| Purification of calcitonin-like peptides from rat brain and pituitary. | |
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MedLine Citation:
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PMID: 9492029 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Accumulating evidence supports the existence of nonthyroidal calcitonin (CT)-like peptides, more similar to fish CTs, which may act as endogenous regulators of CT receptors in brain and other tissues. In this study, we have carried out large-scale extractions from Sprague-Dawley rat brain diencephalon and pituitary, and purified a novel, biologically active, CT-like peptide from pituitary. Monitoring of the calcitonin-like activity of the peptides from rat brain and pituitary required different detection systems. While the brain CT cross-reacted with C-terminally directed salmon CT-specific antisera, the pituitary CT did not. However, the pituitary CT was biologically active, exhibiting specific interaction with CT receptors to activate adenylate cyclase. Conventional chromatographic techniques were employed to purify the CT-like peptides. Although the brain CT was not purified to homogeneity, size exclusion chromatography revealed the presence of multiple molecular weight forms of immunoreactive CT. Of these, only the lowest molecular weight form was biologically active. Purification from the pituitary resulted in the isolation of a biologically active peptide with a mass of 3267 Da. This mass differs from the mass of both salmon and thyroid-derived rat CT. Initial amino acid sequencing of the pituitary CT indicated that it was N-terminally blocked. Following aminopeptidase digestion, a unique six amino acid sequence, EKSQSP, was identified. Elucidation of the amino acid composition provided supporting evidence that the peptide was novel and was consistent with a full length peptide of approximately 30 amino acids. These data support the existence of novel, nonthyroidal, CTs which are potential regulators of CT receptor-mediated functions. |
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Authors:
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J M Hilton; K I Mitchelhill; G Pozvek; M Dowton; M Quiza; P M Sexton |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Endocrinology Volume: 139 ISSN: 0013-7227 ISO Abbreviation: Endocrinology Publication Date: 1998 Mar |
Date Detail:
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Created Date: 1998-03-12 Completed Date: 1998-03-12 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0375040 Medline TA: Endocrinology Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 982-92 Citation Subset: AIM; IM |
Affiliation:
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John Holt Protein Structure Laboratory, St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Calcitonin / chemistry, isolation & purification* Cells, Cultured Diencephalon / chemistry* Humans Molecular Sequence Data Pituitary Gland / chemistry* Rats Rats, Sprague-Dawley Receptors, Calcitonin / analysis |
| Chemical | |
Reg. No./Substance:
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0/Receptors, Calcitonin; 9007-12-9/Calcitonin |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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