The Experts below are selected from a list of 216 Experts worldwide ranked by ideXlab platform
Z. Fan - One of the best experts on this subject based on the ideXlab platform.
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amitosis like Nuclear Division in erythrocytes of triploid rainbow trout oncorhynchus mykiss
Journal of Fish Biology, 2010Co-Authors: B. Wang, Y. Liu, X. Chen, Z. FanAbstract:This work shows that the atypical erythrocytes in triploid rainbow trout Oncorhynchus mykiss were morphologically similar to those of toads. The nuclei of the cells can be bell-shaped, constricted or irregular. It is presumed that such Nuclear Division is probably amitosis.
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Amitosis‐like Nuclear Division in erythrocytes of triploid rainbow trout Oncorhynchus mykiss
Journal of fish biology, 2010Co-Authors: B. Wang, Y. Liu, X. Chen, Z. FanAbstract:This work shows that the atypical erythrocytes in triploid rainbow trout Oncorhynchus mykiss were morphologically similar to those of toads. The nuclei of the cells can be bell-shaped, constricted or irregular. It is presumed that such Nuclear Division is probably amitosis.
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BRIEF COMMUNICATIONS Amitosis-like Nuclear Division in erythrocytes of triploid rainbow trout Oncorhynchus mykiss
2010Co-Authors: B. Wang, Y. Liu, X. Chen, Z. FanAbstract:Rainbow trout Oncorhynchus mykiss (Walbaum) is a cold-water aquaculture species, which belongs to Salmonidae of Salmoniformes. The induction and biology of triploid fish have received considerable attention from researchers and cultivators due to the fish’s superior meat quality and growth vigour caused by sterility (Gervai et al., 1980; Lou, 1984; Wu et al., 1986; Gui et al., 1990; Recoubratsky et al., 1992). Atypical or divided erythrocyte nuclei are commonly distinguished in triploid fish such as triploid O. mykiss (Zou et al., 2006; Han et al., 2007). Dorafshan et al. (2008) considered that atypical erythrocytes in triploid Caspian salmon Salmo trutta caspius L. were behind the mechanism to cope with stress in fish, and triploids might be less tolerant to stress than diploids; such a Nuclear pattern in triploid brook trout Salvelinus fontinalis (Mitchill) reflected some kind of functional depression or mobilization of granulocytes (Wlasow et al., 2004). The atypical cells are regarded as a cytological marker for triploidy. (Benfey & Sutterlin,1984; Zhu et al., 1992; Liu et al., 2003). There are, however, no systematic studies on Nuclear constriction, abnormal Division or exploration into the cause of such Nuclear Division. It was found that the erythrocytes in triploid O. mykiss were very similar to those of toads in morphology. The Nuclear Division or atypical cells of amphibians are considered to be an example of amitosis (Pan, 1956; Barni et al., 1995); a comparative morphological study of erythrocytes was carried out between the triploid O. mykiss and toads to test this assumption.
B. Wang - One of the best experts on this subject based on the ideXlab platform.
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amitosis like Nuclear Division in erythrocytes of triploid rainbow trout oncorhynchus mykiss
Journal of Fish Biology, 2010Co-Authors: B. Wang, Y. Liu, X. Chen, Z. FanAbstract:This work shows that the atypical erythrocytes in triploid rainbow trout Oncorhynchus mykiss were morphologically similar to those of toads. The nuclei of the cells can be bell-shaped, constricted or irregular. It is presumed that such Nuclear Division is probably amitosis.
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Amitosis‐like Nuclear Division in erythrocytes of triploid rainbow trout Oncorhynchus mykiss
Journal of fish biology, 2010Co-Authors: B. Wang, Y. Liu, X. Chen, Z. FanAbstract:This work shows that the atypical erythrocytes in triploid rainbow trout Oncorhynchus mykiss were morphologically similar to those of toads. The nuclei of the cells can be bell-shaped, constricted or irregular. It is presumed that such Nuclear Division is probably amitosis.
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BRIEF COMMUNICATIONS Amitosis-like Nuclear Division in erythrocytes of triploid rainbow trout Oncorhynchus mykiss
2010Co-Authors: B. Wang, Y. Liu, X. Chen, Z. FanAbstract:Rainbow trout Oncorhynchus mykiss (Walbaum) is a cold-water aquaculture species, which belongs to Salmonidae of Salmoniformes. The induction and biology of triploid fish have received considerable attention from researchers and cultivators due to the fish’s superior meat quality and growth vigour caused by sterility (Gervai et al., 1980; Lou, 1984; Wu et al., 1986; Gui et al., 1990; Recoubratsky et al., 1992). Atypical or divided erythrocyte nuclei are commonly distinguished in triploid fish such as triploid O. mykiss (Zou et al., 2006; Han et al., 2007). Dorafshan et al. (2008) considered that atypical erythrocytes in triploid Caspian salmon Salmo trutta caspius L. were behind the mechanism to cope with stress in fish, and triploids might be less tolerant to stress than diploids; such a Nuclear pattern in triploid brook trout Salvelinus fontinalis (Mitchill) reflected some kind of functional depression or mobilization of granulocytes (Wlasow et al., 2004). The atypical cells are regarded as a cytological marker for triploidy. (Benfey & Sutterlin,1984; Zhu et al., 1992; Liu et al., 2003). There are, however, no systematic studies on Nuclear constriction, abnormal Division or exploration into the cause of such Nuclear Division. It was found that the erythrocytes in triploid O. mykiss were very similar to those of toads in morphology. The Nuclear Division or atypical cells of amphibians are considered to be an example of amitosis (Pan, 1956; Barni et al., 1995); a comparative morphological study of erythrocytes was carried out between the triploid O. mykiss and toads to test this assumption.
Yoshiharu Inoue - One of the best experts on this subject based on the ideXlab platform.
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methylglyoxal inhibits Nuclear Division through alterations in vacuolar morphology and accumulation of atg18 on the vacuolar membrane in saccharomyces cerevisiae
Scientific Reports, 2020Co-Authors: Wataru Nomura, Miho Aoki, Yoshiharu InoueAbstract:Methylglyoxal (MG) is a natural metabolite derived from glycolysis, and it inhibits the growth of cells in all kinds of organisms. We recently reported that MG inhibits Nuclear Division in Saccharomyces cerevisiae. However, the mechanism by which MG blocks Nuclear Division remains unclear. Here, we show that increase in the levels of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) is crucial for the inhibitory effects of MG on Nuclear Division, and the deletion of PtdIns(3,5)P2-effector Atg18 alleviated the MG-mediated inhibitory effects. Previously, we reported that MG altered morphology of the vacuole to a single swelling form, where PtdIns(3,5)P2 accumulates. The changes in the vacuolar morphology were also needed by MG to exert its inhibitory effects on Nuclear Division. The known checkpoint machinery, including the spindle assembly checkpoint and morphological checkpoint, are not involved in the blockade of Nuclear Division by MG. Our results suggest that both the accumulation of Atg18 on the vacuolar membrane and alterations in vacuolar morphology are necessary for the MG-induced inhibition of Nuclear Division.
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toxicity of dihydroxyacetone is exerted through the formation of methylglyoxal in saccharomyces cerevisiae effects on actin polarity and Nuclear Division
Biochemical Journal, 2018Co-Authors: Wataru Nomura, Miho Aoki, Yoshiharu InoueAbstract:Dihydroxyacetone (DHA) is the smallest ketotriose, and it is utilized by many organisms as an energy source. However, at higher concentrations, DHA becomes toxic towards several organisms including the budding yeast Saccharomyces cerevisiae In the present study, we show that DHA toxicity is due to its spontaneous conversion to methylglyoxal (MG) within yeast cells. A mutant defective in MG-metabolizing enzymes (glo1Δgre2Δgre3Δ) exhibited higher susceptibility to DHA. Intracellular MG levels increased following the treatment of glo1Δgre2Δgre3Δ cells with DHA. We previously reported that MG depolarized the actin cytoskeleton and changed vacuolar morphology. We herein demonstrated the depolarization of actin and morphological changes in vacuoles following a treatment with DHA. Furthermore, we found that both MG and DHA caused the morphological change in nucleus, and inhibited the Nuclear Division. Our results suggest that the conversion of DHA to MG is a dominant contributor to its cytotoxicity.
Pamela A. Silver - One of the best experts on this subject based on the ideXlab platform.
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nuf2 a spindle pole body associated protein required for Nuclear Division in yeast
Journal of Cell Biology, 1994Co-Authors: Mark A Osborne, T Jinks, Gabriel Schlenstedt, Pamela A. SilverAbstract:The NUF2 gene of the yeast Saccharomyces cerevisiae encodes an essential 53-kd protein with a high content of potential coiled-coil structure similar to myosin. Nuf2 is associated with the spindle pole body (SPB) as determined by coimmunofluorescence with known SPB proteins. Nuf2 appears to be localized to the intraNuclear region and is a candidate for a protein involved in SPB separation. The Nuclear association of Nuf2 can be disrupted, in part, by 1 M salt but not by the detergent Triton X-100. All Nuf2 can be removed from nuclei by 8 M urea extraction. In this regard, Nuf2 is similar to other SPB-associated proteins including Nufl/SPC110, also a coiled-coil protein. Temperature-sensitive alleles of NUF2 were generated within the coiled-coil region of Nuf2 and such NUF2 mutant cells rapidly arrest after temperature shift with a single undivided or partially divided nucleus in the bud neck, a shortened mitotic spindle and their DNA fully replicated. In sum, Nuf2 is a protein associated with the SPB that is critical for Nuclear Division. Anti-Nuf2 antibodies also recognize a mammalian 73-kd protein and display centrosome staining of mammalian tissue culture cells suggesting the presence of a protein with similar function.
Toshiya Endo - One of the best experts on this subject based on the ideXlab platform.
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nep98p is a component of the yeast spindle pole body and essential for Nuclear Division and fusion
Journal of Biological Chemistry, 2003Co-Authors: Shuhichi Nishikawa, Yumiko Terazawa, Tadashi Makio, Takeshi Nakayama, Aiko Hirata, Toshiya EndoAbstract:Abstract During the mating of yeast Saccharomyces cerevisiae, two haploid nuclei fuse to produce a diploid nucleus. This process requires the functions of BiP/Kar2p, a member of the Hsp70 family in the endoplasmic reticulum, and its partner protein, Jem1p. To investigate further the role of BiP and Jem1p in Nuclear fusion, we screened for partner proteins for Jem1p by the yeast two-hybrid system and identified Nep98p. Nep98p is an essential integral membrane protein of the Nuclear envelope and is enriched in the spindle pole body (SPB), the sole microtubule-organizing center in yeast. Temperature-sensitivenep98 mutant cells contain abnormal SPBs lacking the half-bridge, suggesting the essential role of Nep98p in the organization of the normal SPB. Additionally, nep98 mutant cells show defects in mitotic Nuclear Division and Nuclear fusion during mating. Because Jem1p is not required for Nuclear Division, Nep98p probably has dual functions in Jem1p-dependent karyogamy and in Jem1p-independent Nuclear Division.
