The human parathyroid hormone N-terminal fragment [hPTH-(1-34)] increases the conversion of exogenous unsaturated fatty acids to prostaglandins (PGs) in calvarial homogenates.
1993
Human Parathyroid Hormone Fragment Stimulates Prostaglandin Synthase in Chick Calvaria
Sample size: 20
publication
Evidence: moderate
Author Information
Author(s): Chin-Yuh Yang, Ching-Liang Meng, Patrick Y-K. Wong
Primary Institution: Tri-Service General Hospital, National Defense Medical Center
Hypothesis
Does hPTH-(1-34) stimulate the de novo synthesis of prostaglandin synthase in chick calvaria?
Conclusion
hPTH-(1-34) significantly increases the activity of prostaglandin synthase in chick calvaria.
Supporting Evidence
- hPTH-(1-34) increased PG synthase activity by about three-fold.
- Indomethacin and actinomycin D blocked the effects of hPTH-(1-34).
- PG synthase was found to be a membrane-bound enzyme in chick calvaria.
Takeaway
A hormone from the parathyroid gland helps chick bones make a substance that is important for many body functions.
Methodology
Chick calvariae were preincubated and then treated with hPTH-(1-34) to measure prostaglandin synthase activity.
Limitations
The study is limited to chick calvaria and may not apply to other species.
Participant Demographics
Chick embryos (17 days old)
Statistical Information
P-Value
p<0.05
Statistical Significance
p<0.05
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