Isolation and Characterization of Chicken Insulin

Kimmel, Joe R.; Pollock, H.G.; Hazelwood, Robert L.

doi:10.1210/endo-83-6-1323

Cited by 259 publications

(63 citation statements)

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“…So far, HPP-cells have not been described in the pancreas of human diabetics. "Pancreatic polypeptide" is a 36-aminoacid peptide which has been isolated from the avian pancreas [9,10] and from the pancreas of several mammals, including man [11,12,13,14]. Cells containing "pancreatic polypeptide" have been demonstrated in the pancreas of chicken [21] and of a variety of other species [22,23,24].…”

Section: Discussionmentioning

confidence: 99%

“…This study has indicated that, in contrast with previous suggestions, the islets in juvenile diabetics should not be considered as atrophic tissue, since they contain well granulated endocrine cells, which might play an important r61e in the physiopathology of diabetes. Moreover, the cellular composition of the diabetic islets was also found to alter with the progression of the disease, as was evident from our observation that with time more and more islets in the juvenile diabetics were almost exclusively composed of cells, containing "pancreatic polypeptide", a substance originally extracted from avian pancreas [9,10], and later from the pancreas of several mammalian species, including man [11,12,13,14].…”

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confidence: 87%

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Hyperplasia of “pancreatic polypeptide”-cells in the pancreas of juvenile diabetics

1977

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Section: Discussionmentioning

confidence: 99%

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confidence: 87%

Hyperplasia of “pancreatic polypeptide”-cells in the pancreas of juvenile diabetics

1977

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“…PP was discovered in 1968, when Kimmel et al (1968), while purifying chicken insulin, found a new peptide hormone that they named 'pancreatic polypeptide'. In mammals, virtually all of the PP-producing cells are located in the pancreas mainly within the islets, located in the periphery, and wedged between the A and B cells.…”

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confidence: 99%

Sonic hedgehog and pancreatic-duodenal homeobox 1 expression distinguish between duodenal and pancreatic gastrinomas

Fendrich¹,

Ramerth²,

Waldmann³

et al. 2009

Endocrine-Related Cancer

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Some 80-90% of gastrinomas are located in the gastrinoma triangle, which includes the duodenum, the pancreatic head, and the hepatoduodenal ligament. The natural history of the tumors depends on their origin. Duodenal gastrinomas are much less aggressive than pancreatic primaries and infrequently develop liver metastases. The reason therefore is unclear. The transcription factor pancreatic-duodenal homeobox 1 (Pdx1) is important in differentiation and development of the pancreas and duodenum. In embryonic development, Sonic hedgehog (Shh) expression establishes a sharp molecular boundary, which allows for the proper patterning of the duodenal and pancreatic epithelium. Pancreatic polypeptide (PP) is expressed in pancreatic islets and is known to be expressed in pancreatic endocrine tumors. This study aims to clarify the expression pattern of Pdx1, Shh, and PP in duodenal and pancreatic gastrinomas. Tissue from 15 patients with duodenal and from 11 patients with pancreatic gastrinomas that underwent surgery between 1987 and 2007 at our institution because of a gastrinoma were evaluated by immunohistochemistry (IHC). Furthermore, tissue from lymph node metastases from two patients with a so far undetected primary gastrinoma was analyzed. IHC revealed strong Pdx1 expression in pancreatic gastrinomas, but not in duodenal gastrinomas. By contrast, there was no Shh expression detectable in pancreatic gastrinomas, but found in all duodenal gastrinomas. This pattern was also true for associated metastases. Shh expression combined with absence of Pdx1 expression in lymph node metastases from patients with an unknown location of the primary suggests a so far undetected duodenal gastrinoma. We show for the first time that only pancreatic, but not duodenal gastrinomas express Pdx1. Moreover, only duodenal gastrinomas express Shh, suggesting a different genetic background of these two tumors. Whereas the expression of Pdx1 in pancreatic gastrinomas might suggest their endocrine origin from islets, duodenal gastrinomas develop from a Pdx1 negative cell cluster. The expression pattern of Pdx1, Shh, and PP in resected metastases can help to locate an otherwise undetected primary gastrinoma.

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“…The molecule contains two regions ofsecondary structurean extended polyproline-like helix (residues [1][2][3][4][5][6][7][8] and an a-helix (residues 14-31) -that run roughly antiparallel. The packing together of nonpolar groups from these regions gives the molecule a hydrophobic core in spite of its small size.…”

mentioning

confidence: 99%

“…Pancreatic polypeptide (PP) is a 36-amino acid peptide found in the endocrine pancreas (1,2). There is close sequence homology among the mammalian peptides although mammalian and avian PPs differ at about 20 positions (Fig.…”

mentioning

confidence: 99%

X-ray analysis (1. 4-Å resolution) of avian pancreatic polypeptide: Small globular protein hormone

Blundell

Pitts

Tickle

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

269

156

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The crystal structure of avian pancreatic polypeptide (aPP), a 36-residue polypeptide with some hormonal properties, has been determined by using single isomorphous replacement and anomalous scattering to 2.1-A resolution. The phases were extended to 1.4-A resolution by using a modified tangent formula. The molecule contains two regions ofsecondary structurean extended polyproline-like helix (residues 1-8) and an a-helix (residues 14-31) -that run roughly antiparallel. The packing together of nonpolar groups from these regions gives the molecule a hydrophobic core in spite of its small size. The aPP molecules form a symmetrical dimer in the crystal stabilized principally by interlocking of nonpolar groups from the a-helices. The aPP dimers are crosslinked by coordination ofZn"+; three aPP molecules contribute ligands to each zinc. The coordination geometry is a distorted trigonal bipyramid. The properties of the aPP molecule in solution are consistent with expectations based on the crystal structure. The aPP molecule has several general features in common with the pancreatic hormones insulin and glucagon. All three hormones have complex mechanisms for self-association. Like insulin, aPP seems to have a stable monomeric structure but its biological activity seems to depend on the more flexible COOH-terminal region analogous to the flexible NH2-terminal region of glucagon.Pancreatic polypeptide (PP) is a 36-amino acid peptide found in the endocrine pancreas (1, 2). There is close sequence homology among the mammalian peptides although mammalian and avian PPs differ at about 20 positions (Fig. 1). All sequences have an amidated COOH terminus, a feature known to occur in other polypeptide hormones such as gastrin, secretin, and oxytocin (3). There is now evidence that PP is synthesized as a larger precursor, in the same way as other pancreatic polypeptide hormones (4).The ultrastructural appearance ofthe PP-producing cells also strongly argues for an endocrine function for this peptide. PP is located in membrane-enclosed granules (5) like those of the alpha and beta pancreatic cells in which glucagon and insulin are synthesized. The PP cells are located on the periphery of the islets at the head of the pancreas, to the exclusion of glucagon cells which occur at the periphery of the islets of the tail end (6). In certain fishes such as the teleost Cottus scorpius, which has two principal islets, the pyloric region has mainly PP cells and the splenic contains no PP cells (7).PP is released into the circulation partly as a result of vagal cholinergic stimulation after feeding or in response to hypoglycemia. Although the half-life is of the order of 5 min the levels remain increased for several hours, indicating a continuous release (8). Injections ofbovine PP (bPP) decrease food intake and body weight in the hyperglycemic ob/ob mouse (9), and injections of either the bovine or avian PP (aPP) cause New Zealand obese mice to revert to normal (10). Although these observations indicate that PP may act as a satiety...

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Isolation and Characterization of Chicken Insulin

Cited by 259 publications

References 0 publications

Hyperplasia of “pancreatic polypeptide”-cells in the pancreas of juvenile diabetics

Hyperplasia of “pancreatic polypeptide”-cells in the pancreas of juvenile diabetics

Sonic hedgehog and pancreatic-duodenal homeobox 1 expression distinguish between duodenal and pancreatic gastrinomas

X-ray analysis (1. 4-Å resolution) of avian pancreatic polypeptide: Small globular protein hormone

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