Isolation of the opioid peptide Leu-Val-Val-hemorphin-7 from bronchoalveolar lavage fluid of a patient with non-small cell lung cancer.
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 beta-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 beta-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.
Duethman
D
D
Regulatory Peptide Center, Department of Biomedical Sciences, Creighton University Medical School, Omaha, Nebraska 68178, USA.
Dewan
N
N
Conlon
J M
JM
D000230:Adenocarcinoma / Q000737:chemistry; D014408:Biomarkers, Tumor / Q000302:isolation & purification; D001992:Bronchoalveolar Lavage Fluid / Q000737:chemistry*; D002289:Carcinoma, Non-Small-Cell Lung / Q000737:chemistry*; D002294:Carcinoma, Squamous Cell / Q000737:chemistry; D002851:Chromatography, High Pressure Liquid; D006454:Hemoglobins / Q000302:isolation & purification*; D006801:Humans; D008175:Lung Neoplasms / Q000737:chemistry*; D010446:Peptide Fragments / Q000302:isolation & purification*
D014408:Biomarkers, Tumor; D006454:Hemoglobins; D010446:Peptide Fragments; C074309:LVV-hemorphin-7