Myosin Light Chain Phosphorylation at Resting Level and the Composition of Myosin Isoforms in the Bladder Body and Urethra

REFERENCES

• Krane RJ, Olsson CA. Phenoxybenzamine in neurogenic bladder dysfunction. I. A theory of micturition. J Urol 1973; 110: 650–2.
   PubMedGoogle Scholar
• McGuire EJ. Mechanisms of urethral continence and their clinical application. World J Urol 1984; 2: 272.
   Web of Science ®Google Scholar
• Levin RM, Shofer FS, Wein AJ. Cholinergic, adrener-gic, and purinergic response of sequential strips of rabbit urinary bladder. J Pharm Exp Thera 1980; 212: 536–40.
   Google Scholar
• Khanna OP, Barbieri EJ, Altamura M, McMichael R. Vesicourethral smooth muscle: function and relation to structure. Urology 1981; 18: 211–8.
   PubMed Web of Science ®Google Scholar
• Mundy AR. Structure and function of the urinary tract. In: Mundy AR, editor. Scientific basis of urology. New York: Churchill Livingstone, 1987: 48–73.
   Google Scholar
• Wein AJ, Levin RM, Barrett DM. Voiding function: relevant anatomy, physiology, and pharmacology. In: Gillenwater JY, Grayhack JT, Howards SS, Duckett JD, editors. Adult and pediatric urology. Chicago: Year Book Medical Publishers, 1987: 800–62.
   Google Scholar
• Guyton AC. Smooth muscle. In: Anon., editors. Text-book of medical physiology. Philadelphia: WP Saunders and Co., 1986: 686–96.
   Google Scholar
• Wein AJ, Raezer DM. Physiology of micturition. In: Krane RJ, Siroky MB, editors. Clinical neurourology. Boston: Little Brown Co., 1979: 1–33.
   Google Scholar
• Somlyo AV, Somlyo AP. Electromechanical and pharmacomechanical coupling in vascular smooth muscle. J Pharmacol Exp Ther 1968; 159: 129–45.
   PubMed Web of Science ®Google Scholar
• Hypolite JA, DiSanto ME, Wein AJ, Chacko S. Regional variations in the composition of myosin isoforms and light chain phosphorylation at the restingtone in rabbit bladder smooth muscle. J Urol 1998; 159: 23.
   Web of Science ®Google Scholar
• Fay FS, Shlevin 1111, Granger WC, Taylot SR. Aequorin luminescence during activation of single isolated smooth muscle cells. Nature 1979; 280: 506–8.
   Google Scholar
• Somlyo AP, Somlyo AV. Signal transduction and regulation in smooth muscle (and erratum in Nature 1994; 372: 812). Nature 1994; 372: 231–6.
   PubMed Web of Science ®Google Scholar
• Adelstein RS, Eisenberg E. Regulation and kinetics of the actin-myosin-ATP interaction. Ann Rev Biochem 1980; 49: 921–56.
   PubMed Web of Science ®Google Scholar
• Kamm KE, Stull JT. The function of myosin and myosin light chain kinase phosphorylation in smooth muscle. Ann Rev Pharmacol Toxicol 1985; 25: 593–620.
   PubMed Web of Science ®Google Scholar
• Kendrick-Jones J, Cande WZ, Tooth PJ, Smith RC, Scholey JM. Studies on the effect of phosphorylation of the 20000 Mr light chain of vertebrate smooth muscle myosin. J Mol Biol 1983; 165: 139–62.
   Google Scholar
• Suzuki H, Onishi H, Takahashi K, Watanabe S. Structure and function of chicken gizzard myosin. J Biochem (Tokyo) 1978; 84: 1529–42.
   PubMed Web of Science ®Google Scholar
• Trybus KM. Filamentous smooth muscle myosin is regulated by phosphorylation. J Cell Biol 1989; 109: 2887–94.
   PubMed Web of Science ®Google Scholar
• Chacko S, Conti MA, Adelstein RS. Effect of phos-phorylation of smooth muscle myosin on actin activa-tion and Ca2+ regulation. Proc Natl Acad Sci USA 1977; 74: 129–33.
   Google Scholar
• Gorecka A, Aksoy MO, Hartshorne DJ. The effect of phosphorylation of gizzard myosin on actin activation. Biochem Biophys Res Commun 1976; 71: 325–31.
   PubMed Web of Science ®Google Scholar
• Sellers JR, Pato MD, Adelstein RS. Reversible phos-phorylation of smooth muscle myosin, heavy meromyo-sin, and platelet myosin. J Biol Chem 1981; 256: 13137–42.
   Google Scholar
• Sobieszek A, Small JV. Regulation of the actin-myosin interaction in vertebrate smooth muscle: activation via a myosin light-chain kinase and the effect of tropomyosin. J Mol Biol 1977; 112: 559–76.
   PubMed Web of Science ®Google Scholar
• Barany M, Barany K. Phosphorylation of the myofi-brillar proteins. Ann Rev Physiol 1980; 42: 275–92.
   PubMed Web of Science ®Google Scholar
• Butler TM, Siegman MJ, Mooers SU. Chemical energy usage during shortening and work production in mammalian smooth muscle. Am J Physiol 1983; 244: C234–42.
   Google Scholar
• Dillon PF, Aksoy MO, Driska SP, Murphy RA. Myosin phosphorylation and the cross-bridge cycle in arterial smooth muscle. Science 1981; 211: 495–7.
   PubMed Web of Science ®Google Scholar
• Gong MC, Cohen P, Kitazawa T, Ikebe M, Masuo M, Somlyo AP, et al. Myosin light chain phosphatase activities and the effects of phosphatase inhibitors in tonic and phasic smooth muscle. J Biol Chem 1992; 267: 14662–8.
   PubMed Web of Science ®Google Scholar
• Chacko S, Longhurst PA. Regulation of actomyosin and contraction in smooth muscle. World J Urol 1994; 12: 292–7.
   PubMed Web of Science ®Google Scholar
• DiSanto ME, Cox RH, Wang Z, Chacko S. NH2-terminal-inserted myosin II heavy chain is expressed in smooth muscle of small muscular arteries. Am J Physiol 1997; 272: C1532–42.
   PubMedGoogle Scholar
• Kelley CA, Takahashi M, Yu JH, Adelstein RS. An insert of seven amino acids confers functional differ-ences between smooth muscle myosins from the intestines and vasculature. J Biol Chem 1993; 268: 12848–54.
   PubMed Web of Science ®Google Scholar
• Damaser MS, Yu HJ, Longhurst PA, Levin RM. The concept of bladder work: work and power in bladder emptying. Scand J Urol Nephrol 1997; Suppl 184: 35–41.
   Google Scholar
• DiSanto M, Wang Z, Menon C, Zheng Y, Chacko T, Hypolite J, et al. Expression of myosin isoforms in smooth muscle cells in the corpus cavemosum penis. Am J Physiol 1998; 275: C976–87.
   PubMedGoogle Scholar
• Hartshorne DJ Physiology of the gastrointestinal tract, 2nd edn, New York: Raven, 1987.
   Google Scholar