G. Lema et G. Enhorning, SURFACE-PROPERTIES AFTER A SIMULATED PLA(2) HYDROLYSIS OF PULMONARY SURFACTANTS MAIN COMPONENT, DPPC, Biochimica et biophysica acta, L. Lipids and lipid metabolism, 1345(1), 1997, pp. 86-92
The inflammation, so conspicuous in cases of respiratory distress. pne
umonia, and asthma, is associated with an airway invasion of plasma pr
oteins and a release into the airway lumen of phospholipase A, (PLA,),
This enzyme catalyzes hydrolysis of surfactant phospholipids, the mos
t abundant and important of which is dipalmitoylphosphatidylcholine (D
PPC). Its hydrolysis yields equimolar proportions of lysophosphatidylc
holine and palmitic acid (LPC/PA), Exact quantification of DPPC hydrol
ysis is complicated. Consequently. it was decided to simulate hydrolys
is whereby DPPC (3 mg/ml) was gradually replaced with LPC/PA (3 mg/ml)
, yielding seven different grades of simulated hydrolysis: 0, 17, 33,
50, 67, 83, and 100%. Surface properties of the seven mixtures were ex
amined with various concentrations of albumin added. The Bubble Surfac
tometer was used to study the surfactant film that is given time to de
velop at a spherical air-liquid interface. A Capillary Surfactometer w
as used to evaluate surface properties required for airway patency. It
was found, using both of these instruments that the surface activity
improved as the simulated hydrolysis of DPPC to LPC/PA increased towar
d 100%, where the activity was maximal. With the Bubble Surfactometer,
surface activity of LPC/PA, 3 mg/ml, improved as albumin concentratio
n increased, and when it reached 15 mg/ml, surface tension became 0 mN
/m after only 2 min. With the Capillary Surfactometer, requiring a muc
h faster film adsorption, albumin had an opposite effect. LPC/PA alone
maintained patency 100% of the time studied, while even a minimal add
ition of albumin inhibited surfactant function. (C) 1997 Elsevier Scie
nce B.V.