Organization of non-muscle myosin during early murine embryonic differentiation

Slager, H.G.; Good, Michael J.; Schaart, Gert; Groenewoud, Jacqueline S.; Mummery, Christine L.

doi:10.1111/j.1432-0436.1992.tb00485.x

Cited by 15 publications

(9 citation statements)

References 34 publications

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“…We explain our experimental results as follows: 1) The colocalization of myosin and actin in the spinous layer, as found in the present study, is consistent with the reported results suggesting that protrusion and retraction of lamellipodia/filopodia are correlated with the dynamism of the myosin and actin molecules [24, 25]. Myosin and actin in the granular layer may be the residues which are slated to disappear in the innermost part of the cornified layer.…”

Section: Discussionsupporting

confidence: 92%

“…Nonmuscle myosin II is known to be widely distributed in species and tissues [3, 9, 11, 13] and seems to function in several types of cells [2–4, 6–8, 22, 24, 25, 28]; however, useful information about myosin and actin in skin/hair is not available. Cross reactions between anti-skeletal muscle myosin antibodies and follicular proteins were reported by Jazwinska et al , with varying results depending on the antibodies used [10].…”

Section: Discussionmentioning

confidence: 99%

“…Herein, we focused on the nonmuscle conventional myosins, which have been suggested to be active in cytokinesis [8, 14], cell movement [1, 22], chemotaxis [2, 6], the postmitotic spreading of cells [4], cell shape [6, 15, 24], stabilization of the actin cytoskeleton [29], incorporation of sperm [23] and enucleation of erythroid cells [26]. Jazwinska et al studied the distribution of skin and follicular antigens as they cross-reacted with antibodies raised against skeletal muscle myosin heavy chains [10].…”

Section: Introductionmentioning

confidence: 99%

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Localization of Myosin and Actin in the Pelage and Whisker Hair Follicles of Rat

Morioka

Matsuzaki

Takata

2006

Acta Histochem. Cytochem

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The combined effects of myosin II and actin enable muscle and nonmuscle cells to generate forces required for muscle contraction, cell division, cell migration, cellular morphological changes, the maintenance of cellular tension and polarity, and so on. However, except for the case of muscle contraction, the details are poorly understood. We focus on nonmuscle myosin and actin in the formation and maintenance of hair and skin, which include highly active processes in mammalian life with respect to the cellular proliferation, differentiation, and movement. The localization of nonmuscle myosin II and actin in neonatal rat dorsal skin, mystacial pad, hair follicles, and vibrissal follicles was studied by immunohistochemical technique to provide the basis for the elucidation of the roles of these proteins. Specificities of the antibodies were verified by using samples from the relevant tissues and subjecting them to immunoblotting test prior to morphological analyses. The myosin and actin were abundant and colocalized in the spinous and granular layers but scarce in the basal layer of the dorsal and mystacial epidermis. In hair and vibrissal follicles, nonmuscle myosin and actin were colocalized in the outer root sheath and some hair matrix cells adjoining dermal papillae. In contrast, most areas of the inner root sheath and hair matrix appeared to comprise very small amounts of myosin and actin. Hair shaft may comprise significant myosin during the course of its keratinization. These results suggest that the actin-myosin system plays a part in cell movement, differentiation, protection and other key functions of skin and hair cells.

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Section: Discussionsupporting

confidence: 92%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Localization of Myosin and Actin in the Pelage and Whisker Hair Follicles of Rat

Morioka

Matsuzaki

Takata

2006

Acta Histochem. Cytochem

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“…However, the underlying mechanism for this patterned YAP localization is not clear. In blastocysts, the F-actin and myosin staining is strong in TE but not detectable in the ICM, suggesting that contractive actin bundles are abundant in the TE (Slager et al 1992). The distribution of F-actin is in nice correlation with YAP Cold Spring Harbor Laboratory Press on June 19, 2019 -Published by genesdev.cshlp.org Downloaded from localization in blastocysts ( Fig.…”

Section: Regulation Of the Hippo Pathway: Implications In Physiologicmentioning

confidence: 87%

The Hippo pathway: regulators and regulations

2013

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Control of cell number is crucial in animal development and tissue homeostasis, and its dysregulation may result in tumor formation or organ degeneration. The Hippo pathway in both Drosophila and mammals regulates cell number by modulating cell proliferation, cell death, and cell differentiation. Recently, numerous upstream components involved in the Hippo pathway have been identified, such as cell polarity, mechanotransduction, and G-protein-coupled receptor (GPCR) signaling. Actin cytoskeleton or cellular tension appears to be the master mediator that integrates and transmits upstream signals to the core Hippo signaling cascade. Here, we review regulatory mechanisms of the Hippo pathway and discuss potential implications involved in different physiological and pathological conditions.

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“…Myosin II is reported to be homogeneously distributed in the cortex of immature rat oocytes (Amsterdam et al, 1976). In preimplantation mouse embryos and blastocysts, myosin II is found in the apical surfaces of blastomeres, restricted to these cortical regions by the continuous basolateral cell contacts formed in the early embryo (Sobel, 1983a,b;1984;Slager et al, 1992). Myosins have also been detected in the nuclei of rat testicular primary spermatocytes (Campanella et al, 1979;De Martino et al, 1980;Walt et al, 1982), in the neck and subacrosomal region of mature human spermatozoa (Campanella et al, 1979;Virtanen et al, 1984), and detected biochemically in ejaculated bull sperm (Tamblyn, 1981).…”

mentioning

confidence: 99%

Differential Expression and Functions of Cortical Myosin IIA and IIB Isotypes during Meiotic Maturation, Fertilization, and Mitosis in Mouse Oocytes and Embryos

Simerly

Nowak

Lanerolle

et al. 1998

MBoC

109

104

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To explore the role of nonmuscle myosin II isoforms during mouse gametogenesis, fertilization, and early development, localization and microinjection studies were performed using monospecific antibodies to myosin IIA and IIB isotypes. Each myosin II antibody recognizes a 205-kDa protein in oocytes, but not mature sperm. Myosin IIA and IIB demonstrate differential expression during meiotic maturation and following fertilization: only the IIA isoform detects metaphase spindles or accumulates in the mitotic cleavage furrow. In the unfertilized oocyte, both myosin isoforms are polarized in the cortex directly overlying the metaphase-arrested second meiotic spindle. Cortical polarization is altered after spindle disassembly with Colcemid: the scattered meiotic chromosomes initiate myosin IIA and microfilament assemble in the vicinity of each chromosome mass. During sperm incorporation, both myosin II isotypes concentrate in the second polar body cleavage furrow and the sperm incorporation cone. In functional experiments, the microinjection of myosin IIA antibody disrupts meiotic maturation to metaphase II arrest, probably through depletion of spindle-associated myosin IIA protein and antibody binding to chromosome surfaces. Conversely, the microinjection of myosin IIB antibody blocks microfilament-directed chromosome scattering in Colcemid-treated mature oocytes, suggesting a role in mediating chromosome-cortical actomyosin interactions. Neither myosin II antibody, alone or coinjected, blocks second polar body formation, in vitro fertilization, or cytokinesis. Finally, microinjection of a nonphosphorylatable 20-kDa regulatory myosin light chain specifically blocks sperm incorporation cone disassembly and impedes cell cycle progression, suggesting that interference with myosin II phosphorylation influences fertilization. Thus, conventional myosins break cortical symmetry in oocytes by participating in eccentric meiotic spindle positioning, sperm incorporation cone dynamics, and cytokinesis. Although murine sperm do not express myosin II, different myosin II isotypes may have distinct roles during early embryonic development. INTRODUCTIONThe cortex of mature mouse oocytes is polarized: the area adjacent to the eccentrically positioned second meiotic spindle is devoid of cortical granules and surface microvilli, diminished in concanavalin A lectin binding and demonstrates an increase in cortical actin filaments (reviewed by Longo, 1989). Similar events are observed in the cortex and plasma membrane in the vicinity of the incorporating sperm head (Nicosia et al., 1977(Nicosia et al., , 1978Shalgi et al., 1978). The induction of these cortical and cell surface modifications are ‡ Corresponding author: Oregon Regional Primate Research Center and Oregon Health Science University, 505 N.W. 185th Avenue, Beaverton, OR 97006-3499. E-mail: schatten@ohsu.edu.© 1998 by The American Society for Cell Biology 2509 strongly correlated to the presence of meiotic chromosomes or demembranated sperm DNA (Longo and Chen, 1985;Maro et al.,...

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Organization of non-muscle myosin during early murine embryonic differentiation

Cited by 15 publications

References 34 publications

Localization of Myosin and Actin in the Pelage and Whisker Hair Follicles of Rat

Localization of Myosin and Actin in the Pelage and Whisker Hair Follicles of Rat

The Hippo pathway: regulators and regulations

Differential Expression and Functions of Cortical Myosin IIA and IIB Isotypes during Meiotic Maturation, Fertilization, and Mitosis in Mouse Oocytes and Embryos

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