Title : Liver carboxylesterase cleaves surfactant protein (SP-) B and promotes surfactant subtype conversion - Ruppert_2006_Biochem.Biophys.Res.Commun_348_1449 |
Author(s) : Ruppert C , Bagheri A , Markart P , Schmidt R , Seeger W , Gunther A |
Ref : Biochemical & Biophysical Research Communications , 348 :1449 , 2006 |
Abstract :
Conversion of the biophysically active large surfactant aggregate subtype of alveolar surfactant into the less surface active small surfactant aggregates occurs in vitro and in vivo, possibly in dependency of a carboxylesterase, entitled surfactant convertase. The substrate has yet not been safely identified. Utilizing the in vitro cycling assay we investigated conversion of an organic rabbit lavage extract reconstituted with SP-A. Porcine liver carboxylesterase, which is closely related to surfactant convertase, induced subtype conversion to a similar degree as compared with native lavage fluid containing endogenous convertase. In addition, we asked for cleavage products of SP-B and identified a approximately 12 kDa band upon cycling with liver carboxylesterase, having the same N-terminus as mature SP-B. A band of same molecular weight was found in native lavage fluid after in vitro conversion mediated by the endogenous convertase. We conclude that SP-B plays a pivotal role during subtype conversion and represents the substrate for surfactant convertase. |
PubMedSearch : Ruppert_2006_Biochem.Biophys.Res.Commun_348_1449 |
PubMedID: 16919595 |
Ruppert C, Bagheri A, Markart P, Schmidt R, Seeger W, Gunther A (2006)
Liver carboxylesterase cleaves surfactant protein (SP-) B and promotes surfactant subtype conversion
Biochemical & Biophysical Research Communications
348 :1449
Ruppert C, Bagheri A, Markart P, Schmidt R, Seeger W, Gunther A (2006)
Biochemical & Biophysical Research Communications
348 :1449