"Cultured"

Characterization of the molecular forms of ANP released by perfused neonatal rat heart.

Although cultures of neonatal rat atria and ventricles have been widely used to study ANP biosynthesis and secretion, little is known regarding the circulating form of ANP in neonatal animals. To begin to address this issue, we have developed a …

The characterization of the ascorbic acid-mediated alpha-amidation of alpha-melanotropin in cultured intermediate pituitary lobe cells.

Previous studies have shown that cultured rat intermediate pituitary lobe cells lose the ability to form ACTH-(1-13)NH2-related molecules (alpha MSH) and instead produce ACTH-(1-14)-related peptides. In vitro studies have shown that peptidylglycine …

Molecular forms of immunoactive atrial natriuretic peptide released from cultured rat atrial myocytes.

Primary cultures of atrial myocytes were prepared from newborn rats and maintained for 8 days in complete serum-free medium. The culture content of immunoactive atrial natriuretic peptide (ANP) increased from 10 to 25 ng/culture during this time. The …

The alpha-amidation of alpha-melanocyte stimulating hormone in intermediate pituitary requires ascorbic acid.

Rat intermediate pituitary cells in primary culture display a time-dependent loss of the ability to produce COOH-terminally alpha-amidated alpha MSH (Glembotski, C.C., Eipper, B.A., and Mains, R.E. (1983) J. Biol. Chem. 258, 7299-7304). Instead of …

Adrenocorticotropin(1-14)OH-related molecules in primary cultures of rat intermediate pituitary cells. Identification and role in the biosynthesis of alpha-melanotropin.

The structures of the altered alpha-melanotropin (alpha MSH or alpha-N-acetyl-ACTH(1-13)NH2)-related molecules produced by cultured rat intermediate pituitary cells were investigated. Peptide analyses demonstrated that the alpha MSH-related molecules …

Selective loss of alpha-melanotropin-amidating activity in primary cultures of rat intermediate pituitary cells.

The production of alpha-melanotropin (alpha-N-acetyl-ACTH(1-13)NH2 (alpha MSH) in rat intermediate pituitary was investigated using reverse phase high performance liquid chromatography, immunoassays, and biosynthetic labeling. Extracts of rat …

Characterization of the peptide acetyltransferase activity in bovine and rat intermediate pituitaries responsible for the acetylation of beta-endorphin and alpha-melanotropin.

Subcellular fractionation studies on the post-translational processing of pro-adrenocorticotropic hormone/endorphin in rat intermediate pituitary.

The subcellular localization of the post-translational processing steps which occur in the conversion of pro-adrenocorticotropic hormone (ACTH)/endorphin into beta-endorphin-sized molecules in rat intermediate pituitary has been studied. Primary cell …