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1.
Metabolism ; 41(1): 11-6, 1992 Jan.
Article in English | MEDLINE | ID: mdl-1538639

ABSTRACT

Several peptide hormones and growth factors have been found in human milk, and we present here the results of measurements of parathyroid hormone-related peptide (PTHrP). A radioimmunoassay (RIA) using a polyclonal antiserum against the mid-region of the molecule has been developed. In milk collected during the first 6 days after parturition, the PTHrP concentrations showed large interindividual variations ranging from 0.3 to 13.7 nmol-Eq/L (0.5 to 24.4 ng-Eq/mL) (n = 67) and increased between days 3 and five postpartum. PTHrP also increased during the first 4 collecting days when measured in milk from the same mother during a prolonged period. On fast-protein liquid chromatography (FPLC), the bulk of PTHrP eluted with a molecular weight of approximately 10 to 12 kd after treatment with urea. After mid-molecule immunoaffinity extraction of PTHrP from milk, higher levels were obtained by the mid-molecule RIA than by an aminoterminal assay, indicating that all fragments did not contain the aminoterminal. Parts of immunoextracted milk PTHrP stimulated cyclic adenosine monophosphate (cAMP) production in rat osteosarcoma cell line, UMR-106. In conclusion, we have found PTHrP-like immunoreactivity in human milk using a mid-region RIA. Parts of the immunoextracts also contained the aminoterminal and possessed PTH-like bioactivity. Whether PTHrP in human milk plays a physiological role in the maternal breast or in the newborn gastrointestinal tract is unknown, but the present observations demonstrate that a portion of the PTHrP is at least potentially biologically active.


Subject(s)
Milk, Human/chemistry , Parathyroid Hormone/analysis , Proteins/analysis , Biological Assay , Female , Humans , Molecular Weight , Parathyroid Hormone-Related Protein , Pregnancy , Proteins/immunology , Radioimmunoassay
2.
FEBS Lett ; 146(1): 73-8, 1982 Sep 06.
Article in English | MEDLINE | ID: mdl-7140976

ABSTRACT

A 37 amino acid-peptide has been isolated from porcine jejuno-ileum on the basis of its glucagon-like activity in liver (interaction with glucagon-binding sites and activation of adenylate cyclase) using gel filtration, ion-exchange and high-performance liquid chromatography. Depending on the criteria chosen, this peptide is referred to as either 'bioactive enteroglucagon' (activity in liver), 'oxyntomodulin' (specific action in gastric oxyntic glands) or 'glucagon-37' (chemical structure).


Subject(s)
Gastrointestinal Hormones/isolation & purification , Glucagon-Like Peptides/isolation & purification , Muscle, Smooth/analysis , Adenylyl Cyclases/metabolism , Animals , Cell Membrane/metabolism , Chemical Phenomena , Chemistry , Ileum/analysis , In Vitro Techniques , Jejunum/analysis , Liver/metabolism , Oxyntomodulin , Rats , Swine
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