• Title/Summary/Keyword: Amoeba proteus

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Effect of Exogenous ATP and ionic Concentration on the Activity of Contractile Vacuoles in Amoeba proteus (배양액의 ATP첨가 및 이온 농도에 따른 Amoeba proteus 수축포의 배출작용)

  • 최범선;주윤수안태인
    • The Korean Journal of Zoology
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    • v.34 no.4
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    • pp.452-459
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    • 1991

  • 담수산 대형 아메바인 각moeba proteus의 위상차 현미경 관찰 및 사진 분석을 통하여 수축포의 배출활동을 조사하f:다. Chalkley's 무기 염류 배양액에 첨가한 0. 1 mM ATP(disodium salt)에 의해 수축포의 배출속도는 270%로 증가하f:으며, 이 ATP의 효과는 Na+ 이온농도가 0.46mM 이상일 때 유효하였다. 실험용액의 NaGl 농도를 10 mM까지 증가시켰을 때 배출작용은 230%에 이르기까지 완만한 직선적 증가를 보였으며, 0.1 mM ATP를 첨가했을 때는 소폭의 NaCl농도 증가(0.50 mM)에 대하여 급격한 상승을 보였다. 이 배출 촉진은 Na+이온에 대해서 선별적으로 이루어졌으며 K+이온으로는 대체될 수 없었다. 배출속도는 Cac12를 제외한 Chalkley's 액에 50 $\mu$ M EDTA(disodium)를 첨가하였을 때에는 2900ye로 증가하였으며 , Caclf 농도가 증가됨에 따라 현격한 감소를 보였다. Chalkley's용액의 Cac12, NaCl을 함께 제외한 경우 배출속도는 대조군 수준에 미달된 데 비하여 0.2 mM Cac12, 10 mM NaCl첨가시에는 대조군의 180%였다. 아메바 수축포의 배출작용이 Na+이온 배출기구로 보고(Pottier efaf., 1987) 이들 결과를 종합해 볼때 아메바의 세포막에는 Na+ 이온의 투과수단으로 칼슘제거에 의해서 촉진확산되는 것과 Na+이온 농도증가에 따른 단순확산이 있을 것으로 사료된다.

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Immunofluorescence Microscopy and Biochemical Characterization of Two Nuclear Envelope Proteins of Amoeba proteus by Using a Monoclonal Antibody (단항체를 이용한 아메바(Amoeba proteus) 의 2종 핵막 단백질에 대한 면역형광현미경적 및 생화학적 특성 조사)

  • 안태인;유시욱조양래
    • The Korean Journal of Zoology
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    • v.34 no.1
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    • pp.44-53
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    • 1991

  • Distribution of the antigens during the cell cycle of amoebae was followed by immunof-luorescence microscopy using a monoclonal antibody against the nucleus as a probe. While the cells were in the interphase, the antigen was localized on the nucleus membrane. But it was dispersed all over the cytoplasm during mitosis and cytokinesis. The molecular weights of the immunoreacted antigens were 210 KD and 190 KD as determined by SDS PAGE and western blotting of the purified nuclei. The antigens were not soluble in non-ionic detergent, but were released from the nucleus by incubation with 0.05 M sodium carbonate, pH 10.6 or with 8 M urea at serial chemical extraction. Thus the antigens appeared to be peripheral proteins of the nurBeus envelope. The isoelectic point of both antigens was 7.64 as determined by 2 D PAGE and transfer blotting. Considering the peiipherd association with the nucleus membrane and the dispersed distribution during mitosis, the antigens could be lamin like proteins. Hourever, it appears also possible that they are the component molecules of the unusually structured aurous lamina of amoeba nucleus since they have the large molecular weight and the basic pl.

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Loss of a Strain-Specific Protein by Bacterial Infection in Amoeba proteus (Amoeba proteus에 있어서 박테리아 감염에 의한 변이주 특이성 단백질의 손실)

  • Ahn, Tae-In;Park, Eui-Yul
    • The Korean Journal of Zoology
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    • v.28 no.1
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    • pp.21-30
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    • 1985

  • By two-dimensional gel electrophoresis loss of a cell-specific protein was detected in tD strain of Amoeba proteus that had been infected by symbiotic bacteria extracted from xD strain. In 50 days of experimental infection by induced phagocytosis the host amoeba lost the ability to synthesize the tD cell-specific protein even after removal of the infective bacteria and xD cell-specific protein by growing the amoebae at $27^\\circC$. By this time the host amoebae were obligately dependent on the bacteria. From these and other results (Lorch and Jeon, Science 221:549), it is clear that the incompatibility of the infected nuclei with the cytoplasm of the uninfected amoeba and the obligate dependence of the host on bacteria are due to the irreversible inactivation or the loss of the cell-specific gene by bacterial infection in this amoeba.

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The Fate of Strain-Specific Protein in xD Strain of Amoeba proteus (Amoeba proteus xD Strain의 변이주 특이성 단백질의 운영)

  • 안태인
    • The Korean Journal of Zoology
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    • v.26 no.3
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    • pp.181-192
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    • 1983

  • Cytosol protein patterns of two strains of A. proteus, tD and xD strain, were compared by two dimensional gel electrophoresis. Among the 200 major polypeptides that could be stained by silver stain method, tD strain contained a cell specific protein whose molecular weight was 45,000 dalton, pI 5.9. On the other hand, the cytosol and the symbiotic vesicles of xD strain contained a symbiosis specific protein (M.W. 29,000; pI 5.5). The fate of the symbiosis specific protein depended on the presence of symbiotic bacteria in the experiment of high temperature effect and of experimental infection. The significance of these results is discussed in relation to their function in organismic association on the basis of the previous findings.

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Characterization of Ubiquitinated Lysosomal Membrane Proteins in Acanthamieba castellanii

  • Oh, Sekyung;Ahn, Tae-In
    • Animal cells and systems
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    • v.4 no.2
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    • pp.165-171
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    • 2000

  • Ubiquitinated proteins in lysosomes were characterized by using two monoclonal antibodies (mAbs): LYS8-1, a mAb to lysosomal proteins, and NYA124, a mAb to ubiquitin. LYS8-1 stained lysosome-like vesicles in immunofluorescence microscopy of Amoeba proteus and Acanthamoeba castellanii. In immunoblotting, LYS8-1's antigens (LYS proteins) were detected as 68-kDa and 77-kDa proteins in A. proteus, and as 30-kDa and 39-kDa proteins in A. castellanii. In immunoprecipitation of A. castellanii, at least four distinct LYS proteins, LVS35p, LyS39p, LyS42p, and LYS46p, were detected and accumulated upon inhibition of lysosome functions but not upon that of 26S proteasome functions. They were all found to be ubiquitinated, and were recovered in the lysosome fractions in subcellular fractionation experiments. In chemical fractionation analyses, LYS35p and LYS39p were demonstrated to be peripherally associated with lysosome membrane, while LYS42p and LYS46p tightly bound to the membrane. These results suggest that the LYS proteins become associated to lysosomal membrane upon ubiquitination.

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