Expression of the Na+/H+ and Cl-/HCO-3 exchanger isoforms in proximal and distal human airways

• Published in: American journal of physiology. Lung cellular and molecular physiology Vol. 276; no. 6; pp. 971 - L978
• Main Authors: Dudeja, P. K, Hafez, N, Tyagi, S, Gailey, C. A, Toofanfard, M, Alrefai, W. A, Nazir, T. M, Ramaswamy, K, Al-Bazzaz, F. J
• Format: Journal Article
• Language: English
• Published: United States 01.06.1999
• Subjects: Adult; Antiporters - genetics; Antiporters - metabolism; Bronchi - cytology; Bronchi - metabolism; Chloride-Bicarbonate Antiporters; Epithelial Cells - metabolism; Female; Humans; Male; Middle Aged; Nucleic Acid Hybridization; Protein Isoforms - metabolism; Ribonucleases; RNA, Messenger - metabolism; Sodium-Hydrogen Exchangers - genetics; Sodium-Hydrogen Exchangers - metabolism; Tissue Distribution - physiology; Trachea - cytology; Trachea - metabolism
• ISSN: 1040-0605; 0002-9513; 1522-1504; 2163-5773
• DOI: 10.1152/ajplung.1999.276.6.L971

Department of Medicine, University of Illinois at Chicago and Westside Veterans Affairs Medical Center, Chicago, Illinois 60612 Recent studies have indicated the presence of Na + /H + and Cl /HCO 3 exchange activities in lung alveolar and tracheal tissues of various species. To date, the identity of the Na + /H + (NHE) and Cl /HCO 3 (AE) exchanger isoforms and their regional distribution in human airways are not known. Molecular species of the NHE and AE gene families and their relative abundance in the human airway regions were assessed utilizing RT-PCR and the RNase protection assay, respectively. Organ donor lung epithelia from various bronchial regions (small, medium, and large bronchi and trachea) were harvested for RNA extraction. Gene-specific primers for the human NHE and AE isoforms were utilized for RT-PCR. Our results demonstrated that NHE1, AE2, and brain AE3 isoforms were expressed in all regions of the human airways, whereas NHE2, NHE3, AE1, and cardiac AE3 were not detected. RNase protection studies for NHE1 and AE2, utilizing glyceraldehyde-3-phosphate dehydrogenase as an internal standard, demonstrated that there were regional differences in the NHE1 mRNA levels in human airways. In contrast, the levels of AE2 mRNA remained unchanged. Differential expression of these isoforms in the human airways may have functional significance related to the airway absorption and secretion of electrolytes. human lung; anion exchangers; cation exchangers; reverse transcription-polymerase chain reaction; ribonuclease protection