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Concerted phosphorylation of endogenous tracheal smooth muscle membrane proteins by Ca 2+ · calmodulin‐, cyclic GMP‐ and cyclic AMP‐dependent protein kinases
Author(s) -
Hogaboom G.Kurt,
Emler Carol A.,
Butcher Fred R.,
Fedan Jeffrey S.
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)80877-6
Subject(s) - west virginia , medicine , archaeology , history
The precise control of the myoplasmic free [Ca”] is an important determinant in the regulation of the contractile state of mammalian smooth muscle [ 11. The control mechanism is thought to reside with membrane Ca’+-transport ATPases which actively pump Ca’+ against a concentration gradient and maintain the intracellular [Ca”] below 0.1 ,uM. The Ca2+transport ATPase has been measured in many smooth muscle types [2,3], purified [4], and its activity has been shown to be modulated by cyclic nucleotides [ 5,6 ] as well as by the Ca*‘-binding protein calmodr lin [3]. MI, appear to be phosphorylated by all 3 second messengers. The functional role of the concerted phosphorylation remains unknown but may be intimately involved in the regulation of smooth muscle membrane function including Ca*+ transport.