Abstract
The decapeptide Leu-Val-Val-Tyr-Pro-Trp-Thr-Gln-Arg-Phe was isolated in high yield (1.5 nmol/ml) from bronchoalveolar lavage (BAL) fluid from a patient with an adenocarcinoma of the lung. This peptide, termed LVV- hemorphin-7 represents residues 32-41 of the β-chain of hemoglobin and has been shown to be an endogenous ligand for opioid receptors. The N-terminal flanking peptide of LVV-hemorphin-7 [residues (1-31) of hemoglobin β-chain] was also isolated in high yield. Neither peptide was detected in BAL fluid from the tumor-free lung of the same patient or from patients with non- neoplastic inflammatory lung disease. LVV-hemorphin-7 was not identified in BAL fluid from seven additional patients with non-small cell lung cancer, indicating that the formation of the peptide is unlikely to be of any diagnostic significance. However, the ability of LVV-hemorphin-7 to inhibit angiotensin-converting enzyme suggests that its formation may be of pathophysiological significance in the regulation of tumor blood flow in certain patients. (C) 2000 Elsevier Science Inc.
Original language | English |
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Pages (from-to) | 137-142 |
Number of pages | 6 |
Journal | Peptides |
Volume | 21 |
Issue number | 1 |
DOIs | |
Publication status | Published - Jan 2000 |
Externally published | Yes |
Keywords
- Hemoglobin
- Hemorphin
- Non-small cell lung cancer
ASJC Scopus subject areas
- Biochemistry
- Physiology
- Endocrinology
- Cellular and Molecular Neuroscience