Abstract

The lung-associated peptide calcitonin (CT) has been localized by immunocytochemical means to discrete pulmonary endocrine (PE) cells. A long-term cell culture of CT-staining PE cells has been established. The molecular configuration of immunoreactive (iCT) from PE cell extracts was determined by gel chromatography, revealing predominantly large molecular weight forms of iCT. The size distribution characteristics of PE Cell iCT were similar to those of intact hamster lung. In contrast, hamster thyroid extracts contain predominantly 4000 dalton iCT (presumed monomer) and apparent iCT fragments. The culture media of the PE cells were found to contain mainly 4000 dalton iCT. We conclude that although the predominant forms of iCT found within cultured PE cells are distinct from those found within thyroidal C-cells, both iCT producing cells release mainly the monomer into the media. Malignant human bronchial carcinoid cells store predominantly monomeric iCT while secreting large molecular weight forms of iCT. Since the PE cell is the putative precursor cell to neuroendocrine malignancies, the disparity noted in the processing of CT may have significant pathobiological implications.

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