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• W2289538320 abstract "I t i s now g e n e r a l l y accepted that changes i n p r o t e i n phosphorylation play an important r o l e i n mediating smooth muscle tone. An attempt was made to determine whether nitrogen oxide c o n t a i n i n g v a s o d i l a t o r s such as sodium n i t r o p r u s s i d e and n i t r o g l y c e r i n exert t h e i r r e l a x ant e f f e c t v i a a phosphorylation r e a c t i o n . I s o e l e c t r i c focusing was i n i t i a l l y used as a method of d e t e c t i n g phosphorylation. However, due to the smaller percentage of p r o t e i n i n smooth muscle with a r e l a t i v e increase i n other c e l l c o n s t i t u e n t s , crude smooth muscle homogenates were deemed to be too complex f o r a n a l y s i s by t h i s technique alone. Phosphorylation changes are commonly studied by incubating the muscle i n l a b e l l e d i n o r g a n i c phosphate, thus l a b e l l i n g the ATP pools. P r o t e i n s are separated by SDS-polyacrylamide gel e l e c t r o p h o r e s i s . Following s t a i n i n g and d r y i n g , gels are exposed to X-ray f i l m and phosphorylation l e v e l s determined. By comparing a o r t i c s t r i p s relaxed i n Ca^-free, 5 mM EGTA Krebs with muscle s t r i p s contracted i n 1^(124 mM) Krebs, a s i g n i f i c a n t d i f f e r e n c e between the phosphorylation l e v e l s of myosin l i g h t chain was q u a n t i t a t e d . By reproducing t h i s well documented phenomena, we demonstrated that we had e s t a b l i s h e d a working methodology i n the l a b o r a t o r y . In view of the controversy i n the l i t e r a t u r e concerning sustained l e v e l s of myosin l i g h t chain phosphorylation during sustained K^-induced c o n t r a c t i o n s , a K^time course study was performed. Levels of myosin l i g h t chain phosphorylation increased s i g n i f i c a n t l y w i t h i n the f i r s t 2 min of c o n t r a c t i o n and were maintained f o r 12 min, though a n o n s i g n i f i c a n t decrease was observed a f t e r 2 min. Tension peaked at 4 min and t h e r e a f t e r remained constant. F inal ly , the effect of nitroglycerin (10~tVl) on C-induced contractions was br ief ly examined. Nitroglycerin caused a 70% relaxation within 2 min and s ignif icant ly decreased myosin l ight chain phosphorylation levels . There also appeared to be an increase in phosphorylation of a 160kD protein with nitroglycerin treatment, which due to technical d i f f i cu l t i es could not be quantitated." @default.
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• W2289538320 date "1984-01-01" @default.
• W2289538320 modified "2023-09-23" @default.
• W2289538320 title "CHANGES IN PROTEIN PHOSPHORYLATION DURING CHANGES IN VASCULAR SMOOTH MUSCLE TONE" @default.
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• W2289538320 doi "https://doi.org/10.14288/1.0096125" @default.
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