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

90 primary breast carcinomas and 18 metastases were immunostained for c-erbB-2 protein and neuron specific enolase. 30 tumours were c-erbB-2 negative and NSE positive, 23 tumours were NSE negative and c-erbB-2 positive. 1 tumour expressed focal immunoreactivity for both markers. 54 of the 108 tumours (50%) did not express either marker. Hormone immunoreactivity was present in single cells and in small groups of cells in 18 of the 31 NSE positive tumours. Bombesin, neurotensin and prealbumin were present in 4 cases each, followed by beta-endorphin and VIP in 3 cases each, leu-enkephalin in 2 cases and gastrin, serotonin, substance P, glucagon and somatostatin in 1 case each. None of 10 NSE negative breast carcinomas were comprised of cells expressing immunoreactivity for hormones. By immunoelectron microscopic examination the c-erbB-2 protein was shown to be present on the cell membrane, on smooth areas, microvilli and in coated pits. Immunoreactivity was also expressed in vesicles in cytoplasm and along rough endoplasmic reticulum. The study shows that c-erbB-2 protein expression and neuroendocrine activity are present in different tumour cell populations. This supports the hypothesis that the presence of c-erbB-2 protein, indicating an elevated cellular tyrosine kinase activity with stimulation of growth, intracellular Ca++, and phosphatidylinositol derivates, means that the same cell does not need regulation of the same factors by stimulation of peptide hormone receptors. Thus the production of autocrine and paracrine factors is switched off.
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PMID:C-erbB-2 protein and neuroendocrine expression in breast carcinomas. 167 29

The expression of NSE and hormone immunoreactivity were examined in lymph node metastases from 15 primary breast carcinomas (6 NSE-positive and 9 NSE-negative). NSE immunoreactivity was expressed in metastases in 7 cases. Both the primary tumour and lymph node metastasis(es) were NSE-positive in 3 cases. In 4 cases NSE-negative primary tumours were associated with NSE-positive lymph node metastases. In 2 of the 7 cases with NSE-positive metastases, the metastatic lesions did not express uniform NSE immunoreactivity. Immunoreactivity for hormones (gastrin (1 case), prealbumin (2 cases), ACTH and beta-endorphin (1 case) and somatostatin (1 case] was present in 5 of the 7 NSE-positive lymph node metastatic lesions. In one case only the same hormone (gastrin) was expressed in both the primary tumour and its lymph node metastasis. The present study shows that no relationship exists between primary tumours and the corresponding lymph node metastases with regard to NSE and hormone immunoreactivity.
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PMID:Neuroendocrine activity in metastatic breast carcinomas. 284 16

Inappropriate TSH hypersecretion was diagnosed in a 38-year-old woman (case 1) and in a 38-year-old man (case 2). Both of them had earlier been treated by ablative therapy for hyperthyroidism. The present diagnosis was based on elevated basal serum TSH levels despite elevated serum free thyroid hormone levels. Both of them had exaggerated TSH responses to TRH (peak value 240 mU/l in case 1 and 408 mU/l in case 2). Their albumin and prealbumin levels were normal. The serum TBG level was normal in case 1 but was elevated in case 2. Serum levels of alpha-subunits of TSH, and pituitary CT scans were normal. Despite mild clinical hyperthyroidism, peripheral indices of thyroid hormone action were normal. They had also relatives with apparent resistance to thyroid hormones. In view of the possibility that prolonged pituitary thyrotrophic stimulation is detrimental, various therapeutic approaches to suppress TSH levels were tried. Both T3 and T4 treatments lowered serum TSH levels, but were poorly tolerated. Acute administration of L-dopa or bromocriptine reduced serum TSH levels, but this was not seen during long-term therapy. TRIAC treatment lowered serum TSH levels, and the drug was well tolerated. Serum TSH responses to TRH were not blunted during T3, T4 or TRIAC treatments. Somatostatin also reduced serum TSH levels, but did not potentiate the effect of low dose T3 therapy. Our results suggest that the patients had unbalanced pituitary and peripheral thyroid hormone resistance, predominantly at the pituitary level. Of the drugs studied, TRIAC seemed to be the most suitable therapy.
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PMID:Effects of thyroid hormones (T4,T3), bromocriptine and Triac on inappropriate TSH hypersecretion. 321 42

This study was undertaken, employing the immunoenzyme method, to confirm the presence of retinol-binding protein in human pancreatic islets, and to compare its distribution with that of prealbumin, insulin, glucagon, somatostatin and pancreatic polypeptide. It was found that most islet cells contained retinol-binding protein, although centrally located cells showed stronger reactivity than those in the peripheral region. The distribution of each of the five polypeptides differed from that of retinol-binding protein, indicating that these peptides did not cross-react with anti-retinol-binding protein antibody. Islet cells which contained prealbumin, on the other hand, were mostly classified as A cells. Further studies are necessary to confirm whether the islet cells produce retinol-binding protein or only store it.
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PMID:Immunohistochemical localization of plasma retinol-binding protein and prealbumin in human pancreatic islets. 352 70

Using an indirect immunoperoxidase staining technique we have demonstrated the plasma protein, prealbumin, in the cells of the pancreatic islets of Langerhans. Serial sections stained with antisera to glucagon, insulin and somatostatin revealed that the distribution of the prealbumin stained cells matched that of the glucagon A-cells. Absorption and cross-absorption experiments with prealbumin and glucagon showed that the staining was specific. We also found positive staining for prealbumin in single cells in the mucosa of the gastrointestinal tract, mainly stomach and colon, and kidney tubules.
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PMID:Immunolocalization of prealbumin: distribution in normal human tissue. 389 38