and colloid-like droplets in the same cells. We suggest that these hybrid cells are the origin of strumal carcinoid.

Carcinoid Tumor↗
PubMed1984

A quantitative study of enteric endocrine cells in celiac sprue.

A quantitative morphological investigation of eight endocrine cell types in mucosal biopsies from adults with untreated celiac sprue was undertaken. The quantitative data expressed as cells per millimeter of epithelium most accurately reflected the changes seen in celiac disease, as it takes into account changes in mucosal thickness due to the absence of villi in celiac biopsies. The results showed significant increases in the number of cholecystokinin and enterochromaffin cells, a significant decrease in somatostatin, gastric inhibitory polypeptide and secretin cells, and no change in the motilin, gastrin, and glicentin cells. Significant changes in cell size (cross-sectional area) were also demonstrated in the somatostatin and gastrin cells which were smaller in the celiac biopsies.

Adult↗
PubMed1998

Surgical aspect of enteroinsular axis after gastrointestinal surgery with reference to incretin secretion.

An alteration of the enteroinsular axis (EIA) may be an important etiologic factor in postsurgical changes in gastrointestinal (GI) function. In this review, we present recent works, both from our laboratory and others, on how changes in the EIA function may be involved in postsurgical GI complications, especially late dumping syndrome (LDS). We found no or minimal direct role for vagal signals in the control of gastric inhibitory polypeptide (GIP) and enteroglucagon secretion, which regulate EIA function. In gastrectomized patients, it is suggested that the hypersecretion of glicentin and glucagon-like peptide-1 (GLP-1) induced by a rapid arrival of nutrients to the distal gut suppresses glucagon secretion and may be a cause of LDS. In patients who underwent proctocolectomy, we observed no significant postoperative changes in EIA function, although there are some conflicting reports. It seems unlikely that ordinary pancreaticobiliary diversion would cause a significant change in EIA function after an oral glucose load. Our experimental model of ileojejunal transposition produced marked hypersecretion of incretin secreted from the distal gut, which may alter EIA function. Further elucidation of the regulatory mechanism of EIA may provide a new strategy for the medical and surgical treatment of LDS.

Digestive System Surgical Procedures↗
PubMed1985

Endocrine liver tumour differential diagnosis from hepatocellular carcinoma.

A liver tumour, initially diagnosed by light microscopy as a hepatocellular carcinoma, was later shown to be endocrine by argyrophilia and electron microscopy. It was tested by immunohistochemistry for insulin, glucagon, gastrin, VIP, pancreatic polypeptide, glicentin, C-peptide and somatostatin. A few cells were shown to contain somatostatin, but the secretion product in most of the cells was not identified. The patient is well, without any sign of endocrine disturbances, 18 months after the operation.

Carcinoma, Hepatocellular↗
PubMed1988

Carcinoid tumor of the middle ear. An immunohistochemical and electron microscopic study. Report of a case.

A primary tumor of the middle ear was examined histologically, histochemically, immunohistochemically and ultrastructurally. Neuroendocrine cell differentiation, a carcinoid feature, was demonstrated by the presence of numerous argyrophil granules, as well as positive serotonin, glicentin, glucagon, and human pancreatic polypeptide (hPP) granules in some of the Grimelium-positive cells. Chromogranin A was also detected in the cells, but much less frequently than Grimelius-positive staining. Neither neuron-specific enolase (NSE) nor epithelial membrane antigen (EMA) was demonstrated in the tumor. Mucin was demonstrated only intraluminally. Electron microscopy revealed many typical neurosecretory granules in tumor cells, but no apical mucin granules. The tumor appeared to be benign, and there has been no sign of recurrence during a postoperative period of one year.

Adult↗
PubMed1990

Atypical carcinoid tumor of the lung, associated with giant-cell transformation in bone metastasis.

A case of neuroendocrine lung tumor located beneath the pleura in a 71-year-old woman is reported. At autopsy, the tumor was found to have metastasized to the bones and liver without involving the hilar lymph nodes. Histologically, the tumor cells at the primary site and in the liver metastasis exhibited a carcinoid-like organoid structure, whereas pleomorphic giant cells were noted in the bone metastasis. The argyrophilic tumor cells were immunoreactive for neuron-specific enolase, chromogranin A, serotonin, calcitonin, calcitonin gene-related peptide, gastrin-releasing peptide, neuropeptide Y, gastrin, pancreatic polypeptide, glicentin, the alpha-subunit of human chorionic gonadotropin, keratin, epithelial membrane antigen, Leu M1 and carcinoembryonic antigen. Electron microscopy revealed abundant neurosecretory granules in the cytoplasm. This was considered to be a rare case of neuroendocrine lung tumor showing carcinoid-like histology at the primary site and large-cell transformation in bone metastasis.

Aged↗
PubMed1999

Diabetic intestinal growth adaptation and glucagon-like peptide 2 in the rat: effects of dietary fibre.

BACKGROUND/AIMS: Dietary fibre influence growth and function of the upper gastrointestinal tract. This study investigates the importance of dietary fibre in intestinal growth in experimental diabetes, and correlates intestinal growth with plasma levels of the intestinotrophic factor, glucagon-like peptide 2 (GLP-2). METHODS: Male Wistar rats were randomised to the following groups: two streptozotocin-diabetic and two control groups fed either a fibre-containing or a fibre-free diet for three weeks. Intestinal weight, length, and morphometric data (villus height, villus area, crypt depth) were measured. Blood samples were obtained after two weeks for measurement of GLP-2 and enteroglucagon (glicentin, oxyntomodulin). RESULTS: The mean daily consumption of food in the two diabetic groups was 40% higher than in controls. In diabetic rats fed fibre, the increase in intestinal weight from day 0 to 20 was sixfold greater than that of the controls and small intestine weight per cm length was increased by 50%. In the diabetic rats fed a fibre-free diet, intestinal growth was 30% less than in diabetic rats fed fibre, and intestinal weight increased only threefold compared with controls. Morphometric data showed that the intestinal increase in diabetic rats fed fibre was due primarily to growth of the mucosal layer. Villus height and crypt depth increased 60% and 40% respectively, but by only 20% in fibre-free diabetic rats. The plasma levels of GLP-2 parallelled diabetic intestinal growth, whereas plasma levels of enteroglucagon increased regardless of the extent of intestinal growth. CONCLUSIONS: Intestinal growth in experimental diabetes is strongly influenced by the presence of dietary fibre. The effect may be mediated by GLP-2.

Animals↗
PubMed2003

Differential regional metabolism of glucagon in anesthetized pigs.

Glucagon metabolism under basal (endogenous) conditions and during intravenous glucagon infusion was studied in anesthetized pigs by use of midregion (M), COOH-terminal (C), and NH2-terminal (N)-RIAs. Arteriovenous concentration differences revealed a negative extraction of endogenous glucagon immunoreactivity across the portal bed (-35.4 +/- 11.0, -40.3 +/- 9.6, -35.6 +/- 16.9%, M-, C-, N-RIA, respectively), reflecting net secretion of pancreatic glucagon and intestinal glicentin and oxyntomodulin, but under exogenous conditions, a net extraction occurred (11.6 +/- 3.6 and 18.6 +/- 5.7%, C- and N-RIA, respectively). Hindlimb extraction of endogenous (17.4 +/- 3.7%, C-RIA) and exogenous (29.1 +/- 4.8 and 19.8 +/- 5.1%, C- and M-RIA) glucagon was detected, indicating M and C cleavage of the molecule. Renal extraction of glucagon was detected by all assays under endogenous (19.4 +/- 6.7, 33.9 +/- 7.1, 29.5 +/- 6.7%, M-, C-, N-RIA) and exogenous conditions (46.9 +/- 4.8, 46.4 +/- 6.0, 47.0 +/- 7.7%; M-, C-, N-RIA), indicating substantial elimination of the peptide. Hepatic glucagon extraction was undetectable under basal conditions and detected only by M-RIA (10.0 +/- 3.8%) during glucagon infusion, indicating limited midregional cleavage of the molecule. The plasma half-life determined by C- and N-RIAs (2.7 +/- 0.2 and 2.3 +/- 0.2 min) were similar, but both were shorter than when determined by M-RIA (3.2 +/- 0.2 min, P < 0.02). Metabolic clearance rates were similar regardless of assay (14.4 +/- 1.1, 13.6 +/- 1.7, 17.0 +/- 1.7 ml x kg-1 x min-1, M-, C-, N-RIA). Porcine plasma degraded glucagon, but this was not significantly affected by the dipeptidyl peptidase IV (DPP IV) inhibitor valine-pyrrolidide, and in anesthetized pigs, glucagon's metabolic stability was unchanged by DPP IV inhibition. We conclude that tissue-specific metabolism of glucagon occurs, with the kidney being the main site of removal and the liver playing little, if any, role. Furthermore, valine-pyrrolidide has no effect on glucagon stability, suggesting that DPP IV is unimportant in glucagon metabolism in vivo, in contrast to its significant role in the metabolism of the other proglucagon-derived peptides and glucose-dependent insulinotropic polypeptide.

Anesthesia↗
PubMed1989

Response of gut glucagon-like immunoreactivity to hypoglycemia in dogs.

Previous studies demonstrated that insulin-induced hypoglycemia enhances glicentin secretion in piglets and prompted us to investigate the response of glucagon-like immunoreactivity (GLI) to hypoglycemia in dogs. Insulin hypoglycemia did not induce any rise of plasma total immunoreactive glucagon (IRG) measured by nonspecific antiserum to glucagon in normal or pancreatectomized dogs under anesthesia. In contrast, insulin-induced hypoglycemia clearly increased plasma total IRG in both normal and pancreatectomized dogs in a conscious state. Administration of acetylcholine resulted in an elevation of plasma total IRG, whereas epinephrine induced a slight increase in plasma total IRG. The infusion of alpha- or beta-adrenergic blockers did not affect the response of plasma total IRG to hypoglycemia, whereas atropine completely blunted the increase in plasma total IRG during insulin hypoglycemia. Similarly atropine abolished the rise of plasma total IRG during intravenous administration of 2-deoxy-D-glucose. It is concluded that hypoglycemia clearly enhances the secretion of GLI from the gut in dogs and that GLI secretion during hypoglycemia is modulated, at least in part, by the autonomic nervous system.

Acetylcholine↗
PubMed1984

Pattern of cell proliferation and enteroglucagon response following small bowel resection in the rat.

Gut resection triggers off a complex series of adaptive changes in the remaining bowel. There is evidence that these are partly mediated by hormonal factors and enteroglucagons have been proposed as candidates for this role. It is uncertain, however, whether plasma enteroglucagon concentrations rise quickly enough to be involved in the rapid initial response or are persistent enough for chronic maintenance. Plasma concentrations of enteroglucagon were therefore estimated at varying times following gut resection and related to crypt cell production rate (CCPR), which was used as an index of cellular proliferation. 96 male Wistar rats had either 75% proximal small bowel resection or jejunal transection (controls). Groups of animals were killed at 1.5, 3, 6, 12, 24 and 48 days following operation and the plasma enteroglucagon and CCPR in the terminal ileum were estimated. Both values were markedly elevated at 1.5 days and continued to rise in a very similar manner in the resected group of rats. Gel permeation chromatography on Sephadex G-50 of plasma samples showed that the increase in plasma enteroglucagon was mainly due to an increase in a component of Kav 0.25, of similar molecular size to that of porcine glicentin. Thus the principal form of enteroglucagon, as a possible trophic hormone, does respond sufficiently quickly, and the response is maintained for long enough, to be involved throughout the adaptive process.

Animals↗