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At least 109 records · Page 6Linked to original sources
PubMed1983

A novel subtyping of intestinal metaplasia of the stomach, with special reference to the histochemical characterizations of endocrine cells.

Intestinal metaplasia of the stomach was grouped into 3 subtypes (A, B and C) according to the degree of pyloric gland involution which was judged from patterns of paradoxical Concanavalin A staining after Katsuyama and Spicer. The appearance of endocrine cells was investigated with immunohistochemical and silver methods. Type A metaplasia with slightly to moderately atrophic pyloric glands corresponded to the incomplete type in the previous classification, while Type C showing complete disappearance of pyloric glands corresponded to the complete type. Type B with severely atrophic pyloric glands was an intermediate. This subtyping reflects the cell kinetics in the intestinalized mucosa well. Regarding the endocrine cells, their total number varied in the order Type A greater than Type B greater than Type C. The selective populations of the endocrine cells including glicentin-containing cells, Grimelius-positive argyrophil cells without argentaffinity and intestinal-type enterochromaffin cells frequently formed hyperplastic foci in the intestinalized areas, where the other gut-type and proper gastric-type endocrine cells were scarcely noted. Immunoreactivity of glucagon or bovine pancreatic polypeptide were occasionally identified in a subpopulation of the glicentin-containing cells.

Adult↗
PubMed1984

Immunocytochemical investigation of the gastro-entero-pancreatic (GEP) neurohormonal peptides in the pancreas and gastrointestinal tract of the dogfish Squalus acanthias.

The pancreas and gastrointestinal tract (GIT) of adults and of an embryonic stage of 11 cm long (about half the length of newborn fish) of the spiny dogfish, Squalus acanthias, were investigated immunocytochemically for the occurrence of the gastro-entero-pancreatic (GEP) neurohormonal peptides. In the pancreas of adult forms 5 endocrine cell types were seen, namely insulin-, somatostatin-, glucagon-, pancreatic polypeptide (PP)- and gastric inhibitory peptide (GIP)-immunoreactive cells. These cell types form scattered islets and were seen sometimes to surround small ducts. GIP-immunoreactivity cells did not occur in glucagon-containing cells. In the mucosa of GIT of adults 18 endocrine cell types were observed, viz. insulin-, somatostatin-, glucagon-, glicentin, PP-, polypeptide YY (PYY)-, vasoactive intestinal polypeptide (VIP)-, GIP-, gastrin C-terminus, CCK-, neurotensin N-terminus-, bombesin/gastrin releasing peptide (GRP)-, substance P-, enkephalin-, alpha-endorphin, beta-endorphin-, serotonin- and calcitonin immunoreactive cells. These cells occurred mostly in the intestine. All these cell types were of the open type, except glucagon- and glicentin-immunoreactive cells in the stomach, which seemed to be of the closed type. In the muscle layers and the submucosa, VIP and substance P- immunoreactive nerves and neurons were observed. In the pancreas of the dogfish embryo only 3 endocrine cell types could be demonstrated, namely insulin-, somatostatin- and glucagon-immunoreactive cells. In the mucosa of the GIT of the embryos studied 12 endocrine cell types were detected, viz. insulin-, somatostatin-, glucagon-, PP-, PYY-, VIP, GIP, gastrin C-terminus-, CCK-, neurotensin N-terminus-, enkephalin- and serotonin immunoreactive cells. The number of these cells, except that of PYY-immunoreactive cells, was lower than that of adults and in some cases their distribution did not correspond with that of adults.

Animals↗
PubMed1991

Glucagonomas of transgenic mice express a wide range of general neuroendocrine markers and bioactive peptides.

Pancreatic tumours of transgenic mice carrying a glucagon-promoted simian virus 40 (SV40) T antigen oncogene have been analysed by histological, histochemical, ultrastructural and radioimmunological means. Seven transgenic mice were examined revealing dysplastic and neoplastic lesions in the endocrine pancreas. Four tumours were identified, one of which metastasized to periadrenal spaces and paravertebral lymph nodes. Benign tumours were composed of argyrophilic, endocrine cells reactive to a range of antibodies against neuroendocrine markers (neuron-specific enolase, protein gene product 9.5, chromogranin A, synaptophysin and protein 7B2) and different fragments of the proglucagon molecule (glucagon, glicentin, glucagon-like polypeptides 1 and 2). A few tumour cells expressed pancreatic polypeptide, somatostatin or insulin. Conventional ultrastructural analysis and immunogold labelling revealed typical glucagon-immunoreactive alpha granules which co-stored glicentin and glucagon-like polypeptides 1 and 2. The malignant primary tumour and its metastases were composed mainly of cells which did not show immunoreactivity for neuroendocrine markers or peptides. Atypical, glucagon-immunogold labelled granules were detected at electron microscopy in differentiated tumour cells and C-type retroviral particles in the largest tumour population of degranulated cells. The transgene-encoded oncoprotein SV40 large T-antigen was detected in the nuclei of well-differentiated tumour cells and in alpha cells of some dysplastic islets. All tumour-bearing mice showed high levels of circulating glucagon-like immunoreactivity. Transgenic mice harbouring the glucagon-promoted SV40 T antigen oncogene may provide a model for human glucagonoma.

Animals↗
PubMedDate not supplied

Multiple hormone storage by 'polycrine' cells in the pancreas (from a case of nesidioblastosis).

Pancreatic tissue from a case of neonatal hypoglycaemia with nesidioblastosis has been studied by routine light and electron microscope techniques and by highly sensitive light and electron microscope immunolocalization methods. A hyperplastic nodule within the pancreas from this case contained enlarged distorted haemorrhagic islets, with a variable rim of exocrine tissue. Islet cells in these areas were shown to contain more than one hormone in separate granules. An immunoperoxidase system using hapten-labelled primary antibodies and photochemical amplification applied to serial semithin sections suggested a consistent overlap between insulin and glucagon immunoreactive cells. Serial ultrathin sections of tissue embedded in LR White showed that some heteromorphous cells with predominantly beta-granules also contained a minority population of granules which had either glucagon or glicentin immunoreactivity. In adjacent studies, the same techniques confirmed that the majority population of granules did indeed contain insulin, and immunocolloidal gold methods were used to show that glucagon and glicentin containing granules were present in the same cells. The significance of these findings is discussed, including the possibility that cells containing more than one granule type might represent a subpopulation of facultative cells in transit from producing one hormone to producing a second. The importance of sensitive immuno-electron microscopy in the investigation of endocrine lesions is stressed.

Cytoplasmic Granules↗
PubMedDate not supplied

Plasma levels of glucagon-like polypeptides in patients with esophagoplasty.

Seven patients with interposition of a jejunal tract between the esophagus and stomach or duodenum (EP group) and ten healthy normal volunteers have been submitted to an oral glucose load (OGTT) to clarify the significance of glucagon-like polypeptides (GLI) induced by glucose in carbohydrate metabolism. Blood glucose (BG) and GLI plasma levels were significantly higher in the EP group than in the normal one (p less than 0.01), respectively 30, 60, 90 min for BG and during all the test for GLI. The fasting immunoreactive glucagon (IRG) plasma levels were significantly lower in patients than in normals (p less than 0.05) whereas a marked and significant increase was observed in the EP group (p less than 0.01) from 90 to 240 min. The precocious stimulation of jejunal mucosa and the rapid intestinal transit which occur in these patients may explain the elevated GLI (probably glicentin) plasma levels. The rise in IRG plasma levels might be due to the enzymatic transformation of glicentin. The role of these types of glucagon on carbohydrate metabolism is still to be fully clarified.

Aged↗
PubMed1985

Rat pancreas contains the proglucagon(64-69) fragment and arginine stimulates its release.

Rat proglucagon(64-69) corresponding to the C-terminal hexapeptide of putative rat glicentin sequence in the precursor was synthesized. A glicentin C-terminal hexapeptide specific radioimmunoassay, using the synthetic hexapeptide as standard, demonstrated the presence in rat pancreas of a peptide identified with the synthetic rat proglucagon(64-69): H-Asn-Arg-Asn-Asn-Ile-Ala-OH. The hexapeptide was released concomitantly with glucagon by arginine stimulation from the isolated perfused rat pancreas. The results indicate that the pancreas co-stores and possibly co-releases the hexapeptide with glucagon as one of the processing products of proglucagon.

Amino Acid Sequence↗
PubMed1985

Glucagon- and PP-related peptides of intestinal L cells and pancreatic/gastric A or PP cells. Possible interrelationships of peptides and cells during evolution, fetal development and tumor growth.

The immunohistochemical detection of six distinct sequences of proglucagon and its derivatives (GRPP, glicentin, glucagon-37, glucagon-29, GLP1, GLP2 and MPGF) in both intestinal L cells and pancreatic or gastric A cells of some mammals (dog, man, guinea pig) confirms that the two cell types produce the same proglucagon molecule, although the final step of its post-translational processing differs in the two cells. Immunohistochemical and ultrastructural patterns of glucagon/glicentin cells in the pancreas of lower vertebrates and early human fetuses, as well as tumor cell studies, suggest an evolution of gastropancreatic A cells from L cells. On the contrary, the PP-related peptide PYY of intestinal L cells, and PP with its C-terminal icosapeptide extension of pancreatic PP cells, likely originate from different prohormones. Although intermediate patterns of peptide expression can be observed, including some F-type PP cells of the dog pancreas (uncinate process) and pyloric mucosa showing PYY immunoreactivity or rare PYY and/or HPP immunoreactive cells of the human rectum lacking glicentin reactivity, no obvious relationship can be established between L cells and pancreatic (F-type) PP cells. However, some evolutionary, embryogenetic and oncogenetic link may exist between L cells and human D1-type PP cells, a minor population of PP cells scattered in the pancreatic tissue of dorsal pouch origin and a major fraction of tumor PP cells.

Animals↗
PubMed1983

Mammalian pancreatic preproglucagon contains three glucagon-related peptides.

We have isolated cDNA clones encoding bovine pancreatic preproglucagon. Twenty-five putative preproglucagon clones were selected by screening 3,100 clones of a fetal bovine pancreas cDNA library with a synthetic oligodeoxynucleotide probe. The probe was a mixture of synthetic 17-base DNA oligomers constructed to correspond to the six carboxyl-terminal amino acids (residues 24-29) of mature glucagon. Restriction mapping of six of these clones suggested that they represented a single mRNA species. Primary sequence analysis of one clone containing a 1,200-base-pair DNA insert revealed that it contained an essentially full-length copy of glucagon mRNA. Analysis of the cDNA suggested a protein coding sequence of 540 nucleotides and 5'- and 3'-untranslated regions of 90 and 471 nucleotides, respectively. This cDNA sequence encoded a 20-amino acid signal sequence followed by one for glicentin, a 69-amino acid polypeptide containing an internal glucagon moiety that has been found in porcine intestines. Glicentin is followed by two additional glucagon-like peptides, each flanked by paired basic amino acids (Lys, Arg) characteristic of prohormone processing. These polypeptide sequences show striking homology with those for glucagon and other members of the glucagon family of peptides.

Amino Acid Sequence↗
PubMed1995

Differential processing of proglucagon by the subtilisin-like prohormone convertases PC2 and PC3 to generate either glucagon or glucagon-like peptide.

Proglucagon is processed differently in the islet alpha cells and the intestinal endocrine L cells to release either glucagon or glucagon-like peptide 1-(7-37) (GLP1-(7-37)), peptide hormones with opposing actions in vivo. In previous studies with a transformed alpha cell line (alpha TC1-6) we demonstrated that the kexin/subtilisin-like prohormone convertase, PC2 (SPC2), is responsible for generating the typical alpha cell pattern of proglucagon processing, giving rise to glucagon and leaving unprocessed the entire C-terminal half-molecule known as major proglucagon fragment or MPGF (Rouillé, Y., Westermark, G., Martin, S. K., Steiner. D. F. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 3242-3246). Here we present evidence, using mouse pituitary AtT-20 cells infected with a vaccinia viral vector encoding proglucagon, that PC3 (SPC3), the major neuroendocrine prohormone convertase in these cells, reproduces the intestinal L cell processing phenotype, in which MPGF is processed to release two glucagon-related peptides, GLP1 and GLP2, while the glucagon-containing N-terminal half-molecule (glicentin) is only partially processed to oxyntomodulin and small amounts of glucagon. Moreover, in AtT-20 cells stably transfected with PC2 (AtT-20/PC2 cells), glicentin was efficiently processed to glucagon, providing further support for the conclusion that PC2 is the enzyme responsible for the alpha cell processing phenotype. In other cell lines expressing both PC2 and PC3 (STC-1 and beta TC-3), proglucagon was also processed extensively to both glucagon and GLP1-(7-37), although STC-1 cells express lower levels of PC2 and processed the N-terminal domain to glucagon less efficiently. In contrast, GH4C1 and COS 7 cells, which express very little or no PC2 or PC3, failed to process proglucagon, aside from a low level of interdomain cleavage which occurred only in the GH4C1 cells. In vitro PC3 did not cleave at the single Arg residue in GLP1 to generate GLP1-(7-37), its truncated biologically active form, indicating the likelihood that another convertase is required for this cleavage.

Amino Acid Sequence↗
PubMed1980

Effects of gastrointestinal polypeptides on hormone content of endocrine pancreas in the rat.

Although trophic actions of gastrointestinal peptides on exocrine pancreas have been shown, little is known regarding their effects in endocrine pancreas. Therefore, we measured the contents of somatostatin-like immunoreactivity (SLI), insulin and glucagon, in pancreatic extracts from rats that had been treated three times a day for 10 days with saline; 1 microgram/kg caerulein; 5, 25, and 100 microgram/kg secretin; 1 microgram/kg caerulein plus 5, 25, and 100 microgram/kg secretin; 25 microgram/kg pancreatic polypeptide; 15 microgram/kg glicentin; or 15 microgram/kg gastric-inhibitory polypeptide. Pancreatic SLI content was significantly increased in rats treated with glicentin and caerulein plus secretin at the two higher doses. No difference was noted between the control and the caerulein plus 100 microgram/kg secretin groups in delta-cell number per islet when examined by the immunoperoxidase technique. These data suggest that because of their effect on SLI content gastrointestinal polypeptides may modulate pancreatic endocrine function.

Animals↗
PubMed1984

Immunocytochemical characterization of secretory granule maturation in pancreatic A-cells.

Antigenic sites related to glucagon and glucagon precursors were characterized by ultrastructural immunocytochemistry in secretory compartments of the pancreatic A-cell, namely Golgi cisternae, condensing granules in Golgi cisternae, coated immature secretory granules, and noncoated mature secretory granules. The C-terminal glucagon immunoreactivity was low in all these compartments except in the noncoated mature secretory granules. By contrast, N-terminal glucagon and glicentin immunoreactivities were high at the condensing granule stage and, respectively, increased (N-terminal) or decreased (glicentin) until the mature secretory granule stage. These data suggest that: 1) glucagon precursors and glucagon coexist at different concentrations in secretory compartments of the A-cell; 2) the condensing granules in Golgi cisternae and immature granules consist predominantly of glucagon precursors; and 3) the removal of the peptide masking the C-terminal of the glucagon molecule occurs between the coated and the mature granule stages.

Animals↗
PubMed1986

Glucagon-like peptides GLP-1 and GLP-2, predicted products of the glucagon gene, are secreted separately from pig small intestine but not pancreas.

We developed specific antibodies and RIAs for glucagon-like peptides 1 and 2 (GLP-1 and GLP-2), two predicted products of the glucagon gene, and studied the occurrence, nature, and secretion of immunoreactive GLP-1 and GLP-2 in pig pancreas and small intestine. Immunoreactive GLP-1 and GLP-2 were identified in glucagon-producing cells of the pancreatic islets, and in glicentin-producing cells of the small intestine. Immunoreactive GLP-1 and 2 in intestinal extracts corresponded in molecular size to peptides synthesized according to the predicted structure. By reverse phase HPLC, intestinal and synthetic GLP-1 behaved similarly, whereas synthetic and intestinal GLP-2 differed. Pancreatic extracts contained a large peptide with both GLP-1 and GLP-2 immunoreactivity. Secretion was studied using isolated perfused pig pancreas during arginine stimulation, and isolated perfused pig ileum during either luminal glucose stimulation or vascular administration of the neuropeptide, gastrin-releasing peptide (GRP). Immunoreactive GLP-1 and GLP-2 were secreted in parallel with pancreatic glucagon and intestinal glicentin. The molecular forms of secreted immunoreactive GLP-1 and 2 corresponded to those identified in the tissue extracts.

Animals↗
PubMed1986

Proglucagon processing in a rat islet cell line resembles phenotype of intestine rather than pancreas.

Proglucagon, synthesized in the pancreatic islets and the intestinal L-cells, contains in its precursor structure glucagon, glicentin, and two glucagon-like peptides (GLP-I and GLP-II) separated by an intervening peptide (IP-II). We have cloned a stable rat islet cell line expressing the glucagon gene at high levels, thereby allowing us to study the posttranslational processing of proglucagon in this cell line. In contrast to the processing of proglucagon in the pancreas, in which glucagon is liberated, in the cell line we found the intestinal pattern of peptides consisting of glicentin, at least two forms of GLP-I [GLP-I-(1-37) and GLP-I-(7-37)], GLP-II, IP-II, and an amidated form of IP-II. No individually processed glucagon peptide was detected. GLP-I-(1-37), GLP-I-(7-37), GLP-II, IP-II, and IP-II amide coeluted with their respective synthetic peptide standards on gel filtration and ion exchange chromatography. The existence of a single glucagon gene in the rat genome and indistinguishable glucagon mRNAs in pancreas and intestine indicates that the neoplastic transformation that occurred in these islet cells is associated with a phenotypic switch in the differential posttranslational processing of proglucagon to a pattern that mimics that found in the intestinal cells. These observations further support the hypothesis of a common progenitor for the intestinal (L) and islet (A) cells.

Animals↗
PubMed1999

Proglucagon processing profile in canine L cells expressing endogenous prohormone convertase 1/3 and prohormone convertase 2.

The tissue-specific differential processing of proglucagon (Pg) yields glucagon in pancreatic A cells and glucagon-like peptide-1 (GLP-1), GLP-2, and glicentin in intestinal L cells. It has been suggested that the difference in Pg cleavage in A and L cells is due to the presence of distinct prohormone convertases (PC) in the two cell types, PC1/3 in the L cell and PC2 in the A cell. PC2 has been shown to cleave the N-terminal part of Pg, being essential for glucagon formation and PC1/3 to cleave the C-terminal part of Pg, leading to the formation of GLP-1. However, some of the cleavage sites in Pg have not proven to be substrates exclusively for either PC2 or PC1/3, and the cleavage profile of Pg in a primary cultured L cell has not yet been correlated with the actual presence of PC2 and PC1/3 in the L cell. We demonstrate here the presence of PC1/3, PC2, and the PC2 chaperone 7b2, in L cells using light immunohistochemistry on sections from canine ileum and on a canine intestinal cell culture enriched for L cells. Analysis of the cultured L cells, using gel chromatography and RIA, confirms the classical intestinal cleavage profile of Pg, resulting in mainly glicentin, oxyntomodulin, GLP-1-(7-37), and GLP-2. Despite the presence of 7b2 and mature PC2, as demonstrated by Western blot, absolute minimal amounts of glucagon were detected. These data show that the presence of intracellular PC2 and 7b2 in a primary cell possessing Pg does not have to lead to the formation of glucagon. This formation must then require an additional element to occur, or alternatively, the results could be explained by a canine specific organization of PC2 and Pg into separate compartments, which would prevent interaction.

Animals↗
PubMed1983

Molecular forms of human enteroglucagon in tissue and plasma: plasma responses to nutrient stimuli in health and in disorders of the upper gastrointestinal tract.

A means of estimating human enteroglucagon (glucagon-like immunoreactivity of intestinal origin) in tissues and plasma is described, based on the subtraction of RIA values obtained with the C-terminal-directed glucagon antiserum RCS5 from the total glucagon-like immunoreactivity determined with the N-terminal- to midmolecule-directed glucagon antiserum R59. Gel filtration on Sephadex G-50 of human plasma and extracts of normal human intestine separated the R59 immunoreactivity into three peaks: a small peak of void volume material, a major peak coeluting with porcine glicentin, and a smaller peak coeluting with pancreatic glucagon. No RCS5 immunoreactivity was detected in the human gut, except for a small amount constituting less than 2% of the total glucagon-like immunoreactivity in the ileum and rectum only. In extracts of human pancreas, the chromatographic profiles obtained with RCS5 and R59 assays differed from the intestinal patterns, but were identical to each other, giving no evidence of a significant amount of pancreatic R59 immunoreactivity that was not also reactive with RCS5. Chromatography of plasmas from healthy subjects and patients with dumping syndrome, active coeliac disease, and tropical sprue showed that only the second major peak of R59 immunoreactivity reflected the basal or postnutrient increases in the plasma enteroglucagon concentration. In patients with exaggerated enteroglucagon release, the rise was again found to be entirely due to an increase in this peak of immunoreactivity. This major molecular form of human enteroglucagon, similar in size to porcine glicentin, is, thus, the form most likely to be of physiological and pathophysiological significance.

Adult↗
PubMed1996

Evidence for redundancy in propeptide/prohormone convertase activities in processing proglucagon: an antisense study.

To further examine the physiological roles of the neuroendocrine prohormone convertases (PCs) in proglucagon processing, alpha TC1-6 cells were transiently transfected with PC1/3 and PC2 expression vectors containing either antisense or sense encoding cDNAs. PC1/3- and PC2-directed RIAs were used to determine that the PC1/3 antisense transfections lowered endogenous levels of PC1/3 by 40 +/- 7.9% but did not alter the levels of PC2. The PC2 antisense transfections decreased the endogenous levels of PC2 by 91 +/- 11.7% without affecting the levels of PC1/3. To quantitate the levels of proglucagon and proglucagon-derived products, transfected cells were metabolically labeled with [3H]tryptophan, and extracts were chromatographed by reversed-phase HPLC. Recovered peptides were then subjected to peptide mapping analyses, allowing precise quantification of 3H-radioactivity incorporated into proglucagon and its cleavage products. Product-precursor ratios were determined, and percent change in the proportion of products generated in antisense-transfected vs. sense-transfected cells was calculated. The decrease in PC1/3 after antisense treatment significantly reduced the amounts of glicentin produced and partially reduced the levels of all other proglucagon cleavage products. PC2 antisense treatment significantly reduced the levels of glicentin and 9K glucagon generated but had no significant effect on the remainder of the proglucagon-derived peptides. These results suggest the existence of redundant mechanisms that ensure the production of each of the intermediate and product peptides derived from proglucagon. PC1/3 is potentially an important enzyme in the processing of most proglucagon-derived peptides, whereas PC2-processing activity appears to predominate at only two of the four potential cleavage sites.

Animals↗
PubMed1987

An immunohistochemical study of the endocrine cells in the gastrointestinal mucosa of the Caiman latirostris.

Twelve endocrine cell types immunoreactive for either 5-hydroxytryptamine (5-HT), somatostatin, gastrin, motilin, neurotensin, bovine pancreatic polypeptide (BPP), avian pancreatic polypeptide (APP), pancreatic glucagon, enteroglucagon, glicentin, secretin or cholecystokinin (CCK) were found in gastrointestinal mucosa of Caiman latirostris. Moderate numbers of enteroglucagon-immunoreactive cells, a few 5-HT-, somatostatin- and motilin-immunoreactive cells and rare pancreatic glucagon-immunoreactive cells were found in the fundic stomach. Numerous gastrin-immunoreactive cells and moderate numbers of somatostatin- and motilin-immunoreactive cells were seen in the pyloric stomach. Moderate numbers of 5-HT-, gastrin-, motilin- and enteroglucagon-immunoreactive cells, a few somatostatin-, neurotensin- and BPP-immunoreactive cells, and rare APP-, pancreatic glucagon-, glicentin-, secretin- and CCK-immunoreactive cells were observed in the proximal intestine. Moderate numbers of 5-HT-immunoreactive cells, small to moderate numbers of neurotensin- and enteroglucagon-immunoreactive cells and occasional somatostatin-, motilin- and BPP-immunoreactive cells were seen in the distal intestine. Moderate numbers of neurotensin-immunoreactive cells and a few 5-HT-immunoreactive cells were found also in the cloaca. Cells immunoreactive for gastrin releasing polypeptide, bombesin and gastric inhibitory peptide were not observed in the caiman gastrointestinal epithelium. The differences in endocrine cell types between the caiman and alligator are discussed in terms of their topographic distribution.

Alligators and Crocodiles↗
PubMed1983

A quantitative immunofluorescent study of the endocrine cell populations in the developing human pancreas.

The immunofluorescent cell content of the pancreas of 8--40-wk fetuses and of 1.5--5-mo Caucasian infants was quantitatively evaluated using anti-insulin, anti-glicentin, anti-glucagon, anti-somatostatin, and anti-pancreatic polypeptide antisera. The most significant findings are: (1) the pancreas of 8--10 wk fetuses contains a sizable population of endocrine cells reacting exclusively to anti-glicentin antiserum. This cell population decreases and disappears in later stages and is replaced by the adult type glucagon/glicentin immunoreactive cell; (2) the pancreatic polypeptide-rich region shows a lower relative endocrine cell content as compared with the glucagon-rich region and its islets appear smaller; (3) in the total pancreas, the relative (volume density) and absolute (microliter) insulin cell content increases regularly with age, while the relative volume of glucagon cells peaks in fetal life (wk 17--20) to decrease in infants, although remaining at higher levels than in adults; the relative and absolute volumes of somatostatin cells are elevated in fetal and infant stages studied where they represent the second most abundant cell type, while pancreatic polypeptide cells appear to least abundant cells during prenatal and infant life. These data show several differences with the pattern of the respective endocrine cell populations in the adult pancreas.

Female↗