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Identification of a putative surfactant convertase in rat lung as a secreted serine carboxylesterase

Identification of a putative surfactant convertase in rat lung as a secreted serine carboxylesterase
Identification of a putative surfactant convertase in rat lung as a secreted serine carboxylesterase
In the alveolar lumen, pulmonary surfactant converts from the contents of secreted lamellar bodies to tubular myelin to apoprotein-depleted vesicles during respiration. Using an in vitro system, researchers have reported that the conversion of tubular myelin to vesicles is blocked by inhibitors of serine hydrolase activity and have tentatively ascribed "convertase" activity to a diisopropyl fluorophosphate (DFP)-binding protein in mouse bronchoalveolar lavage (BAL). We purified and sequenced the homologous enzyme from rat BAL fluid. Amino acid sequence from the amino terminus and an internal cyanogen bromide peptide of the purified rat DFP-binding protein perfectly match the sequence of the carboxylesterase ES-2. Although ES-2 was initially cloned from liver, we found a 1.8-kilobase mRNA for ES-2 in decreasing relative abundance in rat liver, kidney, and lung but not in heart or spleen. Although further studies are required to establish the identity between "convertase" and ES-2 or a homologous member of the carboxylesterase family, our results raise the possibility that a protein with esterase/lipase activity plays a role in extracellular surfactant metabolism.
1040-0605
L404-L410
Barr, Frederick
3672efce-3e9f-4e56-bcfc-6c90e82f6558
Clark, Howard W.
70550b6d-3bd7-47c6-8c02-4f43f37d5213
Hawgood, Samuel
5e406d87-8445-448a-a068-b693d061d6dd
Barr, Frederick
3672efce-3e9f-4e56-bcfc-6c90e82f6558
Clark, Howard W.
70550b6d-3bd7-47c6-8c02-4f43f37d5213
Hawgood, Samuel
5e406d87-8445-448a-a068-b693d061d6dd

Barr, Frederick, Clark, Howard W. and Hawgood, Samuel (1998) Identification of a putative surfactant convertase in rat lung as a secreted serine carboxylesterase. American Journal of Physiology. Lung Cellular and Molecular Physiology, 274 (3), part 1, L404-L410.

Record type: Article

Abstract

In the alveolar lumen, pulmonary surfactant converts from the contents of secreted lamellar bodies to tubular myelin to apoprotein-depleted vesicles during respiration. Using an in vitro system, researchers have reported that the conversion of tubular myelin to vesicles is blocked by inhibitors of serine hydrolase activity and have tentatively ascribed "convertase" activity to a diisopropyl fluorophosphate (DFP)-binding protein in mouse bronchoalveolar lavage (BAL). We purified and sequenced the homologous enzyme from rat BAL fluid. Amino acid sequence from the amino terminus and an internal cyanogen bromide peptide of the purified rat DFP-binding protein perfectly match the sequence of the carboxylesterase ES-2. Although ES-2 was initially cloned from liver, we found a 1.8-kilobase mRNA for ES-2 in decreasing relative abundance in rat liver, kidney, and lung but not in heart or spleen. Although further studies are required to establish the identity between "convertase" and ES-2 or a homologous member of the carboxylesterase family, our results raise the possibility that a protein with esterase/lipase activity plays a role in extracellular surfactant metabolism.

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Published date: March 1998

Identifiers

Local EPrints ID: 158577
URI: https://eprints.soton.ac.uk/id/eprint/158577
ISSN: 1040-0605
PURE UUID: 3da61155-bbe4-4e84-b388-a29bcc4954ea

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Date deposited: 14 Jul 2010 08:37
Last modified: 18 Jul 2017 12:38

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