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J Appl Physiol 76: 657-662, 1994;
8750-7587/94 $5.00
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Journal of Applied Physiology, Vol 76, Issue 2 657-662, Copyright © 1994 by American Physiological Society

ARTICLES

Dependence of surfactant function on extracellular pH: mechanisms and modifications

I. Y. Haddad, B. A. Holm, L. Hlavaty and S. Matalon
Department of Pediatrics, University of Alabama at Birmingham 35294.

We investigated alterations in pH on the surface properties of natural lung surfactant and the calf lung surfactant extract (CLSE), suspended in 10 mM N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid, using a pulsating bubble surfactometer. Increasing the pH value of the medium to > 7.4 decreased the ability of CLSE, but not of natural lung surfactant mixtures (2 mg phospholipid/ml), to achieve a low minimum surface tension during dynamic compression and enhanced their sensitivity to albumin inactivation. These detrimental effects on surface tension were reversed by addition of surfactant protein A (SP-A; 3% by weight) or by increasing the lipid concentration to 4 mg/ml. SP-A-induced lipid aggregation at pH 10 was not different than at pH 7.4. Alkalinization impaired the ability of CLSE to restore normal lung mechanics in excised surfactant-deficient rats lungs. These results indicate that cooperation between SP-A and the hydrophobic surfactant proteins has an important role in achieving low minimum surface tension at pH > or = 7.6.


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