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)

An enzyme-linked immunoassay for somatostatin using somatostatin-alkaline phosphatase conjugate as "labeled" antigen was developed. Minimal detectable dose at present was 40 pg per tube. Serial dilutions of rat hypothalamic extract gave a gradual change of antibody-bound alkaline phosphatase activity which was parallel to that with standard somatostatin. Precision and accuracy of the method were comparable to those in radioimmunoassay reported by others. This method will be a useful tool for the determination of somatostatin, especially in tissues.
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PMID:Enzyme-linked immunoassay of somatostatin. 35 83

The neuronal distributions of somatostatin and neuropeptide Y and their respective mRNAs in hippocampal slice cultures were examined by immunohistochemical staining and in situ hybridization. For the in situ hybridization we used an alkaline phosphatase-labelled oligodeoxynucleotide probe for somatostatin mRNA and an 35S-labelled oligodeoxynucleotide probe for neuropeptide Y mRNA. For both neuropeptides the immunostained and hybridized neurons displayed a comparable, organotypic distribution. Most labelled neurons were located in the dentate hilus and stratum oriens of CA3 and CA1. Additional neurons were found in stratum radiatum and pyramidale of CA3, but very few in the corresponding layers of CA1. In all locations the density of somatostatin- and neuropeptide Y-reactive cells exceeded that observed in vivo. Also, the hybridization signal of the individual neurons appeared enhanced in the slice cultures. Methodologically it was noted that the non-radioactive alkaline phosphatase-labelled oligodeoxynucleotide probe gave excellent in situ hybridization results with detailed cellular resolution and no apparent problems of tissue penetration, even when used on whole-mount explants. These results demonstrate that somatostatin and neuropeptide Y-immunoreactive and mRNA containing neurons retain their organotypic distribution and basic morphological characteristics in the slice cultures. The supernormal density of these neurons and their hybridization signals indicate that a transient developmental increase in neuropeptide expression may persist in vitro.
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PMID:Somatostatin and neuropeptide Y in organotypic slice cultures of the rat hippocampus: an immunocytochemical and in situ hybridization study. 134 30

By inserting appropriate peptide ligands into surface loops on globular proteins, we expect to develop probes for the location, accessibility, and steric and electrostatic environment of these ligand-binding sites on their membrane-bound receptors. Three residues in a loop on the surface of E. coli alkaline phosphatase were substituted by an 18-residue peptide containing the receptor-binding segment of somatostatin-14 without significantly affecting the catalytic properties of the enzyme. This hybrid protein was then used to investigate the ligand-binding site of somatostatin receptors. Tryptic cleavage of the hybrid protein within the inserted sequence, and binding of the hybrid protein to antisomatostatin antibodies demonstrated the surface accessibility of the guest peptide. Both the wild-type enzyme and the hormone-enzyme hybrid displaced 125I-labeled somatostatin from rat brain membrane receptors only at high concentrations. However, chemical cationization of the hybrid protein, which again did not disturb the phosphatase activity, enhanced its receptor-binding potency to a level only 23 times lower than that of somatostatin itself and 280 times higher than that of the cationized wild-type protein. This alkaline phosphatase/somatostatin hybrid protein appears, therefore, to be a suitable starting point for the development of probes for the steric and electrostatic environment of the ligand-binding site of somatostatin receptors.
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PMID:Alkaline phosphatase-somatostatin hybrid proteins as probes for somatostatin-14 receptors. 135 57

In order to investigate the possible involvement of corticotropin-releasing factor (CRF) and somatostatin (SRIF) on thyrotropin-releasing hormone (TRH) neuronal cell activity in the rat hypothalamic paraventricular nucleus, we have proceeded to the simultaneous localization of CRF or SRIF and TRH. For this purpose, we used a dual immunostaining procedure that employed antibodies to CRF and SRIF and peroxidase-labeled goat anti-rabbit IgG as a first sequence, and antibodies to a cryptic fragment (Phe178-Glu199) of pro-TRH (to label TRH neurons) and alkaline phosphatase-labeled goat anti-rabbit IgG as the second sequence. A rich innervation of the paraventricular nucleus by immunoreactive CRF and SRIF fibers was observed. A large number of CRF and SRIF nerve endings were seen intimate anatomic proximity and often appeared to surround TRH-containing cell bodies. These results strongly suggest that TRH neurons might be regulated by both CRF and SRIF. These interactions might be the neuroanatomical basis for the already observed inhibitory effects of CRF and SRIF on TRH release.
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PMID:Neuroanatomical connections between corticotropin-releasing factor (CRF) and somatostatin (SRIF) nerve endings and thyrotropin-releasing hormone (TRH) neurons in the paraventricular nucleus of rat hypothalamus. 135 8

Acromegaly is characterized by growth hormone (GH) hypersecretion and insulin-like growth factor-I (IGF-I) excess, both of which stimulate osteoblast proliferation. At diagnosis, GH excess has usually been present for years. Furthermore, impaired gonadotropin secretion with hypogonadism is frequent. To date, studies of changes in bone mineral density (BMD) in acromegaly have been limited and the available data inconsistent. To investigate the effects of GH excess on proximal femur and lumbar spine BMD, a case series of 25 patients with acromegaly (8 eugonadal, 17 hypogonadal) documented by high plasma GH and IGF-I concentrations was studied. BMD was measured using dual-photon absorptiometry, hormonal and biochemical measurements, which included GH, IGF-I, serum calcium, phosphate, alkaline phosphatase, 1,25 dihydroxy vitamin D and urinary calcium and hydroxyproline excretion. Seven patients were re-studied after IGF-I was suppressed for six months by the somatostatin analog 201-995 (five patients) or pituitary adenomectomy (two patients). BMD was normal in 22 patients and was decreased at one site each in one eugonadal and two hypogonadal patients. BMD was similar between the eugonadal and hypogonadal groups at all sites. Urinary hydroxyproline excretion was equally increased in both groups. There was no correlation between any of the hormonal or biochemical parameters and the age, sex, race and body mass index matched Z-scores of BMD at any site. Following normalization of IGF-I for 6 mo in seven patients, there was no significant change of BMD. We conclude that proximal femoral and lumbar spine BMD is normal in most patients with active acromegaly, including those who are hypogonad. Successful treatment of acromegaly does not result in major short-term changes in BMD.
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PMID:Bone mineral density of the axial skeleton in acromegaly. 151 33

The effect of acute dopamine receptor antagonist treatment on cellular prosomatostatin mRNA expression was investigated in the adult rat striatum using the technique of non-radioactive in situ hybridization. Adult female Wistar rats were given a single intraperitoneal injection of either raclopride (D2 antagonist), SCH 23390 (D1 antagonist) or the D1 (S) enantiomer SCH 23388. Animals were killed either 1, 3 or 9 h following the single i.p. injection and their brains rapidly removed. Striatal sections were then processed for in situ hybridization using an alkaline phosphatase-labelled oligonucleotide probe complementary to a portion of the rat somatostatin cDNA. Blockade of dopamine D1 and D2 receptors resulted in a significant decrease in the cellular content of prosomatostatin mRNA. However, no change in the number of prosomatostatin mRNA containing striatal cells was observed following any of the treatments at any time point. These findings demonstrate that the cellular content of prosomatostatin mRNA in the adult rat striatum is influenced by selective dopamine D1 and D2 receptor antagonists. Further, these findings are consistent with a functional interaction between dopamine and somatostatin in the rat striatum.
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PMID:Dopaminergic D1 and D2 receptor antagonists decrease prosomatostatin mRNA expression in rat striatum. 168 31

Specific binding sites for the peptide hormone somatostatin have previously been demonstrated in long bones from neonatal rats. In the present study, the distribution of somatostatin receptors during embryonic bone formation has been investigated using the stable radioiodinated somatostatin analogue, SDZ 204-090. Somatostatin receptors in rat long bones were first detectable at the time of invasion of the cartilage model by osteogenic cells. Initially, receptors were detectable throughout the region occupied by osteogenic cells. As bone growth proceeded, however, receptors were restricted to the region of most recent invasion of the hypertrophic cartilage, where osteoid had not yet been deposited. In vivo labelling studies in neonatal rats were carried out to identify the cells bearing somatostatin receptors. Receptors were present in a restricted region of the metaphysis, immediately adjacent to the hypertrophic cartilage. Chondrocytes, osteoclasts, and mature osteoblasts were not labelled by the radioligand. The labelled cells were often apposed to remnants of cartilage matrix and stained positively for the osteoblast marker, alkaline phosphatase. Thus the cells with specific somatostatin-binding sites were probably osteoblast precursor cells. Specific binding was detectable in all endochondral bones examined, including those of the skull, but no specific binding was found in the membrane bones of the skull. These data suggest that somatostatin is involved in the regulation of osteoblast differentiation during endochondral bone formation.
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PMID:Somatostatin receptors are restricted to a subpopulation of osteoblast-like cells during endochondral bone formation. 171 2

We applied Southwestern and Western blotting and gel retardation techniques to investigate the changes that occur in the cyclic adenosine monophosphate (cAMP)-responsive element (CRE) binding (CREB) proteins in rapidly growing, chemically induced 5123tc and 5123D Morris hepatomas. Using the CRE sequences from the c-fos, E2A, and somatostatin gene promoters, we identified in the nuclear proteins from normal unstimulated or proliferating rat liver cells six different protein factors of Mr 34,000, 36,000, 40,000, 47,000, 56,000, and 72,000 capable of binding to the element. The Mr 47,000 protein had the highest specificity for the core CRE, suggesting its importance in cAMP-mediated gene expression. We could not find the Mr 47,000 CREB protein in the 5123tc and 5123D hepatomas. Our efforts to detect this protein in the tumors by (a) using the CRE sequence from different gene promoters, (b) altering the protocol for extracting nuclear proteins, or (c) attempting to restore its DNA-binding property by phosphorylation [with endogenous protein kinase(s), a catalytic subunit of cAMP-dependent protein kinase, and protein kinase C/dephosphorylation (with alkaline phosphatase)] were unsuccessful. The loss of tje Mr 47,000 CREB protein from solid tumors of the Morris hepatoma is likely to be related to the neoplastic properties of the tumor cell rather than to cell growth because the level of this protein remained unchanged during a 6-day period of liver regeneration. The nuclear extract from the Morris hepatoma that did not have the Mr 47,000 CRE-binding factor contained proteins immunologically related to the CREB, c-Jun, and c-Fos proteins. We conclude that the Mr 47,000 factor represents a distinct member of the CRE-binding protein family and that its absence from the hepatomas may lead to aberrant expression of cAMP-inducible genes.
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PMID:Changes in cyclic adenosine monophosphate-responsive element binding proteins in rat hepatomas. 182 83

1. The use of radioactive and biotinylated oligonucleotide probes has been optimized to detect and analyze by in situ hybridization, neurons expressing neuropeptide genes (vasopressin, oxytocin, somatostatin). 2. In situ hybridization was performed on cryostat-cut sections obtained from tissues perfused with 1% formaldehyde. Radioactive probes were labeled by tailing with 35S-dATP and revealed with autoradiography. Biotinylated probes were obtained either by the incorporation of 11-biotin dUTP or by the addition of biotinylated nucleotides to the oligonucleotide during its synthesis. Biotin was revealed with streptavidin alkaline phosphatase and the appropriate substrate. 3. In the adult rat brain, radioactive and biotinylated probes revealed peptidergic neurons. The biotinylated probes provided an optimal cellular and subcellular resolution with a sensitivity similar to that observed with radioactive probes. Staining was selectively restricted to the cytoplasm and to the proximal part of processes. 4. Biotinylated vasopressin probes with 10 biotins added demonstrated magnocellular neurons and parvocellular neurons in the suprachiasmatic nucleus and the bed nucleus stria terminalis. 5. Vasopressin gene expression was studied during ontogeny in the rat fetus and neonate. Vasopressin mRNA was first detectable at gestational day 16 in the supraoptic nucleus in neurons of neuroblastic appearance. An aspect similar to the one present in adult was found at gestational day 19 in magnocellular neurons and at day 3 postnatal in parvocellular neurons. 6. The results confirm that radioactive oligonucleotide probes are efficient tools to investigate neuropeptide gene expression by in situ hybridization and demonstrate that biotinylated oligonucleotides are very efficient and provide a much higher resolution than radioactive probes with a reasonable sensitivity.
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PMID:Topography and ontogeny of the neurons expressing vasopressin, oxytocin, and somatostatin genes in the rat brain: an analysis using radioactive and biotinylated oligonucleotides. 197 Jul 59

The cellular localization of preprosomatostatin mRNA in the rat brain and sensory ganglia has been examined in detail using a newly developed highly sensitive non-radioactive in situ hybridization histochemistry procedure. An alkaline phosphatase labelled anti-sense 30mer oligodeoxynucleotide probe was used for detection of somatostatin mRNA. This probe readily demonstrated somatostatin gene expression throughout the rat CNS with very high contrast and good cellular localization. As a result, we visualized numerous somatostatin mRNA-positive cells in many CNS areas which had previously not been shown to contain a mRNA signal. This method detected a number of somatostatin mRNA-positive cells, in the mitral cell layer of accessory olfactory bulb, the glomerular layer of the main olfactory bulb, the dorsal part of the lateral septum, superficial gray layer of superior colliculus, inferior colliculus, anterior ventral cochlear nucleus, granular layer and Purkinje cell layer of cerebellum, and substantia gelatinosa of medulla and spinal cord, all areas where signal detection using radiolabelled in situ probes has previously been rather difficult. The principle advantages of the present method include the very precise cellular resolution of signal, the rapid reaction time and low background. The sensitivity of the present method seems to be at least equivalent to most immunocytochemical procedures and more sensitive than most isotopic in situ hybridization methods.
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PMID:Distribution of somatostatin mRNA in the rat nervous system as visualized by a novel non-radioactive in situ hybridization histochemistry procedure. 197 30


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