It has been shown that CAMP-dependent phosphorylation of a soluble sperm protein is important for the initiation of flagellar motion. The suggestion has been made that this motility initiation protein, named axokinin, is the major 56,000-dalton phosphoprotein present in both dog sperm and in other c
Immunofluorescence localization of the regulatory subunit type II of cAMP-dependent protein kinase in PC12 and 3T3 cells in different proliferative states
β Scribed by Igor I. Shmyrev; Irina D. Grozdova; Aleksei D. Kondratyev; Elena G. Mamayeva; Evgenii S. Severin
- Publisher
- Springer
- Year
- 1990
- Tongue
- English
- Weight
- 398 KB
- Volume
- 93
- Category
- Article
- ISSN
- 0300-8177
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β¦ Synopsis
Localization of the regulatory subunit of cAMP-dependent protein kinase type II was studied in proliferating and quiescent fibroblasts 3T3 and in a cell line of neural origin pheochromocytoma PC12. In actively proliferating PC12 cells the regulatory subunit was found to be localized in the nucleus. Transition of these cells into a quiescent state was accompanied by a regulatory subunit translocation to the cytoplasm. In 3T3 cells the regulatory subunit was localized in the cytoplasm both in the quiescent and proliferating (though less actively than PC12 cells) states. Similar results were obtained both with monoclonal antibodies and with rabbit monospecific antiserum raised against the regulatory subunit type II from pig brain.
π SIMILAR VOLUMES
The phosphorylative neuromodulation of the regulatory subunit of protein kinase type II (R-II) in cytosolic fractions from denervated and sham-operated, contralateral soleus muscles of the rat was evaluated. The denervation-induced increase in the 32P-phosphorylation of R-II is not related to an inc
CAMP-binding regulatory subunits (RI Or RI1) but share a common catalytic subunit (C) (9,14). RI and RII Medica,