Bombesin-like peptides in human small cell carcinoma of the lung |
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| Authors: | K Yoshizaki V de Bock I Takai N S Wang S Solomon |
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| Affiliation: | 1. Departments of Medicine, Biochemistry, Obstetrics and Gynecology and Pathology, McGill University, Canada;2. Endocrine Laboratory, Royal Victoria Hospital, Montreal, Quebec, Canada;1. Discovery Sciences, Innovative Medicines, AstraZeneca R&D, 431 83 Molndal, Sweden;2. Respiratory, Inflammation and Autoimmunity, Innovative Medicines, AstraZeneca R&D, 431 83 Molndal, Sweden;1. Department of Chemistry, National Institute of Technology, Warangal, India;2. Analytical Chemistry Division, IICT, Hyderabad, AP, India;1. Department of Neurology, Karolinska University Hospital, Stockholm, Sweden;2. Department of Neuroscience, Neurology, Uppsala University, Sweden;3. Department of Clinical Neuroscience, Sahlgrenska University Hospital, Gothenburg, Sweden;4. Department of Neurology, Skane University Hospital, Lund, Sweden;5. Department of Neurology and Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden;6. Department of Neurology, Neurocentre Norrlands University Hospital, Umeå, Sweden;7. Department of Neurology, Molde Hospital HNR, Molde, Norway;8. Department of Geriatric Medicine and Rehabilitation, Sundsvall Hospital, Sundsvall, Sweden;9. AbbVie Inc., USA;10. AbbVie AB, Sweden;1. Dept. of Bionanotechnology, Graduate School, South Korea;2. College of Pharmacy, Hanyang University – ERICA, Ansan, 15588, South Korea |
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| Abstract: | The nature of bombesin-like immunoreactive peptides was studied in extracts of small cell carcinoma of the human lung. Three peaks, I, II and III, designated by their increasing retention times, were separated by reversed-phase high performance liquid chromatography (HPLC) with trifluoroacetic acid (TFA) as counter ion. None of the peaks corresponded to bombesin. Peak III was eluted at the same position as porcine gastrin releasing peptide (GRP) but was separated from it in another reversed-phase system using heptafluorobutyric acid (HFBA). Peak II material eluted in the position of bombesin in the HFBA system but not in the TFA system. The elution position of Peak I corresponded to that of the carboxyl terminal fragments of GRP, i.e. GRP18-27 and GRP19-27. This correspondence was observed in each of the reversed-phase and gel filtration systems used. The Peak III peptide was converted to peak I after incubation with trypsin. It was reasoned that this conversion could be one of the steps in the processing of bombesin-like peptides in human small cell carcinoma. |
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