Stachybotrys chartarum alters surfactant-related phospholipid synthesis and CTP : cholinephosphate cytidyltransferase activity in isolated fetal rat type II cells
| Autor: | C. Hastings, J. E. Scott, S. Dakshinamurti, T.G. Rand, James A. Thliveris, A. R. Shaw, H. T. Bergen, G. A. Lombaert, H. H. Mantsch, B. L. Giles |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2004 |
| Předmět: |
Cytidine Diphosphate Choline
Stachybotrys chartarum Cytidylyltransferase Phospholipid Stachybotrys Cell Separation Toxicology Choline Rats Sprague-Dawley Surface-Active Agents chemistry.chemical_compound Cytosol Fetus Pulmonary surfactant Pregnancy Phosphatidylcholine Animals Choline-Phosphate Cytidylyltransferase Cells Cultured Chromatography High Pressure Liquid Phospholipids biology fungi Spores Fungal biology.organism_classification Cytidylyltransferase activity Enzyme assay Rats Biochemistry chemistry Phosphatidylcholines biology.protein Female |
| Popis: | Stachybotry chartarum, a fungal contaminant of water-damaged buildings commonly grows on damp cellulose-containing materials. It produces a complex array of mycotoxins. Their mechanisms of action on the pulmonary system are not entirely clear. Previous studies suggest spore products may depress formation of disaturated phosphatidylcholine (DSPC), the major surface-active component of pulmonary surfactant (PS). If S. chartarum can indeed affect formation of this phospholipid, then mold exposure may be a significant issue for pulmonary function in both mature lung and developing fetal lung. To address this possibility, fetal rat type II cells, the principal source of DSPC, were used to assess effects of S. chartarum extract on formation of DSPC. Isolated fetal rat lung type II cells prelabeled with 3H-choline and incubated with spore extract showed decreased incorporation of 3H-choline into DSPC. The activity of CTP:cholinephosphate cytidylyltransferase (CPCT), the rate-limiting enzyme in phosphatidylcholine synthesis was reduced by approximately 50% by a 1:10 dilution of spore extract. Two different S. chartarum extracts (isolates from S. chartarum (Cleveland) and S. chartarum (Hawaiian)) were used to compare activity of CPCT in the presence of phosphatidylglycerol (PG), a known activator. PG produced an approximate two-fold increase in CPCT activity. The spore isolate from Hawaii did not alter enzyme activity. S. chartarum (Cleveland) eliminated the PG-induced activation of CPCT. These results support previous observations that mold products alter PS metabolism and may pose a risk in developing lung, inhibiting surfactant synthesis. Different isolates of the same species of fungus are not equivalent in terms of potential exposure risks. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|