In lab tests, the thymosin beta‑4 (1-4) fragment caused incomplete competitive inhibition of calmodulin-stimulated hypothalamic phosphodiesterase, with an inhibition constant of 600 nM.
In plain wordsIn lab tests, the short thymosin beta‑4 fragment partly blocked a brain enzyme that calmodulin switches on. This was not full-length thymosin beta‑4.
- Peptide
- Thymosin beta-4 (human)
- Outcome
- DecreaseInhibition of calmodulin-stimulated phosphodiesterase
- Study
n: not reported in source
hypothalamic calmodulin-dependent cAMP phosphodiesterase- Outcome group
- Receptor activity and mechanism · Pharmacology
Measurements
- Inhibition constant (Ki)
- 600 nM
- calmodulin-stimulated phosphodiesterase
Source sentences
In the course of the study of the interrelationship between the immune and neuroendocrine systems we have found that the tetrapeptide caused incomplete competitive inhibition of hypothalamic calmodulin (CaM)-dependent phosphodiesterase (PDE) stimulated by CaM.
2 context sentences(design, population, supporting numbers)
The value of the inhibition constant (Ki) amounted to 600 nM.
It was previously shown that the N-fragment (1-4) of thymosin beta 4 (Ac-Ser-Asp-Lys-Pro-OH) inhibits in vivo the entry of cell populations into S-phase.
In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin beta-4 (human).