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Myosins Are Differentially Expressed under Oxidative Stress in Chronic Streptozotocin-Induced Diabetic Rat Brains

DOI: 10.1155/2013/423931

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Abstract:

Diabetes mellitus is a disease characterized by persistent hyperglycemia, which may lead to brain tissue damage due to oxidative stress and also contributes to neuronal death and changes in synaptic transmission. This study evaluated the effect of oxidative stress and the use of antioxidants supplementation on myosins expression levels in the brains of chronic diabetic rats induced by streptozotocin. Lipid peroxidation, antioxidant enzymes activities, and myosins-IIB and -Va expressions at transcriptional and translational levels were examined after 90 days induction. The chronic effect of the diabetes led to the upregulation of superoxide dismutase (SOD) and catalase (CAT) activities, and the downregulation of glutathione peroxidase (GPx), but there was no statistically significant increase in the malondialdehyde (MDA) levels. These alterations were accompanied by high myosin-IIB and low myosin-Va expressions. Although the antioxidant supplementation did not interfere on MDA levels, the oxidative stress caused by chronic hyperglycemia was reduced by increasing SOD and restoring CAT and GPx activities. Interestingly, after supplementation, diabetic rats recovered only myosin-Va protein levels, without interfering on myosins mRNA levels expressed in diabetic rat brains. Our results suggest that antioxidant supplementation reduces oxidative stress and also regulates the myosins protein expression, which should be beneficial to individuals with diabetes/chronic hyperglycemia. 1. Introduction Diabetes mellitus is a multifactorial disease characterized by chronic hyperglycemia resulting from abnormalities in insulin action and/or insulin secretion [1]. Research evidences support that both acute and chronic hyperglycemia produce negative impacts on the central nervous system leading to tissues damage [2, 3]. One mechanism behind this neuronal injury is oxidative stress, due to the excessive free radical generation from the oxidation of elevated intracellular glucose levels [4]. The brain contains large amounts of enzymes to protect against oxidative damage [5]. Endogenous antioxidant system, including enzymatic (glutathione peroxidase, superoxide dismutase, and catalase) and nonenzymatic (vitamin E, vitamin C, glutathione, and uric acid) antioxidants, offers protection to cells and tissues against glucose-induced oxidative injury in diabetics [6–10]. The enhancement on oxygen free radical in brain during hyperglycemia [11] contributes to increased neuronal death trough protein oxidation, DNA damage, and peroxidation of membrane lipids [12] as well as changes

References

[1]  R. E. Lamb and B. J. Goldstein, “Modulating an oxidative-inflammatory cascade: potential new treatment strategy for improving glucose metabolism, insulin resistance, and vascular function,” International Journal of Clinical Practice, vol. 62, no. 7, pp. 1087–1095, 2008.
[2]  T. Nishikawa, D. Edelstein, X. L. Du et al., “Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage,” Nature, vol. 404, no. 6779, pp. 787–790, 2000.
[3]  A. M. A. Brands, R. P. C. Kessels, E. H. F. de Haan, L. J. Kappelle, and G. J. Biessels, “Cerebral dysfunction in type 1 diabetes: effects of insulin, vascular risk factors and blood-glucose levels,” European Journal of Pharmacology, vol. 490, no. 1–3, pp. 159–168, 2004.
[4]  J. W. Russell, D. Golovoy, A. M. Vincent et al., “High glucose-induced oxidative stress and mitochondrial dysfunction in nuerons,” The FASEB Journal, vol. 16, no. 13, pp. 1738–1748, 2002.
[5]  I. Tayarani, J. Chaudiere, J.-M. Lefauconnier, and J.-M. Bourre, “Enzymatic protection against peroxidative damage in isolated brain capillaries,” Journal of Neurochemistry, vol. 48, no. 5, pp. 1399–1402, 1987.
[6]  B. Hammond, H. A. Kontos, and M. L. Hess, “Oxygen radicals in the adult respiratory distress syndrome, in myocardial ischemia and reperfusion injury, and in cerebral vascular damage,” Canadian Journal of Physiology and Pharmacology, vol. 63, no. 3, pp. 173–187, 1985.
[7]  G. del Boccio, D. Lapenna, E. Porreca et al., “Aortic antioxidant defence mechanisms: time-related changes in cholesterol-fed rabbits,” Atherosclerosis, vol. 81, no. 2, pp. 127–135, 1990.
[8]  D. Bonnefont-Rousselot, “Glucose and reactive oxygen species,” Current Opinion in Clinical Nutrition and Metabolic Care, vol. 5, no. 5, pp. 561–568, 2002.
[9]  D. Bonnefont-Rousselot, J. P. Bastard, M. C. Jaudon, and J. Delattre, “Consequences of the diabetic status on the oxidant/antioxidant balance,” Diabetes and Metabolism, vol. 26, no. 3, pp. 163–176, 2000.
[10]  R. Rahimi, S. Nikfar, B. Larijani, and M. Abdollahi, “A review on the role of antioxidants in the management of diabetes and its complications,” Biomedicine and Pharmacotherapy, vol. 59, no. 7, pp. 365–373, 2005.
[11]  G. Baydas, H. Canatan, and A. Turkoglu, “Comparative analysis of the protective effects of melatonin and vitamin E on streptozocin-induced diabetes mellitus,” Journal of Pineal Research, vol. 32, no. 4, pp. 225–230, 2002.
[12]  C. L. Hawkins and M. J. Davies, “Generation and propagation of radical reactions on proteins,” Biochimica et Biophysica Acta, vol. 1504, no. 2-3, pp. 196–219, 2001.
[13]  A. Artola, “Diabetes-, stress- and ageing-related changes in synaptic plasticity in hippocampus and neocortex—the same metaplastic process?” European Journal of Pharmacology, vol. 585, no. 1, pp. 153–162, 2008.
[14]  W. H. Gispen and G.-J. Biessels, “Cognition and synaptic plasticity in diabetes mellitus,” Trends in Neurosciences, vol. 23, no. 11, pp. 542–549, 2000.
[15]  M. Aragno, R. Mastrocola, M. G. Catalano, E. Brignardello, O. Danni, and G. Boccuzzi, “Oxidative stress impairs skeletal muscle repair in diabetic rats,” Diabetes, vol. 53, no. 4, pp. 1082–1088, 2004.
[16]  C. Coirault, A. Guellich, T. Barbry, J. L. Samuel, B. Riou, and Y. Lecarpentier, “Oxidative stress of myosin contributes to skeletal muscle dysfunction in rats with chronic heart failure,” American Journal of Physiology—Heart and Circulatory Physiology, vol. 292, no. 2, pp. H1009–H1017, 2007.
[17]  B. J. Foth, M. C. Goedecke, and D. Soldati, “New insights into myosin evolution and classification,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 10, pp. 3681–3686, 2006.
[18]  J. R. Sellers, “Myosins: a diverse superfamily,” Biochimica et Biophysica Acta, vol. 1496, no. 1, pp. 3–22, 2000.
[19]  A. Bose, A. Guilherme, S. I. Robida et al., “Glucose transporter recycling in response to insulin is facilitated by myosin Myo1c,” Nature, vol. 420, no. 6917, pp. 821–824, 2002.
[20]  M. E. Brown and P. C. Bridgman, “Myosin Function in Nervous and Sensory Systems,” Journal of Neurobiology, vol. 58, no. 1, pp. 118–130, 2004.
[21]  L. K. Calábria, G. C. N. da Cruz, R. Nascimento et al., “Overexpression of myosin-IIB in the brain of a rat model of streptozotocin-induced diabetes,” Journal of the Neurological Sciences, vol. 303, no. 1-2, pp. 43–49, 2011.
[22]  L. T. K. Chung, T. Hosaka, N. Harada et al., “Myosin IIA participates in docking of Glut4 storage vesicles with the plasma membrane in 3T3-L1 adipocytes,” Biochemical and Biophysical Research Communications, vol. 391, no. 1, pp. 995–999, 2010.
[23]  A. V. da Costa, L. K. Calábria, R. Nascimento, W. J. Carvalho, L. R. Goulart, and F. S. Espindola, “The streptozotocin-induced rat model of diabetes mellitus evidences significant reduction of myosin-Va expression in the brain,” Metabolic Brain Disease, vol. 26, no. 4, pp. 247–251, 2011.
[24]  T. Yoshizaki, T. Imamura, J. L. Babendure, J.-C. Lu, N. Sonoda, and J. M. Olefsky, “Myosin 5a is an insulin-stimulated Akt2 (protein kinase Bβ) substrate modulating GLUT4 vesicle translocation,” Molecular and Cellular Biology, vol. 27, no. 14, pp. 5172–5183, 2007.
[25]  A. V. da Costa, L. K. Calabria, F. B. Furtado et al., “Neuroprotective effects of Pouteria ramiflora (Mart.) Radlk (Sapotaceae) extract on the brains of rats with streptozotocin-induced diabetes,” Metabolic Brain Disease, vol. 28, no. 3, pp. 411–419, 2013.
[26]  C. Beaulieu, R. Kestekian, J. Havrankova, and M. Gascon-Barre, “Calcium is essential in normalizing intolerance to glucose that accompanies vitamin D depletion in vivo,” Diabetes, vol. 42, no. 1, pp. 35–43, 1993.
[27]  L. A. Martini, A. S. Catania, and S. R. G. Ferreira, “Role of vitamins and minerals in prevention and management of type 2 diabetes mellitus,” Nutrition Reviews, vol. 68, no. 6, pp. 341–354, 2010.
[28]  A. G. Pittas, J. Lau, F. B. Hu, and B. Dawson-Hughes, “Review: the role of vitamin D and calcium in type 2 diabetes. A systematic review and meta-analysis,” Journal of Clinical Endocrinology and Metabolism, vol. 92, no. 6, pp. 2017–2029, 2007.
[29]  M. F. Essop, W. A. Chan, and S. Hattingh, “Proteomic analysis of mitochondrial proteins in a mouse model of type 2 diabetes,” Cardiovascular Journal of Africa, vol. 22, no. 4, pp. 175–178, 2011.
[30]  S. Persengiev, B. P. C. Koeleman, K. Downes et al., “Association analysis of myosin IXB and type 1 diabetes,” Human Immunology, vol. 71, no. 6, pp. 598–601, 2010.
[31]  P. G. Reeves, F. H. Nielsen, and G. C. Fahey Jr., “AIN-93 purified diets for laboratory rodents: Final report of the American Institute of Nutrition ad hoc writing committee on the reformulation of the AIN-76A rodent diet,” Journal of Nutrition, vol. 123, no. 11, pp. 1939–1951, 1993.
[32]  M. M. Bradford, “A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding,” Analytical Biochemistry, vol. 72, no. 1-2, pp. 248–254, 1976.
[33]  H. Aebi, H. Suter, and R. N. Feinstein, “Activity and stability of catalase in blood and tissues of normal and acatalasemic mice,” Biochemical Genetics, vol. 2, no. 3, pp. 245–251, 1968.
[34]  H. Towbin, T. Staehelin, and J. Gordon, “Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications,” Proceedings of the National Academy of Sciences of the United States of America, vol. 76, no. 9, pp. 4350–4354, 1979.
[35]  R. E. Larson, J. A. Ferro, and E. A. Queiroz, “Isolation and purification of actomyosin ATPase from mammalian brain,” Journal of Neuroscience Methods, vol. 16, no. 1, pp. 47–58, 1986.
[36]  D. M. Suter, F. S. Espindola, C. H. Lin, P. Forscher, and M. S. Mooseker, “Localization of unconventional myosins V and VI in neuronal growth cones,” Journal of Neurobiology, vol. 42, pp. 370–382, 2000.
[37]  E. M. Espreafico, R. E. Cheney, M. Matteoli et al., “Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains,” Journal of Cell Biology, vol. 119, no. 6, pp. 1541–1557, 1992.
[38]  J. L. Yin, N. A. Shackel, A. Zekry et al., “Real-time reverse transcriptase-polymerase chain reaction (RT-PCR) for measurement of cytokine and growth factor mRNA expression with fluorogenic probes or SYBR Green I,” Immunology and Cell Biology, vol. 79, no. 3, pp. 213–221, 2001.
[39]  P. A. Low, K. K. Nickander, and H. J. Tritschler, “The roles of oxidative stress and antioxidant. Treatment in experimental diabetic neuropathy,” Diabetes, vol. 46, supplement 2, pp. S38–S42, 1997.
[40]  F. Gardoni, A. Kamal, C. Bellone et al., “Effects of streptozotocin-diabetes on the hippocampal NMDA receptor complex in rats,” Journal of Neurochemistry, vol. 80, no. 3, pp. 438–447, 2002.
[41]  E. Coleman, R. Judd, L. Hoe, J. Dennis, and P. Posner, “Effects of diabetes mellitus on astrocyte GFAP and glutamate transporters in the CNS,” Glia, vol. 48, no. 2, pp. 166–178, 2004.
[42]  S. S. Kamboj, K. Chopra, and R. Sandhir, “Neuroprotective effect of N-acetylcysteine in the development of diabetic encephalopathy in streptozotocin-induced diabetes,” Metabolic Brain Disease, vol. 23, no. 4, pp. 427–443, 2008.
[43]  J. P. Hernández-Fonseca, J. Rincón, A. Pedrea?ez et al., “Structural and ultrastructural analysis of cerebral cortex, cerebellum, and hypothalamus from diabetic rats,” Experimental Diabetes Research, vol. 2009, Article ID 329632, 12 pages, 2009.
[44]  R. J. Gomes, C. A. M. de Oliveira, C. Ribeiro et al., “Effects of exercise training on hippocampus concentrations of insulin and IGF-1 in diabetic rats,” Hippocampus, vol. 19, no. 10, pp. 981–987, 2009.
[45]  K. Asplund, K. Grankvist, S. Marklund, and I. B. Taljedal, “Partial protection against streptozotocin-induced hyperglycaemia by superoxide dismutase linked to polyethylene glycol,” Acta Endocrinologica, vol. 107, no. 3, pp. 390–394, 1984.
[46]  R. Kakkar, J. Kalra, S. V. Mantha, and K. Prasad, “Lipid peroxidation and activity of antioxidant enzymes in diabetic rats,” Molecular and Cellular Biochemistry, vol. 151, no. 2, pp. 113–119, 1995.
[47]  R. Kakkar, S. V. Mantha, J. Radhi, K. Prasad, and J. Kalra, “Antioxidant defense system in diabetic kidney: a time course study,” Life Sciences, vol. 60, no. 9, pp. 667–679, 1997.
[48]  S. Genet, R. K. Kale, and N. Z. Baquer, “Alterations in antioxidant enzymes and oxidative damage in experimental diabetic rat tissues: effect of vanadate and fenugreek (Trigonella foenum graecum),” Molecular and Cellular Biochemistry, vol. 236, no. 1-2, pp. 7–12, 2002.
[49]  P. V. Limaye, N. Raghuram, and S. Sivakami, “Oxidative stress and gene expression of antioxidant enzymes in the renal cortex of streptozotocin-induced diabetic rats,” Molecular and Cellular Biochemistry, vol. 243, no. 1-2, pp. 147–152, 2003.
[50]  S. R. Panneerselvam and S. Govindasamy, “Effect of sodium molybdate on the status of lipids, lipid peroxidation and antioxidant systems in alloxan-induced diabetic rats,” Clinica Chimica Acta, vol. 345, no. 1-2, pp. 93–98, 2004.
[51]  B. Halliwell, “Reactive oxygen species and the central nervous system,” Journal of Neurochemistry, vol. 59, no. 5, pp. 1609–1623, 1992.
[52]  N. N. Ulusu, M. Sahilli, A. Avci et al., “Pentose phosphate pathway, glutathione -dependent enzymes and antioxidant defense during oxidative stress in diabetic rodent brain and peripheral organs: effects of stobadine and vitamin E,” Neurochemical Research, vol. 28, no. 6, pp. 815–823, 2003.
[53]  M. R. Siddiqui, A. Taha, K. Moorthy, M. E. Hussain, S. F. Basir, and N. Z. Baquer, “Amelioration of altered antioxidant status and membrane linked functions by vanadium and Trigonella in alloxan diabetic rat brains,” Journal of Biosciences, vol. 30, no. 4, pp. 483–490, 2005.
[54]  W.-C. Huang, S.-W. Juang, I.-M. Liu, T.-C. Chi, and J.-T. Cheng, “Changes of superoxide dismutase gene expression and activity in the brain of streptozotocin-induced diabetic rats,” Neuroscience Letters, vol. 275, no. 1, pp. 25–28, 1999.
[55]  N. Sinha, N. Z. Baquer, and D. Sharma, “Anti-lipidperoxidative role of exogenous dehydroepiendrosterone (DHEA) administration in normal ageing rat brain,” Indian Journal of Experimental Biology, vol. 43, no. 5, pp. 420–424, 2005.
[56]  A. Kuhad and K. Chopra, “Curcumin attenuates diabetic encephalopathy in rats: behavioral and biochemical evidences,” European Journal of Pharmacology, vol. 576, no. 1–3, pp. 34–42, 2007.
[57]  T. K. Makar, K. Rimpel-Lamhaouar, D. G. Abraham, V. S. Gokhale, and A. J. L. Cooper, “Antioxidant defense systems in the brains of type II diabetic mice,” Journal of Neurochemistry, vol. 65, no. 1, pp. 287–291, 1995.
[58]  O.-G. Kwag, S.-O. Kim, J.-H. Choi, I.-K. Rhee, M.-S. Choi, and S.-J. Rhee, “Vitamin E improves microsomal phospholipase A2 activity and the arachidonic acid cascade in kidney of diabetic rats,” Journal of Nutrition, vol. 131, no. 4, pp. 1297–1301, 2001.
[59]  J. S. Suresh Kumar and V. P. Menon, “Effect of diabetes on levels of lipid peroxides and glycolipids in rat brain,” Metabolism, vol. 42, no. 11, pp. 1435–1439, 1993.
[60]  S. A. Wohaieb and D. V. Godin, “Alterations in free radical tissue-defense mechanisms in streptozocin-induced diabetes in rat. Effects of insulin treatment,” Diabetes, vol. 36, no. 9, pp. 1014–1018, 1987.
[61]  Y. G. ?zkaya, A. Agar, P. Yargi?oglu et al., “The effect of exercise on brain antioxidant status of diabetic rats,” Diabetes and Metabolism, vol. 28, no. 5, pp. 377–384, 2002.
[62]  V. M. Bhor, N. Raghuram, and S. Sivakami, “Oxidative damage and altered antioxidant enzyme activities in the small intestine of streptozotocin-induced diabetic rats,” International Journal of Biochemistry and Cell Biology, vol. 36, no. 1, pp. 89–97, 2004.
[63]  M. B. Zemel, W. Thompson, A. Milstead, K. Morris, and P. Campbell, “Calcium and dairy acceleration of weight and fat loss during energy restriction in obese adults,” Obesity Research, vol. 12, no. 4, pp. 582–590, 2004.
[64]  I. H. de Boer, L. F. Tinker, S. Connelly et al., “Calcium plus vitamin D supplementation and the risk of incident diabetes in the women's health initiative,” Diabetes Care, vol. 31, no. 4, pp. 701–707, 2008.
[65]  I. Fridovich, “Superoxide radical and superoxide dismutases,” Annual Review of Biochemistry, vol. 64, pp. 97–112, 1995.
[66]  M. Valko, H. Morris, and M. T. D. Cronin, “Metals, toxicity and oxidative stress,” Current Medicinal Chemistry, vol. 12, no. 10, pp. 1161–1208, 2005.
[67]  C. G. Taylor, “Zinc, the pancreas, and diabetes: insights from rodent studies and future directions,” BioMetals, vol. 18, no. 4, pp. 305–312, 2005.
[68]  C. Scheede-Bergdahl, M. Penkowa, J. Hidalgo et al., “Metallothionein-mediated antioxidant defense system and its response to exercise training are impaired in human type 2 diabetes,” Diabetes, vol. 54, no. 11, pp. 3089–3094, 2005.
[69]  M. Beltramini, P. Zambenedetti, M. Raso, M. I. IbnlKayat, and P. Zatta, “The effect of Zn(II) and streptozotocin administration in the mouse brain,” Brain Research, vol. 1109, no. 1, pp. 207–218, 2006.
[70]  C. G. Taylor, W. J. Bettger, and T. M. Bray, “Effect of dietary zinc or copper deficiency on the primary free radical defense system in rats,” Journal of Nutrition, vol. 118, no. 5, pp. 613–621, 1988.
[71]  H. Yoshida, K. Sasaki, Y. Hirowatari et al., “Increased serum iron may contribute to enhanced oxidation of low-density lipoprotein in smokers in part through changes in lipoxygenase and catalase,” Clinica Chimica Acta, vol. 345, no. 1-2, pp. 161–170, 2004.
[72]  R. A. Kowluru, R. L. Engerman, and T. S. Kern, “Diabetes-induced metabolic abnormalities in myocardium: effect of antioxidant therapy,” Free Radical Research, vol. 32, no. 1, pp. 67–74, 2000.
[73]  M. Valko, D. Leibfritz, J. Moncol, M. T. D. Cronin, M. Mazur, and J. Telser, “Free radicals and antioxidants in normal physiological functions and human disease,” International Journal of Biochemistry and Cell Biology, vol. 39, no. 1, pp. 44–84, 2007.
[74]  G. Paolisso, A. D'Amore, D. Giugliano, A. Ceriello, M. Varricchio, and F. D'Onofrio, “Pharmacologic doses of vitamin E improve insulin action in healthy subjects and non-insulin-dependent diabetic patients,” American Journal of Clinical Nutrition, vol. 57, no. 5, pp. 650–656, 1993.
[75]  G. Paolisso, G. di Maro, D. Galzerano et al., “Pharmacological doses of vitamin E and insulin action in elderly subjects,” American Journal of Clinical Nutrition, vol. 59, no. 6, pp. 1291–1296, 1994.
[76]  N. C. Ward, J. H. Y. Wu, M. W. Clarke et al., “The effect of vitamin E on blood pressure in individuals with type 2 diabetes: a randomized, double-blind, placebo-controlled trial,” Journal of Hypertension, vol. 25, no. 1, pp. 227–234, 2007.
[77]  H. Yanagisawa, M. Sato, M. Nodera, and O. Wada, “Excessive zinc intake elevates systemic blood pressure levels in normotensive rats—potential role of superoxide-induced oxidative stress,” Journal of Hypertension, vol. 22, no. 3, pp. 543–550, 2004.
[78]  K. Moorthy, D. Sharma, S. F. Basir, and N. Z. Baquer, “Administration of estradiol and progesterone modulate the activities of antioxidant enzyme and aminotransferases in naturally menopausal rats,” Experimental Gerontology, vol. 40, no. 4, pp. 295–302, 2005.
[79]  K. Moorthy, U. C. S. Yadav, M. R. Siddiqui et al., “Effect of hormone replacement therapy in normalizing age related neuronal markers in different age groups of naturally menopausal rats,” Biogerontology, vol. 6, no. 5, pp. 345–356, 2005.
[80]  C. A. Grillo, G. G. Piroli, G. E. Wood, L. R. Reznikov, B. S. McEwen, and L. P. Reagan, “Immunocytochemical analysis of synaptic proteins provides new insights into diabetes-mediated plasticity in the rat hippocampus,” Neuroscience, vol. 136, no. 2, pp. 477–486, 2005.
[81]  D. Zhu, K. S. Tan, X. Zhang, A. Y. Sun, G. Y. Sun, and J. C.-M. Lee, “Hydrogen peroxide alters membrane and cytoskeleton properties and increases intercellular connections in astrocytes,” Journal of Cell Science, vol. 118, no. 16, pp. 3695–3703, 2005.
[82]  M. J. Mihm, F. Yu, P. J. Reiser, and J. A. Bauer, “Effects of peroxynitrite on isolated cardiac trabeculae: selective impact on myofibrillar energetic controllers,” Biochimie, vol. 85, no. 6, pp. 587–596, 2003.
[83]  S. Mochida, H. Kobayashi, Y. Matsuda, Y. Yuda, K. Muramoto, and Y. Nonomura, “Myosin II is involved in transmitter release at synapses formed between rat sympathetic neurons in culture,” Neuron, vol. 13, no. 5, pp. 1131–1142, 1994.
[84]  S. L. Reck-Peterson, D. W. Provance Jr., M. S. Mooseker, and J. A. Mercer, “Class V myosins,” Biochimica et Biophysica Acta, vol. 1496, no. 1, pp. 36–51, 2000.

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