Is dipalmitoylphosphatidylcholine a substrate for convertase?

Rajiv Dhand, Jared Young, Andelle Teng, Subbiah Krishnasamy, Nicholas J. Gross

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Convertase has homology with carboxylesterases, but its substrate(s) is not known. Accordingly, we determined whether dipalmitoylphosphatidylcholine (DPPC), the major phospholipid in surfactant, was a substrate for convertase. We measured [3H]choline release during cycling of the heavy subtype containing [3H]choline-labeled DPPC with convertase, phospholipases A2, B, C and D, liver esterase, and elastase. Cycling with liver esterase or peanut or cabbage phospholipase D produced the characteristic profile of heavy and light peaks observed on cycling with convertase. In contrast, phospholipases A2, B, and C and yeast phospholipase D produced a broad band of radioactivity across the gradient without distinct peaks. [3H]choline was released when natural surfactant containing [3H]choline-labeled DPPC was cycled with yeast phospholipase D but not with convertase or peanut and cabbage phospholipases D. Similarly, yeast phospholipase D hydrolyzed [3H]choline from [3H]choline-labeled DPPC after incubation in vitro, whereas convertase, liver esterase, or peanut and cabbage phospholipases D did not. Thus convertase, liver esterase, and plant phospholipases D did not hydrolyze choline form DPPC either on cycling or during incubation with enzyme in vitro. In conclusion, conversion of heavy to light subtype of surfactant by convertase may require a phospholipase D type hydrolysis of phospholipids, but the substrate in this reaction is not DPPC.

Original languageEnglish (US)
JournalAmerican Journal of Physiology - Lung Cellular and Molecular Physiology
Volume278
Issue number1 22-1
StatePublished - Jan 1 2000
Externally publishedYes

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1,2-Dipalmitoylphosphatidylcholine
Phospholipase D
Choline
Esterases
Brassica
Lysophospholipase
Yeasts
Liver
Phospholipases A2
Surface-Active Agents
Phospholipids
Carboxylic Ester Hydrolases
Light
Pancreatic Elastase
Type C Phospholipases
Radioactivity
Hydrolysis

All Science Journal Classification (ASJC) codes

  • Physiology
  • Pulmonary and Respiratory Medicine
  • Cell Biology
  • Physiology (medical)

Cite this

Is dipalmitoylphosphatidylcholine a substrate for convertase? / Dhand, Rajiv; Young, Jared; Teng, Andelle; Krishnasamy, Subbiah; Gross, Nicholas J.

In: American Journal of Physiology - Lung Cellular and Molecular Physiology, Vol. 278, No. 1 22-1, 01.01.2000.

Research output: Contribution to journalArticle

Dhand, Rajiv ; Young, Jared ; Teng, Andelle ; Krishnasamy, Subbiah ; Gross, Nicholas J. / Is dipalmitoylphosphatidylcholine a substrate for convertase?. In: American Journal of Physiology - Lung Cellular and Molecular Physiology. 2000 ; Vol. 278, No. 1 22-1.
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