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. 1969 Nov 1;43(2):312–328.

FORMATION OF ARROWHEAD COMPLEXES WITH HEAVY MEROMYOSIN IN A VARIETY OF CELL TYPES

Harunori Ishikawa 1, Richard Bischoff 1, Howard Holtzer 1
PMCID: PMC2107852  PMID: 5344150

Abstract

Heavy meromyosin (HMM) forms characteristic arrowhead complexes with actin filaments in situ. These complexes are readily visualized in sectioned muscle. Following HMM treatment similar complexes appear in sectioned fibroblasts, chondrogenic cells, nerve cells, and several types of epithelial cells. Thin filaments freshly isolated from chondrogenic cells also bind HMM and form arrowhead structures in negatively stained preparations. HMM-filament complexes are prominent in the cortex of a variety of normal metaphase and Colcemid-arrested metaphase cells. There is no detectable binding of HMM with other cellular components such as microtubules, 100-A filaments, tonofilaments, membranes, nuclei, or collagen fibrils. The significance of HMM-filament binding is discussed in view of the finding that arrowhead complexes form in types of cells not usually thought to contain actin filaments.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ALLEN E. R., PEPE F. A. ULTRASTRUCTURE OF DEVELOPING MUSCLE CELLS IN THE CHICK EMBRYO. Am J Anat. 1965 Jan;116:115–147. doi: 10.1002/aja.1001160107. [DOI] [PubMed] [Google Scholar]
  2. Abbott J., Holtzer H. The loss of phenotypic traits by differentiated cells, V. The effect of 5-bromodeoxyuridine on cloned chondrocytes. Proc Natl Acad Sci U S A. 1968 Apr;59(4):1144–1151. doi: 10.1073/pnas.59.4.1144. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Adelman M. R., Borisy G. G., Shelanski M. L., Weisenberg R. C., Taylor E. W. Cytoplasmic filaments and tubules. Fed Proc. 1968 Sep-Oct;27(5):1186–1193. [PubMed] [Google Scholar]
  4. Aronson J. F. The use of fluorescein-labeled heavy meromyosin for the cytological demonstration of actin. J Cell Biol. 1965 Jul;26(1):293–298. doi: 10.1083/jcb.26.1.293. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bischoff R., Holtzer H. The effect of mitotic inhibitors in myogenesis in vitro. J Cell Biol. 1968 Jan;36(1):111–127. [PMC free article] [PubMed] [Google Scholar]
  6. Buckley I. K., Porter K. R. Cytoplasmic fibrils in living cultured cells. A light and electron microscope study. Protoplasma. 1967;64(4):349–380. doi: 10.1007/BF01666538. [DOI] [PubMed] [Google Scholar]
  7. Farquhar M. G., Palade G. E. Cell junctions in amphibian skin. J Cell Biol. 1965 Jul;26(1):263–291. doi: 10.1083/jcb.26.1.263. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. HUXLEY H. E. ELECTRON MICROSCOPE STUDIES ON THE STRUCTURE OF NATURAL AND SYNTHETIC PROTEIN FILAMENTS FROM STRIATED MUSCLE. J Mol Biol. 1963 Sep;7:281–308. doi: 10.1016/s0022-2836(63)80008-x. [DOI] [PubMed] [Google Scholar]
  9. Hatano S., Oosawa F. Extraction of an actin-like protein from the plasmodium of a myxomycete and its interaction with myosin A from rabbit striated muscle. J Cell Physiol. 1966 Oct;68(2):197–202. doi: 10.1002/jcp.1040680214. [DOI] [PubMed] [Google Scholar]
  10. Hatano S., Oosawa F. Isolation and characterization of plasmodium actin. Biochim Biophys Acta. 1966 Oct 31;127(2):488–498. doi: 10.1016/0304-4165(66)90402-8. [DOI] [PubMed] [Google Scholar]
  11. Inoué S., Sato H. Cell motility by labile association of molecules. The nature of mitotic spindle fibers and their role in chromosome movement. J Gen Physiol. 1967 Jul;50(6 Suppl):259–292. [PMC free article] [PubMed] [Google Scholar]
  12. Ishikawa H., Bischoff R., Holtzer H. Mitosis and intermediate-sized filaments in developing skeletal muscle. J Cell Biol. 1968 Sep;38(3):538–555. doi: 10.1083/jcb.38.3.538. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Ishikawa H. Formation of elaborate networks of T-system tubules in cultured skeletal muscle with special reference to the T-system formation. J Cell Biol. 1968 Jul;38(1):51–66. doi: 10.1083/jcb.38.1.51. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kelly D. E. Myofibrillogenesis and Z-band differentiation. Anat Rec. 1969 Mar;163(3):403–425. doi: 10.1002/ar.1091630305. [DOI] [PubMed] [Google Scholar]
  15. Marchesi V. T., Steers E., Jr Selective solubilization of a protein component of the red cell membrane. Science. 1968 Jan 12;159(3811):203–204. doi: 10.1126/science.159.3811.203. [DOI] [PubMed] [Google Scholar]
  16. Mazia D., Ruby A. Dissolution of erythrocyte membranes in water and comparison of the membrane protein with other structural proteins. Proc Natl Acad Sci U S A. 1968 Nov;61(3):1005–1012. doi: 10.1073/pnas.61.3.1005. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Morgan J., Fyfe D., Wolpert L. Isolation of microfilaments from Amoeba proteus. Exp Cell Res. 1967 Oct;48(1):194–198. doi: 10.1016/0014-4827(67)90299-6. [DOI] [PubMed] [Google Scholar]
  18. Okazaki K., Holtzer H. An analysis of myogenesis in vitro using fluorescein-labeled antimyosin. J Histochem Cytochem. 1965 Nov-Dec;13(8):726–739. doi: 10.1177/13.8.726. [DOI] [PubMed] [Google Scholar]
  19. REYNOLDS E. S. The use of lead citrate at high pH as an electron-opaque stain in electron microscopy. J Cell Biol. 1963 Apr;17:208–212. doi: 10.1083/jcb.17.1.208. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Renaud F. L., Rowe A. J., Gibbons I. R. Some properties of the protein forming the outer fibers of cilia. J Cell Biol. 1968 Jan;36(1):79–90. [PMC free article] [PubMed] [Google Scholar]
  21. Rhea R. P. Electron microscopic observations on the slime mold Physarum polycephalum with specific reference to fibrillar structures. J Ultrastruct Res. 1966 Jun;15(3):349–379. doi: 10.1016/s0022-5320(66)80113-2. [DOI] [PubMed] [Google Scholar]
  22. SZENT-GYORGYI A. G. Meromyosins, the subunits of myosin. Arch Biochem Biophys. 1953 Feb;42(2):305–320. doi: 10.1016/0003-9861(53)90360-9. [DOI] [PubMed] [Google Scholar]
  23. SZENTKIRALYI E. M. The binding of H-meromyosin on crossstriated myofibrils. Exp Cell Res. 1961 Jan;22:18–30. doi: 10.1016/0014-4827(61)90082-9. [DOI] [PubMed] [Google Scholar]
  24. Sakai H. Studies on sulfhydryl groups during cell division of sea-urchin eggs. 8. Some properties of mitotic apparatus proteins. Biochim Biophys Acta. 1966 Jan 4;112(1):132–145. doi: 10.1016/s0926-6585(96)90015-1. [DOI] [PubMed] [Google Scholar]
  25. Schmitt F. O. Fibrous proteins--neuronal organelles. Proc Natl Acad Sci U S A. 1968 Aug;60(4):1092–1101. doi: 10.1073/pnas.60.4.1092. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Shelanski M. L., Taylor E. W. Isolation of a protein subunit from microtubules. J Cell Biol. 1967 Aug;34(2):549–554. doi: 10.1083/jcb.34.2.549. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Stephens R. E. The mitotic apparatus. Physical chemical characterization of the 22S protein component and its subunits. J Cell Biol. 1967 Feb;32(2):255–275. doi: 10.1083/jcb.32.2.255. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Taylor A. C. Microtubules in the microspikes and cortical cytoplasm of isolated cells. J Cell Biol. 1966 Feb;28(2):155–168. doi: 10.1083/jcb.28.2.155. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Young M. Studies on the structural basis of the interaction of myosin and actin. Proc Natl Acad Sci U S A. 1967 Dec;58(6):2393–2400. doi: 10.1073/pnas.58.6.2393. [DOI] [PMC free article] [PubMed] [Google Scholar]

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