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Ovine anterior pituitary proopiomelanocortin gene expression is not increased by ACTH secretagogues in vitro. 1993

N Levin, and C Wallace, and N Bengani, and M Blum, and P Farnworth, and A I Smith, and J L Roberts
Arthur M. Fishberg Research Center in Neurobiology, Mount Sinai School of Medicine, New York, New York 10029.

Recent reports have demonstrated that the secretion of ACTH from sheep anterior pituitary primary cultures is markedly stimulated by arginine vasopressin (AVP) but not by CRF, and that AVP-stimulated ACTH secretion is potentiated by CRF. It has also been reported that AVP increases total ACTH content (secreted plus intracellular ACTH), suggesting that AVP stimulates POMC biosynthesis in the ovine anterior pituitary. These observations differ from the rat, in which CRF is the most potent of the ACTH-releasing factors and the only ACTH secretagogue which stimulates POMC gene expression and biosynthesis. The second messenger pathways which mediate CRF- and AVP-stimulated ACTH release (protein kinase A and protein kinase C, respectively) are the same in sheep and rat corticotrophs. The present studies were undertaken to determine if ovine POMC gene expression, unlike the rat POMC gene, is stimulated by AVP via the protein kinase C pathway. A 295 base pair portion of the ovine POMC gene was isolated using polymerase chain reaction and sequenced. Ovine POMC messenger RNA (mRNA) levels were quantitated using this partial complementary DNA clone in a solution hybridization/nuclease protection assay with cytoplasmic RNA from sheep anterior pituitary primary cultures which had been treated with various combinations of ACTH secretagogues or with glucocorticoids for 18 h. Treatment with AVP, alone or with CRF, greatly increased total and secreted ACTH levels; however, the amount of POMC mRNA in these cells was not significantly increased. Treatments which stimulated secretion to a lesser extent and did not alter total ACTH levels (CRF alone, cAMP alone, or with phorbol ester) were associated with a decrease in POMC mRNA levels relative to untreated cells. Glucocorticoid treatment decreased both total ACTH and POMC mRNA levels. Taken together, the data demonstrate a lack of secretagogue-induced stimulation of POMC mRNA levels concomitant with increased total ACTH levels, an unexpected result given the close association between secretion of POMC-derived peptides and POMC gene expression in other mammalian corticotroph systems.

UI MeSH Term Description Entries
D008297 Male Males
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010903 Pituitary Gland, Anterior The anterior glandular lobe of the pituitary gland, also known as the adenohypophysis. It secretes the ADENOHYPOPHYSEAL HORMONES that regulate vital functions such as GROWTH; METABOLISM; and REPRODUCTION. Adenohypophysis,Anterior Lobe of Pituitary,Anterior Pituitary Gland,Lobus Anterior,Pars Distalis of Pituitary,Adenohypophyses,Anterior Pituitary Glands,Anterior, Lobus,Anteriors, Lobus,Lobus Anteriors,Pituitary Anterior Lobe,Pituitary Glands, Anterior,Pituitary Pars Distalis
D011333 Pro-Opiomelanocortin A 30-kDa protein synthesized primarily in the ANTERIOR PITUITARY GLAND and the HYPOTHALAMUS. It is also found in the skin and other peripheral tissues. Depending on species and tissues, POMC is cleaved by PROHORMONE CONVERTASES yielding various active peptides including ACTH; BETA-LIPOTROPIN; ENDORPHINS; MELANOCYTE-STIMULATING HORMONES; and others (GAMMA-LPH; CORTICOTROPIN-LIKE INTERMEDIATE LOBE PEPTIDE; N-terminal peptide of POMC or NPP). POMC,Pro-Opiocortin,ACTH-Endorphin Precursor,ACTH-beta-Lipotropin Precursor,Corticotropin-beta-Lipotropin Precursor,Endorphin-ACTH Precursor,Opiocortin,Pre-POMC,Pre-pro-opiocortin,Preproopiomelanocortin,Pro-ACTH-Endorphin,Pro-Opio-Melanocortin,Proopiocortin,Proopiomelanocortin,ACTH Endorphin Precursor,ACTH beta Lipotropin Precursor,Corticotropin beta Lipotropin Precursor,Endorphin ACTH Precursor,Pre POMC,Pre pro opiocortin,Pro ACTH Endorphin,Pro Opio Melanocortin,Pro Opiocortin,Pro Opiomelanocortin
D002478 Cells, Cultured Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others. Cultured Cells,Cell, Cultured,Cultured Cell
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D003346 Corticotropin-Releasing Hormone A peptide of about 41 amino acids that stimulates the release of ADRENOCORTICOTROPIC HORMONE. CRH is synthesized by neurons in the PARAVENTRICULAR NUCLEUS of the HYPOTHALAMUS. After being released into the pituitary portal circulation, CRH stimulates the release of ACTH from the PITUITARY GLAND. CRH can also be synthesized in other tissues, such as PLACENTA; ADRENAL MEDULLA; and TESTIS. ACTH-Releasing Hormone,CRF-41,Corticotropin-Releasing Factor,Corticotropin-Releasing Hormone-41,ACTH-Releasing Factor,CRF (ACTH),Corticoliberin,Corticotropin-Releasing Factor-41,ACTH Releasing Factor,ACTH Releasing Hormone,Corticotropin Releasing Factor,Corticotropin Releasing Factor 41,Corticotropin Releasing Hormone,Corticotropin Releasing Hormone 41
D004247 DNA A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine). DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D000324 Adrenocorticotropic Hormone An anterior pituitary hormone that stimulates the ADRENAL CORTEX and its production of CORTICOSTEROIDS. ACTH is a 39-amino acid polypeptide of which the N-terminal 24-amino acid segment is identical in all species and contains the adrenocorticotrophic activity. Upon further tissue-specific processing, ACTH can yield ALPHA-MSH and corticotrophin-like intermediate lobe peptide (CLIP). ACTH,Adrenocorticotropin,Corticotropin,1-39 ACTH,ACTH (1-39),Adrenocorticotrophic Hormone,Corticotrophin,Corticotrophin (1-39),Corticotropin (1-39),Hormone, Adrenocorticotrophic,Hormone, Adrenocorticotropic
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein

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