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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| Format: | Article |
| Language: | English |
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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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| _version_ | 1832545918488936448 |
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| author | Chin-Yuh Yang Ching-Liang Meng Patrick Y- K. Wong |
| author_facet | Chin-Yuh Yang Ching-Liang Meng Patrick Y- K. Wong |
| author_sort | Chin-Yuh Yang |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-5935c83ee3a64342b344c6eda8e89d78 |
| institution | Kabale University |
| issn | 0962-9351 1466-1861 |
| language | English |
| publishDate | 1993-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Mediators of Inflammation |
| spelling | doaj-art-5935c83ee3a64342b344c6eda8e89d782025-02-03T07:24:19ZengWileyMediators of Inflammation0962-93511466-18611993-01-012214314710.1155/S0962935193000213Human parathyroid hormone fragment stimulates the de novo synthesis of prostaglandin endoperoxide synthase in chick calvariaChin-Yuh Yang0Ching-Liang Meng1Patrick Y- K. Wong2Department of Dentistry, Tri-Service General Hospital, National Defense Medical Center, 18 Sy-Yuan Road, Taipei 100, TaiwanDepartment of Dentistry, Tri-Service General Hospital, National Defense Medical Center, 18 Sy-Yuan Road, Taipei 100, TaiwanDepartment of Dentistry, Tri-Service General Hospital, National Defense Medical Center, 18 Sy-Yuan Road, Taipei 100, TaiwanThe 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.http://dx.doi.org/10.1155/S0962935193000213 |
| spellingShingle | Chin-Yuh Yang Ching-Liang Meng Patrick Y- K. Wong Human parathyroid hormone fragment stimulates the de novo synthesis of prostaglandin endoperoxide synthase in chick calvaria Mediators of Inflammation |
| title | Human parathyroid hormone fragment stimulates the de novo synthesis of prostaglandin endoperoxide synthase in chick calvaria |
| title_full | Human parathyroid hormone fragment stimulates the de novo synthesis of prostaglandin endoperoxide synthase in chick calvaria |
| title_fullStr | Human parathyroid hormone fragment stimulates the de novo synthesis of prostaglandin endoperoxide synthase in chick calvaria |
| title_full_unstemmed | Human parathyroid hormone fragment stimulates the de novo synthesis of prostaglandin endoperoxide synthase in chick calvaria |
| title_short | Human parathyroid hormone fragment stimulates the de novo synthesis of prostaglandin endoperoxide synthase in chick calvaria |
| title_sort | human parathyroid hormone fragment stimulates the de novo synthesis of prostaglandin endoperoxide synthase in chick calvaria |
| url | http://dx.doi.org/10.1155/S0962935193000213 |
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