Immunofluorescent identification of dystrophin, actin, myosin light and heavy chains in somatic muscle cells of earthworm Lumbricus terrestris
- Authors: Nurullin L.F.1,2, Volkov E.M.1
-
Affiliations:
- Kazan State Medical University
- Kazan Institute of Biochemistry and Biophysics of Federal Research Center “Kazan Scientific Center of the Russian Academy of Sciences”
- Issue: Vol 66, No 1 (2024)
- Pages: 99-104
- Section: Articles
- URL: https://journals.rcsi.science/0041-3771/article/view/256177
- DOI: https://doi.org/10.31857/S0041377124010099
- EDN: https://elibrary.ru/HXYKMJ
- ID: 256177
Cite item
Abstract
In muscle cells of the motor muscles of the earthworm Lumbricus terrestris dystrophin, actin, fast and slow isoforms of myosin heavy chains were identified by fluorescence microscopy. It can be assumed that the expression of these proteins was carried out at the earliest stages of the evolutionary formation of the intracellular contractile apparatus of the motor tissue in both invertebrates and vertebrates. This study will complement the picture of the evolutionary formation of motor muscle tissue.
Keywords
Full Text
About the authors
L. F. Nurullin
Kazan State Medical University; Kazan Institute of Biochemistry and Biophysics of Federal Research Center “Kazan Scientific Center of the Russian Academy of Sciences”
Author for correspondence.
Email: lenizn@yandex.ru
Russian Federation, Kazan; Kazan
E. M. Volkov
Kazan State Medical University
Email: euroworm@mail.ru
Russian Federation, Kazan
References
- Давид О.Ф. Морфофизиологические основы локомоции аннелид. АН СССР. Ин-т эвол. физиол. и биохим. им. И.М. Сеченова. Л.: Наука, 1990. 168 c. (David O.F. 1990. Morfofiziologicheskie osnovy lokomocii annelid. AN SSSR. In-t evoluc. fiziologii i biohimii im. I.M. Sechenova. L.: Nauka. 168 p.)
- Cadot B., Gache V., Gomes E.R. 2015. Moving and positioning the nucleus in skeletal muscle — one step at a time. Nucleus. V. 6. P. 373. https://doi.org/10.1080/19491034. 2015.1090073
- Dancker P., Löw I., Hasselbach W., Wieland T. 1975. Interaction of actin with phalloidin: polymerization and stabilization of F-actin. Biochim. Biophys. Acta. V. 400. P. 407. https://doi.org/10.1016/0005-2795(75)90196-8
- Filippova A., Purschke G., Tzetlin A.B., Müller M.C.M. 2006. Three-dimensional reconstruction of the F-actin musculature of Dorvillea kastjani (Dorvilleidae, Polychaeta) by means of phalloidin-labelling and cLSM. Scientia Marina. V. 70(S3). P. 293. https://doi.org/ 10.3989/scimar.2006.70s3293
- Filippova A., Pürschke G., Tzetlin A.B., Müller M.C.M. 2010. Musculature in polychaetes: comparison of Myrianida prolifera (Syllidae) and Sphaerodoropsis sp. (Sphaerodoridae). Invertebrate Biology. V. 129. P. 184. https://doi.org/10.1111/j.1744-7410.2010.00191.x
- Florczyk-Soluch U., Polak K., Dulak J. 2021. The multifaceted view of heart problem in Duchenne muscular dystrophy. Cell. Mol. Life. Sci. V. 78. P. 5447. https://doi.org/ 10.1007/s00018-021-03862-2
- Fromherz S., Szent-Györgyi A.G. 1995. Role of essential light chain EF hand domains in calcium binding and regulation of scallop myosin. Proc. Natl. Acad. Sci. USA. V. 92. P. 7652. https://doi.org/10.1073%2Fpnas.92.17.7652
- Giugia J., Gieseler K., Arpagaus M., Ségalat L. 1999. Mutations in the dystrophin-like dys-1 gene of Caenorhabditis elegans result in reduced acetylcholinesterase activity. FEBS Lett. V. 463. P. 270. https://doi.org/10.1016/s0014-5793(99)01651-8
- Han Y.H., Ryu K.B., Medina Jiménez B.I., Kim J., Lee H.Y., Cho S.J. 2020. Muscular development in Urechis unicinctus (Echiura, Annelida). Int. J. Mol. Sci. V. 21. P. 1. https://doi.org/10.3390/ijms21072306
- Hooper S.L., Thuma J.B. 2005. Invertebrate muscles: muscle specific genes and proteins. Physiol. Rev. V. 85. P. 1001. https://doi.org/10.1152/physrev.00019.2004
- Kanzawa N., Kawamura Y., Matsuno A., Maruyama K. 1991. Characterization of myosin isolated from bodywall smooth muscle of the annelid, Urechis unicinctus. Proc. Japan Acad. V. 67. P. 176. https://doi.org/10.2183/pjab.67.176
- Li Y., Hu H., Butterworth M.B., Tian J.B., Zhu M.X., O’Neil R.G. 2016. Expression of a Diverse array of Ca2+-activated K+ channels (SK1/3, IK1, BK) that functionally couple to the mechanosensitive TRPV4 channel in the collecting duct system of kidney. PLoS One. V. 11: e0155006. https://doi.org/10.1371/journal.pone.0155006
- Lovato T.L., Meadows S.M., Baker P.W., Sparrow J.C., Cripps R.M. 2001. Characterization of muscle actin genes in Drosophila virilis reveals significant molecular complexity in skeletal muscle types. Insect. Mol. Biol. V. 10. P. 333. https://doi.org/10.1046/j.0962-1075.2001.00270.x
- Lowey S., Waller G.S., Trybus K.M. 1993. Function of skeletal muscle myosin heavy and light chain isoforms by an in vitro motility assay. J. Biol. Chem. V. 268. P. 20414. https://doi.org/10.1016/S0021-9258(20)80744-3
- Meedel T.H. 1983. Myosin expression in the developing ascidian embryo. J. Exp. Zool. V. 227. P. 203. https://doi.org/10.1002/jez.1402270205
- Mercer R.C., Mudalige W.A., Ige T.O., Heeley D.H. 2011. Vertebrate slow skeletal muscle actin — conservation, distribution and conformational flexibility. Biochim. Biophys. Acta. V. 1814. P. 1253. https://doi.org/10.1016/j.bbapap.2011.06.009
- Miller D.M. 3rd, Ortiz I., Berliner G.C., Epstein H.F. 1983. Differential localization of two myosins within nematode thick filaments. Cell. V. 34. P. 477. https://doi.org/10.1016/0092-8674(83)90381-1
- Nieznanski K., Nieznanska H., Skowronek K., Kasprzak A.A., Stepkowski D. 2003. Ca2+ binding to myosin regulatory light chain affects the conformation of the N-terminus of essential light chain and its binding to actin. Arch. Biochem. Biophys. V. 417. P. 153. https://doi.org/10.1016/s0003-9861(03)00382-5
- Ono S., Pruyne D. 2012. Biochemical and cell biological analysis of actin in the nematode Caenorhabditis elegans. Methods. V. 56. P. 11. https://doi.org/10.1016/j.ymeth.2011.09.008
- Pilgram G.S., Potikanond S., Baines R.A., Fradkin L.G., Noordermeer J.N. 2010. The roles of the dystrophin-associated glycoprotein complex at the synapse. Mol. Neurobiol. V. 41. P. 1. https://doi.org/10.1007/s12035-009-8089-5
- Roberts R.G., Bobrow M. 1998. Dystrophins in vertebrates and invertebrates. Hum. Mol. Genet. V. 7. P. 589. https://doi.org/10.1093/hmg/7.4.589
- Royuela M., Hugon G., Rivier F., Paniagua R., Mornet D. 2001. Dystrophin-associated proteins in obliquely striated muscle of the leech Pontobdella muricata (Annelida, Hirudinea). Histochem. J. V. 33. P. 135. https://doi.org/ 10.1023/A:1017979623095
- Royuela M., Paniagua R., Rivier F., Hugon G., Robert A., Mornet D. 1999. Presence of invertebrate dystrophin-like products in obliquely striated muscle of the leech, Pontobdella muricata (Annelida, Hirudinea). Histochem. J. V. 31. P. 603. https://doi.org/10.1023/A:1003855108802
- Rüchel J., Müller M.C.M. 2007. F-actin framework in Spirorbis cf. spirorbis (Annelida: Serpulidae): phalloidin staining investigated and reconstructed by cLSM. Invertebr. Biol. V. 126. P. 173. https://doi.org/10.1111/j.1744-7410.2007.00087.x
- Sadoulet-Puccio H.M., Kunkel L.M. 1996. Dystrophin and its isoforms. Brain Pathol. V. 6. P. 25. https://doi.org/ 10.1111/j.1750-3639.1996.tb00780.x
- Sweeney H.L., Holzbaur E.L.F. 2018. Motor proteins. Cold Spring Harb. Perspect. Biol. V. 10: a021931. https://doi.org/10.1101/cshperspect.a021931
- Volkov E.M., Nurullin L.F., Svandová I., Nikolsky E.E., Vyskocil F. 2000. Participation of electrogenic Na+,K+-ATPase in the membrane potential of earthworm body wall muscles. Physiol. Res. V. 49. P. 481. http://www.biomed.cas.cz/physiolres/pdf/49/49_481.pdf
- Wang Y., Mattson M.P., Furukawa K. 2002. Endoplasmic reticulum calcium release is modulated by actin polymerization. J. Neurochem. V. 82. P. 945. https://doi.org/ 10.1046/j.1471-4159.2002.01059.x
- Wells L., Edwards K.A., Bernstein S.I. 1996. Myosin heavy chain isoforms regulate muscle function but not myofibril assembly. EMBO J. V. 15. P. 4454. https://doi.org/10.1002/j.1460-2075.1996.tb00822.x
- Wilson D.G.S., Tinker A., Iskratsch T. 2022. The role of the dystrophin glycoprotein complex in muscle cell mechanotransduction. Commun. Biol. V. 5. P. 1022. https://doi.org/10.1038/s42003-022-03980-y