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Results for “Pro-Opiomelanocortin”

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At least 793 records · Page 44Linked to original sources
PubMed1986

Immunocytochemical localization of pro gamma MSH, gamma MSH, ACTH and beta endorphin/beta lipotrophin in the fetal sheep pituitary: an ontogenetic study.

An immunocytochemical staining technique was used to localize four fragments [pro gamma MSH, gamma MSH, ACTH and beta endorphin/beta lipotrophin (beta endorphin/beta LPH)] of the proopiomelanocortin molecule in both the adult and fetal sheep pituitary. In the adult sheep anterior pituitary each fragment was localized in cells that were darkly stained, stellate and widely distributed throughout the gland. The same cells, identified in three serial sections, stained with anti-pro gamma MSH, anti-ACTH and anti-beta endorphin/beta LPH. In the fetal sheep anterior pituitary all the proopiomelanocortin derived fragments were present at 38 days gestation. Between about 90 and 130 days of gestation both adult type proopiomelanocortin cells (small, stellate) and uniquely fetal cells (large, columnar) were present. Both adult-type and fetal proopiomelanocortin cells were identified in serial sections of the fetal anterior pituitary, stained with anti-pro gamma MSH, anti-ACTH and anti-beta endorphin/beta LPH. The adult intermediate lobe was immunoreactive with anti-pro gamma MSH and anti-beta endorphin/beta LPH but not with anti-gamma MSH or anti-ACTH. The fetal intermediate lobe was immunoreactive with all four antisera from 60 days gestation.

Adrenocorticotropic Hormone↗
PubMed1986

Regulation of proopiomelanocortin (POMC) mRNA levels in primary pituitary cultures.

The effect of a variety of neurotransmitters and of corticotropin releasing factor (CRF) upon levels of mRNA coding for proopiomelanocortin (POMC) was studied in primary cultures of rat pituitary. Total nucleic acid was extracted from cells, fixed on nitrocellulose and hybridized to a single-stranded alpha 32P-labeled DNA complementary to 150 bases of mouse POMC mRNA. After two days incubation with CRF (10(-8) M), the levels of POMC mRNA in both the anterior (AL) and the intermediate lobe (IL) cells increased by about 100%. A similar increase in the IL cells was seen after incubation with the beta-adrenergic agonist isoprenalin (10(-6) M). In contrast, dopamine (10(-6) M) and GABA (10(-6) M) decreased POMC mRNA levels in the IL cells to about 50% of control levels without affecting POMC mRNA levels in the AL cells. In both pituitary lobes, POMC mRNA was decreased by the Ca2+-channel blocker D600 (10(-5) M) and increased by forskolin (10(-6) M). This indicates that both cAMP and Ca2+ ions play an important role as intracellular messengers for the control of POMC gene expression in normal melanotrope and corticotrope cells.

Animals↗
PubMed1988

Proopiomelanocortin producing cells of spleen: increase after transplantation with opioid-peptide producing Ehrlich ascites tumor cells.

Proopiomelanocortin (POMC) peptides are produced by many cell systems, including a population of macrophage-like cells in mouse spleen. After transplantation of mice with Ehrlich ascites tumor cells, the number of POMC producing spleen cells increase up to 10-fold by 5 to 6 days. The POMC peptides produced by these cells increase even more, as evidenced by radioimmunoassay. Thus, these data indicate both proliferation of splenic POMC cells and increased production of POMC peptides per cell after tumor challenge. Characterization of the peptides by sequence-specific radioimmunoassays and high performance liquid chromatography documents the presence of both ACTH(1-39) and of ACTH(1-14) in these cells. These peptides have multifacetted effects on immune parameters and may exhibit a general antiinflammatory action, partly mediated through inhibition of interleukin 1-stimulated events. The tumor cells themselves do not produce POMC peptides, but display met- and leu-enkephalin immunoreactivity. Also cultured tumor cells display such immunoreactivity, indicating endogenous production of opioid peptides. The opioid peptides of the tumor cells may both affect host immune defenses and play intratumoral autocrine or paracrine roles.

Animals↗
PubMed1987

[Expression in Escherichia coli cells of the nucleotide sequence of DNA coding for the bovine lipotropic hormone].

A cDNA fragment of bovine proopiomelanocortin coding for beta-lipotropic hormone was joined with a promoter and ribosome binding site of B. amyloliquefaciens and cloned in E. coli in pBR 327 plasmid. The level of beta-lipotropin synthesis in bacterial cells transformed by the obtained plasmid was estimated immunochemically. The level of beta-lipotropin production was shown to be 5 mg per liter of bacterial culture.

Amino Acid Sequence↗