Title : Interactions of pulmonary surfactant protein SP-A with monolayers of dipalmitoylphosphatidylcholine and cholesterol: roles of SP-A domains.

Pub. Date : 1999 May

PMID : 10224161






11 Functional Relationships(s)
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1 Interactions of pulmonary surfactant protein SP-A with monolayers of dipalmitoylphosphatidylcholine and cholesterol: roles of SP-A domains. 1,2-Dipalmitoylphosphatidylcholine surfactant protein A1 Rattus norvegicus
2 Pulmonary surfactant protein A (SP-A) is an oligomeric glycoprotein that binds dipalmitoylphosphatidylcholine (DPPC). 1,2-Dipalmitoylphosphatidylcholine surfactant protein A1 Rattus norvegicus
3 Pulmonary surfactant protein A (SP-A) is an oligomeric glycoprotein that binds dipalmitoylphosphatidylcholine (DPPC). 1,2-Dipalmitoylphosphatidylcholine surfactant protein A1 Rattus norvegicus
4 Interactions of rat SP-A and recombinant SP-As with pure and binary monolayers of DPPC and cholesterol were studied using a rhomboid surface balance at 37 degrees C. A marked inflection at equilibrium surface tension (23 mN/m) in surface tension-area isotherm of a pure DPPC film was abolished by rat SP-A. 1,2-Dipalmitoylphosphatidylcholine surfactant protein A1 Rattus norvegicus
5 Both rat SP-A and SP-Ahyp decreased surface area reduction required for pure DPPC films to reach near zero surface tension from 30 to 25%. 1,2-Dipalmitoylphosphatidylcholine surfactant protein A1 Rattus norvegicus
6 Both rat SP-A and SP-Ahyp decreased surface area reduction required for pure DPPC films to reach near zero surface tension from 30 to 25%. 1,2-Dipalmitoylphosphatidylcholine surfactant protein A1 Rattus norvegicus
7 SP-Ahyp, E195Q,R197D, mutated in carbohydrate recognition domain (CRD) known to be essential for SP-A-vesicle interactions, conveyed a detrimental effect on DPPC surface activity. 1,2-Dipalmitoylphosphatidylcholine surfactant protein A1 Rattus norvegicus
8 SP-Ahyp, E195Q,R197D, mutated in carbohydrate recognition domain (CRD) known to be essential for SP-A-vesicle interactions, conveyed a detrimental effect on DPPC surface activity. 1,2-Dipalmitoylphosphatidylcholine surfactant protein A1 Rattus norvegicus
9 When mixed films were formed by successive spreading of DPPC/SP-A/cholesterol, rat SP-A, SP-Ahyp, or SP-ADeltaG8-P80 blocked the interaction of cholesterol with DPPC; SP-Ahyp,E195Q,R197D could not impede the interaction; SP-Ahyp,C6S or SP-Ahyp,DeltaN1-A7 only partially blocked the interaction, and cholesterol appeared to stabilize SP-Ahyp,C6S-DPPC association. 1,2-Dipalmitoylphosphatidylcholine surfactant protein A1 Rattus norvegicus
10 When mixed films were formed by successive spreading of DPPC/SP-A/cholesterol, rat SP-A, SP-Ahyp, or SP-ADeltaG8-P80 blocked the interaction of cholesterol with DPPC; SP-Ahyp,E195Q,R197D could not impede the interaction; SP-Ahyp,C6S or SP-Ahyp,DeltaN1-A7 only partially blocked the interaction, and cholesterol appeared to stabilize SP-Ahyp,C6S-DPPC association. 1,2-Dipalmitoylphosphatidylcholine surfactant protein A1 Rattus norvegicus
11 When mixed films were formed by successive spreading of DPPC/SP-A/cholesterol, rat SP-A, SP-Ahyp, or SP-ADeltaG8-P80 blocked the interaction of cholesterol with DPPC; SP-Ahyp,E195Q,R197D could not impede the interaction; SP-Ahyp,C6S or SP-Ahyp,DeltaN1-A7 only partially blocked the interaction, and cholesterol appeared to stabilize SP-Ahyp,C6S-DPPC association. 1,2-Dipalmitoylphosphatidylcholine surfactant protein A1 Rattus norvegicus