Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P61278 (somatostatin)
 22,083 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Although the general organization of the sheep brain is similar to that of other mammals, there are species differences in the fine architecture and neurotransmitter distribution. In sheep, perikarya are generally scattered, unlike the situation in rodents where they are clustered. The same organization is observed in cows and primates. The density of neurones immunoreactive for tyrosine hydroxylase in the dorsorostral diencephalon of sheep is lower than in rodents; A14 and A15 dopaminergic cell groups do not present a dorsal part. Only one adrenergic group, C2, is observed in the dorsomedial medulla oblongata. GnRH-immunoreactive neurones are mainly found in the anterior hypothalamic-preoptic areas, a few being present in the mediobasal hypothalamus. The density of several neurones containing neuropeptides (for example vasoactive intestinal polypeptide, cholecystokinin and somatostatin) in the caudal brain of sheep is lower than in other species and in the forebrain of sheep. These differences contribute to different patterns of innervation of brain areas compared with other species. For example, the suprachiasmatic nucleus does not present a dense network of fibres immunoreactive for 5-hydroxytryptamine and neuropeptide Y as observed in rats. These morphological studies constitute information necessary for further physiological investigations.
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PMID:Distribution of neurotransmitters in the sheep brain. 762 14

Insulin has been isolated from an extract of the pancreas of an Agnathan, the river lamprey Lampetra fluviatilis. The primary structure of the peptide (A-chain: GIVEQ CCHRK CSIYD MENYC N; B-chain: SALTG AGGTH LCGSH LVEAL YVVCG DRGFF YTPSK T) is the same as that of insulin from the sea lamprey Petromyzon marinus. In contrast, Lampetra glucagon (HAQGS FTSDY SKYLD SKQAK DFVIW LMNT), isolated from an extract of intestine, is structurally more similar to human glucagon (five amino acid substitutions) than to Petromyzon glucagon (six substitutions). Similarly, the primary structure of somatostatin (AAAAP GAAGG AQLPL GNRER KAGCK NFFWK TFSSC), isolated from Lampetra pancreas, contains eight amino acid substitutions and an additional residue compared with Petromyzon somatostatin. Somatostatin, isolated from Lampetra brain, has an identical structure to mammalian somatostatin-14 (AGCKN FFWKT FTSC), indicative of the same tissue-specific expression of different somatostatin genes that was previously observed in Petromyzon. In contrast to the reduced binding affinity of other fish insulins, lamprey insulin was equipotent with porcine insulin in inhibiting the binding of [3-[125I]iodotyrosine-A14] human insulin to the human insulin receptor.
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PMID:Characterization of insulin, glucagon, and somatostatin from the river lamprey, Lampetra fluviatilis. 857 65

Insulin was purified from an extract of the pancreas of the Burmese python, Python molurus (Squamata:Serpentes) and its primary structure established as: A Chain: Gly-Ile-Val-Glu-Gln-Cys-Cys-Glu-Asn-Thr10-Cys-Ser-Leu-Tyr-Glu-Leu- Glu-Asn-Tyr-Cys20-Asn. B-Chain: Ala-Pro-Asn-Gln-His-Leu-Cys-Gly-Ser-His10-Leu-Val-Glu-Ala-Leu-Tyr- Leu-Val-Cys-Gly20-Asp-Arg-Gly-Phe-Tyr-Tyr-Ser-Pro-Arg-Ser30. With the exception of the conservative substitution Phe --> Tyr at position B25, those residues in human insulin that comprise the receptor-binding and those residues involved in dimer and hexamer formation are fully conserved in python insulin. Python insulin was slightly more potent (1.8-fold) than human insulin in inhibiting the binding of [125I-Tyr-A14] insulin to the soluble full-length recombinant human insulin receptor but was slightly less potent (1.5-fold) than human insulin for inhibiting binding to the secreted extracellular domain of the receptor. The primary structure of python glucagon contains only one amino acid substitution (Ser28 --> Asn) compared with turtle/duck glucagon and python somatostatin is identical to that of mammalian somatostatin-14. In contrast, python pancreatic polypeptide (Arg-Ile-Ala-Pro-Val-Phe-Pro-Gly-Lys-Asp10-Glu-Leu-Ala-Lys-Phe- Tyr20-Thr-Glu-Leu-Gln-Gln-Tyr-Leu-Asn-Ser-Ile30-Asn-Arg-Pro-Arg -Phe.NH2) contains only 35 instead of the customary 36 residues and the amino acid sequence of this peptide has been poorly conserved between reptiles and birds (18 substitutions compared with alligator and 20 substitutions compared with chicken).
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PMID:Purification and characterization of islet hormones (insulin, glucagon, pancreatic, polypeptide and somatostatin) from the Burmese python, Python molurus. 935 Sep 78

Cysteamine, a potent depletor of prolactin and somatostatin, was used to determine the role of prolactin and somatostatin in the control of central dopamine neurones in prepubertal rats. Cysteamine (100 mg/kg, i.p., twice daily) was injected for 7, 14 or 21 days in 28-day-old Sprague-Dawley female rats in one study and for 3 days in 35-day-old rats in another. In control rats, the 3, 4-dihydroxyphenylacetic acid (DOPAC) levels in the median eminence increased threefold from day 35 to day 49, and serum prolactin concentration increased about 50%. Cysteamine lowered serum prolactin concentrations to 20%, and median eminence DOPAC and dopamine levels to 32-50% of control levels in both studies. The DOPAC levels in the nucleus accumbens and striatum were also lowered, while both DOPAC and dopamine in the paraventricular nucleus and periventricular nucleus (A14) were increased by cysteamine. A single injection of rat prolactin (0.01, 0.1 or 1 mg/kg) significantly increased DOPAC or DOPA levels in the median eminence, nucleus accumbens and striatum, but not in the paraventricular nucleus or A14 at 14 h later in 28-day old female rats or in 40-day-old rats pretreated with cysteamine. In contrast, central injection of somatostatin dose (0.001-1 microg/rat) and time (30-90 min) dependently decreased the DOPAC levels in the median eminence, paraventricular nucleus and A14 and increased those in the nucleus accumbens and striatum of adult female rats. These results indicate that serum prolactin is important for the maturation and maintenance of dopamine systems in the median eminence, nucleus accumbens and striatum, while somatostatin exhibits inhibitory and stimulatory effects on hypothalamic and midbrain dopamine systems, respectively.
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PMID:Stimulatory role of prolactin on the development of tuberoinfundibular dopaminergic neurones in prepubertal female rats: studies with cysteamine and somatostatin. 1058 25

Insulin, glucagon, somatostatin-14, and three structurally related molecular forms of peptide tyrosine-tyrosine (PYY) were isolated from an extract of the combined pancreas and gastrointestinal tract of the pallid sturgeon, Scaphirhynchus albus. Pallid sturgeon insulin was identical to insulin from the Russian sturgeon, Acipenser guldenstaedti, and to insulin-2 from the paddlefish, Polyodon spathula, and was approximately twofold less potent than human insulin in inhibiting the binding of [3-[(125)I] iodotyrosine-A14] human insulin to the soluble human insulin receptor. The sturgeon glucagon (HSQGMFTNDY(10)-SKYLEEKLAQ(20) EFVEWLKNGK(30)S), like the two paddlefish glucagons, contains 31 rather than 29 amino acid residues, indicative of an anomalous pathway of posttranslational processing of proglucagon. Pallid sturgeon somatostatin, identical to human somatostatin-14, was also isolated in a second molecular form containing an oxidized tryptophan residue, but [Pro(2)]somatostatin-14, previously isolated from the pituitary of A. guldenstaedti, was not identified. Sturgeon PYY (FPPKPEHPGD(10)DAPAEDVAKY(20)YTALRHYINL(30) ITRQRY.HN(2)) was also isolated in variant forms containing the substitutions (Phe(1) --> Ala) and (Ala(18) --> Val), indicative of at least two gene duplications occurring within the Acipenseriformes lineage. The amino acid sequences of the pallidsturgeon PYY peptides are appreciably different from the proposed "ancestral" PYY sequence that has otherwise been very strongly conserved among the actinopterygian and elasmobranch fish.
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PMID:Gastroenteropancreatic hormones (insulin, glucagon, somatostatin, and multiple forms of PYY) from the pallid sturgeon, Scaphirhynchus albus (Acipenseriformes). 1112

Based on previous work describing the distribution of somatostatin-28 (1-12) in the male alpaca (Lama pacos) diencephalon, and owing to the well known interactions between this peptide and the catecholaminergic system, the aims of this work are (1) to describe the distribution of putative catecholaminergic cell groups in the alpaca diencephalon and (2) to study the possible morphological basis of the interactions between these substances in the diencephalon of the alpaca by using double immunohistochemistry methods. Thus, the distribution of catecholaminergic cell groups in the alpaca diencephalon agrees with that previously described in the diencephalon of other mammalian species of the same order: the A11, A12, A13, A14 and A15d cell groups have been identified; however, we have observed an additional hitherto undescribed cell group containing tyrosine hydroxylase in the medial habenula. In addition, double-labelling procedures did not reveal neurons containing tyrosine hydroxylase and somatostatin, suggesting that the hypothalamic interactions between catecholamines and somatostatin at intra-cellular level must be carried out by a somatostatin molecule other than fragment (1-12). Otherwise, the overlapping distribution patterns of these substances would suggest some interconnections between groups of chemospecific neurons. These results could be the starting point for future studies on hypothalamic functions in alpacas, for example those concerning reproductive control, since other physiological studies have suggested that this species could have different regulatory mechanisms from other mammalian species. Our results support the Manger hypothesis that the same nuclear complement of neural systems exists in the brain of species of the same order.
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PMID:Mapping of tyrosine hydroxylase in the diencephalon of alpaca (Lama pacos) and co-distribution with somatostatin-28 (1-12). 2347 24