Chromatographic characteristics of pro-opiomelanocortin-derived peptides from the rat transplantable tumour 7315a
| Autor: | F. E. Estivariz, M. I. Morano |
|---|---|
| Rok vydání: | 1987 |
| Předmět: |
beta-Lipotropin
endocrine system medicine.medical_specialty Pituitary gland Pro-Opiomelanocortin Endocrinology Diabetes and Metabolism Radioimmunoassay Peptide Biology Peptide hormone chemistry.chemical_compound Endocrinology Adrenocorticotropic Hormone Internal medicine Mole medicine Animals Pituitary Neoplasms Melanocyte-Stimulating Hormones Rats Inbred BUF chemistry.chemical_classification beta-Endorphin Biological activity Rats medicine.anatomical_structure chemistry Sephadex Chromatography Gel Female Endorphins Peptides hormones hormone substitutes and hormone antagonists |
| Zdroj: | Journal of Endocrinology. 112:417-425 |
| ISSN: | 1479-6805 0022-0795 |
| DOI: | 10.1677/joe.0.1120417 |
| Popis: | Adrenocorticotrophin (ACTH) and other proopiomelanocortin (POMC)-derived peptides produced by the 7315a corticomammotrophic tumour have been poorly studied although they elicit profound hypertrophy and hyperplasia in the adrenal glands of recipient Buffalo rats. Tumour extracts were chromatographed on Sephadex G-75 and fractions monitored for POMC-derived peptides by four radioimmunoassay (RIA) systems: ACTH, α-MSH, β-lipotrophin (β-LPH)/endorphin and N-terminal POMC (N-POMC). Chromatograms were compared with those of pars distalis extracts from normal Buffalo rats. All four RIA systems detected immunoreactive material in tumour extracts. ACTH, β-LPH/ endorphin and N-POMC were present in approximately equimolar amounts (ACTH content 93·40 ± 5·27 (s.e.m.) pmol/g) whereas α-MSH was present in smaller amounts (2·83± 0·13 pmol/g). Total peptide content correlated well with tumour weight. ACTH immunoreactivity (IR) in Sephadex chromatograms was located in a large 20 000 mol. wt peak, an ACTH(1–39) peak and a smaller peak coinciding with ACTH(1–24). The latter two peaks showed biological activity consistent with ACTH(1–39) and an ACTH (1–24)-like peptide respectively. The β-LPH/endorphin RIA revealed a peak eluting at approximately 20 000 mol. wt which could not be ascribed to any known POMC peptide containing the endorphin sequence. A β-LPH-like peak, a β-endorphin-like peak and a smaller-sized peak, which contained the bulk of the β-LPH/endorphin IR, were detected; the low molecular weight peak probably representing α- or γ-endorphin. The N-POMC RIA revealed a 20 000 mol. wt peak and a wide peak which could not be completely resolved into two peaks, and which probably represented N-POMC(1–95) and (N-POMC(1–74). No 30 000 mol. wt precursor could be detected with any of the RIA systems employed. Sephadex chromatography of material released from perfused dispersed tumour cells revealed identical IR peaks with all RIA systems used. Glycosylation of tumour POMC peptides was assessed by Concanavalin A–agarose (Con A) chromatography of pooled IR peaks from Sephadex chromatograms. The 20 000 mol. wt (both IR-ACTH and IR-N-POMC) peak, IR-N-POMC(1–95) and IR-N-POMC(1–74) peaks all bound to Con A and were specifically eluted with methylglucoside. Sephadex G-75 and Con A chromatography of pooled pars distalis extracts from normal Buffalo rats were performed. They showed significant differences, compared with tumour extract chromatograms, with all the RIA systems employed. It is concluded that the 7315a tumour processes POMC in a different manner when compared with normal Buffalo rat pars distalis and that it may be used as an interesting model in which to study the processing of POMC. In addition it may shed light on the role of POMC-derived peptides, other than ACTH(1–39), on adrenal growth and function. J. Endocr. (1987) 112, 417–425 |
| Databáze: | OpenAIRE |
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