Impact of various glycosaminoglycans upon cAMP-dependent protein kinase
✍ Scribed by Joachim Dittmann; Carsten Krischek; Günther Harisch
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 167 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0263-6484
No coin nor oath required. For personal study only.
✦ Synopsis
The physiological eects of the second messenger cAMP are displayed by cAMP-dependent protein kinase-medicated phosphorylation of speci®c target proteins which in turn control diverse cellular functions. We have determined this enzyme substrate phosphorylation in the presence of various glycosaminoglycans using a cAMP-dependent protein kinase isolated from rat liver. The results indicate that sulfated and unsulfated polysaccharides are able to inhibit phosphorylation of histone type IIa catalysed by cAMP-dependent protein kinase. Based on their impact upon substrate phosphorylation, glycosaminoglycans can be divided into three groups: group I with the highest inhibitory eect: dermatan sulfate and heparan sulfate; group II: chondroitin 4-sulfate and group III with the lowest inhibitory eect: chondroitin 6-sulfate, keratan sulfate and hyaluronic acid.
📜 SIMILAR VOLUMES
These studies examined the extent to which protein kinase C (PKC) and cAMP-dependent protein kinase (PKA) regulate the neuronal differentiation of the raphe-derived neuronal cell line, RN33B. A differentiation-specific 2.25-fold increase in soluble PKA activity was observed. Neither membrane-associa
The signal transduction pathway of cAMP, mediated by the cAMP-dependent protein kinase (PKA), is involved in the regulation of metabolisms, cell growth and differentiation and gene expression. Isolated PKA mutants from Chinese hamster ovary (CHO) cells were used in our laboratory to study the role o
Bicarbonate/CO 2 , a physiological effector of sperm capacitation, has been shown to induce a rapid and reversible change in the lipid architecture of the plasma membrane of live boar sperm: the change is detectable as an increase in the cells' ability to bind the fluorescent dye merocyanine, a char