Human parathyroid hormone fragment stimulates the de novo synthesis of prostaglandin endoperoxide synthase in chick calvaria
The human parathyroid hormone N-terminal fragment [hPTH-(1–34)] increases the conversion of exogenous unsaturated fatty acids to prostaglandins (PGs) in calvarial homogenates. Enzyme activities were completely blocked by indomethacin (5 × 10−7 M), a PG synthase inhibitor, and actinomycin D (5 μM), a...
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| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
Wiley
1993-01-01
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| Series: | Mediators of Inflammation |
| Online Access: | http://dx.doi.org/10.1155/S0962935193000213 |
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| Summary: | The human parathyroid hormone N-terminal fragment [hPTH-(1–34)] increases the conversion of exogenous unsaturated fatty acids to prostaglandins (PGs) in calvarial homogenates. Enzyme activities were completely blocked by indomethacin (5 × 10−7 M), a PG synthase inhibitor, and actinomycin D (5 μM), an inhibitor of transcription, by binding to DNA. In addition, a potent inhibitor of protein synthesis, cycloheximide (10 μM), totally inhibited the stimulating effect of hPTH-(1–34) on prostaglandin endoperoxide synthase (PG synthase, EC 1.14.99.1). The stimulatory effect of hPTH-(1–34) on PG synthase was also reduced by the addition of stannous chloride. However, epidermal growth factor (EGF), platelet-derived activating factor (PDGF), and ionophore A23187 did not show the same stimulating effect as hPTH-(1–34) on PG synthase in calvaria. The results further demonstrated that PG synthase is a membrane-bound enzyme in chick calvaria. In this communication, evidence is presented that hPTH-(1–34) stimulates the de novo synthesis of PG synthase as demonstrated by the increased activity in calvarial homogenates and microsomes. |
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| ISSN: | 0962-9351 1466-1861 |