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  • Cell & Developmental Biology  (23)
  • Electronics and Electrical Engineering  (12)
  • 11
    Electronic Resource
    Electronic Resource
    Effect of tolbutamide on the metabolism of Tetrahymena (1974)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 83 (1974), S. 275-286 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Tolbutamide partially inhibited the growth but increased the glycogen content of Tetrahymena pyriformis in logarithmically growing cultures. Tolbutamide slightly increased 14CO2 production from [1-14C] and [6-14HC] glucose and [2-14C] pyruvate, but had little effect on the oxidation of [1-14C] acetate when any of these substrates were added to the proteose-peptone medium in which the cells had been grown. Measurement of 14CO2 production from [1-14C] and [2-I4C]-glyoxylate showed that this substrate was primarily oxidized via the glyoxylate cycle, with little if any oxidation occurring via the peroxisomal glyoxylate oxidase. Addition of tolbutamide inhibited the glyoxylate cycle as indicated by a marked reduction in label appearing in CO2 and in glycogen from labeled acetate. In control cells, addition of acetate strongly inhibited the oxidation of [2-14C]-pyruvate whereas addition of pyruvate had little effect on the oxidation of [1-14C]-acetate. Acetate was more effective than pyruvate in preventing the growth inhibitory and glycogen-increasing effects of tolbutamide. The data suggest that one effect of tolbutamide may be to interfere with the transfer of isocitrate and acetyl CoA across mitochondrial membranes.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1040830215
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  • 12
    Electronic Resource
    Electronic Resource
    Treatment with α-difluoromethylornithine plus a spermidine analog leads to spermine depletion and growth inhibition in cultured L1210 leukemia cells (1984)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 121 (1984), S. 476-482 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Of the three biological polyamines, putrescine (Put), spermidine (Spd), and spermine (Spm), the relevance of Spm to cell proliferation has yet to be defined because of our general inability to deplete it selectively in intact cells. In the present study, Spm depletion was accomplished by treating cultured L1210 cells for 96 hr with α-difluoromethylornithine (DFMO) and an analog of Spd such as aminopropylcadaverine. N4-methylSpd, N4-ethylSpd, or homoSpd. DFMO, a specific inhibitor of ornithine decarboxylase, halts continued polyamine biosynthesis and the Spd analog serves as a functional substitute for Spd. Thus, while the Spd analog fulfills the role(s) of Spd in cell proliferation, Spm becomes steadily depleted. In cells treated with DFMO plus the analog, aminopropylcadaverine, Spm pools decline steadily and growth inhibition occurs after 48 hr (when Spm pools decline to 60% of control). By 96 hr, Spm is ∼ 15% of control and growth is 〈 30%. Prevention studies with exogenous polyamines confirm a causai relationship between Spm depletion and growth inhibition. The critical levels of polyamines for cell proliferation to take place were found to be 30% of control for Spd and 60% for Spm. The use of DFMO plus a Spd analog is proposed as a system for studying the cellular consequences of Spm depletion. Spd depletion can be achieved for comparison purposes by treating cells with DFMO alone.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041210305
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  • 13
    Electronic Resource
    Electronic Resource
    In vitro proliferation and differentiation of hemic precursor cells from marrow and blood of naturally chimeric marmosetsSupported in part by United States Public Health Service grant R01 AMO 9289-04,05 AIB from the National Institutes of Health. (1972)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 79 (1972), S. 27-41 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Marmosets are unique in that they are “always” blood cell chimeras. When the nucleated cells from the bone marrow and from the peripheral blood of marmosets were incubated in the appropriate culture fluid they were shown capable of extensive proliferation in vitro. Two patterns of cellular proliferation, adherent and nonadherent, occurred in the same culture vessel. Repeated passage of nonadherent cells in RPMI 1640 medium supplemented with calf serum resulted in relatively long-term fluid bulk cultures showing myelocytic differentiation and megakaryocytic maturation. As myelocytic maturation became the predominant feature of cultures mitoses of the precursors diminished. About half of 41 marrow-derived cultures underwent extensive proliferation lasting about two months, as evidenced by an increasing cellularity and the presence of dividing cells. Such active growth occurred in one culture for over 120 days. The natural blood-cell chimerism of marmosets was demonstrated in vitro by cytogenetic analyses of metaphases from four relatively long term marrow cultures. The ratios of male and female cells remained either relatively stable or changed slowly with time in culture. Cells having both diploid and polyploid number of chromosomes were identified male or female, suggesting chimerism in myelocytic and megakaryocytic series. Marmoset lymph node and spleen cells proliferated as lymphoid cultures for various lengths of time up to five weeks but these cells did not differentiate into hemic cell lines. Attempts to culture human and rodent hemic tissue by the procedure used on marmoset tissue were unsuccessful.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1040790104
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  • 14
    Electronic Resource
    Electronic Resource
    Subunits of immunoglobulins and their relationship to antibody specificityResearch sponsored by the U.S. National Science Foundation and the Medical Research Council, London. (1966)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 67 (1966), S. 51-64 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Subunits of immunoglobulins have been prepared by two methods, both of which have contributed to our knowledge of the structural basis of antibody specificity. The first method is enzymic hydrolysis with either papain or pepsin and leads to the unequivocal conclusion that each combining site is contained in a fragment (Fab) of about 45,000 molecular weight and formed from the light chain and the N-terminal half of the heavy chain, the Fd fragment. The second method of preparing subunits is to reduce the interchain disulfide bonds and to isolate the chains. This should decide whether the combining site is in the Fd fragment, the light chain, or is formed jointly by both. In fact, considerable loss of affinity for the antigen follows, whatever technique is used to dissociate the peptide chains and, although many papers have been published on this subject, no definite answer has yet been obtained. Although the majority opinion probably favors the view that both chains are concerned in the formation of the combining site, our tentative conclusion is that the site is placed entirely in the heavy chain and that the light chain has only a semispecific role in facilitating the reformation of the native configuration of the heavy chain after its disruption under the conditions necessary for dissociation of the two chains.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1040670407
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  • 15
    Electronic Resource
    Electronic Resource
    Identification of surface autoantigens which appear during spermatogenesis (1982)
    New York, NY : Wiley-Blackwell
    Gamete Research 5 (1982), S. 35-48 
    Details
    ISSN: 0148-7280
    Keywords: autoantigens ; spermatogenesis ; rabbit ; antigens ; membrane proteins ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Autoantigens that appear during spermatogenesis in the rabbit were identified using immunoadsorbent chromatography and SDS-PAGE. To identify cell-surface proteins, samples of freshly isolated, staged cells were labeled by the lactoperoxidase or Iodo-Gen iodination procedure and run on SDS-PAGE. Autoradiograms of the stained, dried gels were prepared. By correlating the band patterns in the SDS gels of immunocolumn and surface-labeled samples with the band patterns in the autoradiograms, it was possible to show when the autoantigenic proteins appeared on the cell surface. To further support the identification of membrane autoantigens, surface-labeled, staged cell samples were lysed in Triton X-100 and immunoprecipitated with antitestis cell autoantisera.Three types of autoantigens have been identified: (1) late class antigens that are present only on late spermatids and epididymal spermatozoa, but are intracellular in early stages, (2) early class antigens which occur on the surface of pachytene spermatocytes and are present throughout subsequent stages of development, and (3) early class, transient antigens, which appear on spermatogenic cells but are not present on epididymal spermatozoa.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1120050105
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  • 16
    Electronic Resource
    Electronic Resource
    An attempt to fatigue the melanophore system in Fundulus and a consideration of lag in melanophore responses (1937)
    Philadelphia : Wiley-Blackwell
    Journal of Cellular and Comparative Physiology 9 (1937), S. 315-329 
    Details
    ISSN: 0095-9898
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1030090303
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  • 17
    Electronic Resource
    Electronic Resource
    Novel monoclonal antibodies identify antigenic determinants unique to cellular senescence (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 142 (1990), S. 425-433 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Normal human diploid fibroblasts exhibit a limited lifespan in vitro and are used as a model to study in vivo aging. Monoclonal antibodies were generated against partially purified surface membranes from human diploid fibroblasts at the end of their lifespan (senescent). Three hybridomas were isolated that secreted antibodies reacting to cellular determinants expressed specifically on senescent human fibroblasts of different origin, including neonatal foreskin, embryonic lung, and adult skin punch biopsy, but not expressed on matched young cells. The antibodies did not bind to immortal human cells and normal young cells made reversibly nondividing, indicating the antigens are not expressed in cells that are not senescent. The antibodies identified senescent cells in a mixed cell population and expression of the senescent cell antigens correlated strongly with the cells inability to synthesize DNA at the onset of senescence. The antigens appeared to be cell surface or extracellular matrix associated, and the epitopes were destroyed by mild trypsin treatment. Western analysis indicated all three antibodies reacted with fibronectin. Though the antigenic determinants on the fibronectir molecule were not accessible in the intact young cell, the epitopes were present in fibronectin extracted from both senescent and young cells, as well as purified human plasma fibronectin. These antibodies and the senescent specific expression of the antigens provide powerful tools to investigate the mechanisms leading to in vitro senescence. This may enable us to investigate directly the relationship between cellular aging and aging of the individual.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041420228
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  • 18
    Electronic Resource
    Electronic Resource
    Regulation of polyamine transport by polyamines and polyamine analogs (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 155 (1993), S. 399-407 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Regulation of polyamine transport in murine L1210 leukemia cells was characterized in order to better understand its relationship to specific intracellular polyamines and their analogs and to quantitate the sensitivity by which it is controlled. Up-regulation of polyamine uptake was evaluated following a 48-hr treatment with a combination of biosynthetic enzyme inhibitors to deplete intracellular polyamine pools. The latter declined gradually over 48 hr and was accompanied by a steady increase in spermidine (SPD) and spermine (SPM) transport as indicated by rises in Vmax to levels ∼4.5 times higher than control values. Restoration of individual polyamine pools during a 6-hr period following inhibitor treatment revealed that SPD and SPM uptake could not be selectively affected by specific pool changes. The effectiveness of individual polyamines in reversing inhibitor-induced stimulation of uptake was as follows: putrescine 〈 SPD 〈 SPM = the SPM analog, N1, N12-bis(ethyl)spermine (BESPM). In contrast to stimulation of transport, down-regulation by exogenous polyamines or analogs occurred rapidly and in response to subtle increases in intracellular pools. Following a 1-hr exposure to 10 μM BESPM, Vmax values for SPD and SPM fell by 70%, whereas the analog pool increased to only 400-500 pmol/106 cells - about 15-20% of the total polyamine pool (∼2.8 nmol/106 cells). SPM produced nearly identical regulatory effects on transport kinetics. Both BESPM and SPM were even more effective at down-regulating transport that had been previously stimulated four to fivefold by polyamine depletion achieved with enzyme inhibitors. A dose response with BESPM at 48 hr revealed a biphasic effect on uptake whereby concentrations of analog 〈 3 μM produced an increase in SPD and SPM Vmax values, whereas concentrations 3 μM and higher produced a marked suppression of these values. Cells treated with 3 μM BESPM for 2 hr and placed in analog-free medium recovered transport capability in only 3 hr. Thus, whereas stimulation of polyamine transport is a relatively insensitive and slowly responsive process that tends to parallel polyamine depletion, down-regulation of polyamine transport by exogenous polyamines and analogs and its reversal are rapidly responsive events that correlate with relatively small (i.e., 15-20%) changes in intracellular polyamine pools.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041550222
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  • 19
    Electronic Resource
    Electronic Resource
    Vanadate reduces sodium-dependent glucose transport and increases glycolytic activity in LLC-PK1 epithelia (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 158 (1994), S. 459-466 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The effect of vanadate pentoxide on apical sodium-dependent glucose transport in LLC-PK1 epithelia was examined. Epithelia grown in the presence or absence of 1 μM vanadate formed confluent monolayers and exhibited no differences in DNA, protein, or ultrastructure. Vanadate-supplemented epithelia demonstrated a lower steady-state α-methyl-D-glucopyranoside (AMG) concentrating capacity and a twofold reduction in apical AMG uptake Jmax. This decreased AMG transport occurred as a consequence of a reduction in the number of transport carriers and was not associated with a change in the sodium electrochemical gradient. The vanadate-induced reduction in apical glucose carrier functional activity and expression was accompanied by a stimulation of intracellular glycolytic flux activity, as evidenced by increased glucose consumption, lactate production, PFK-1 activity, and intracellular ATP. There was no difference in intracellular cAMP levels between vanadate-supplemented and non-supplemented epithelia. These results demonstrate an association between stimulation of glycolytic pathway activity and an adaptive response in the form of a reduction in the function and expression of the sodium-dependent apical glucose transporter in LLC-PK1 epithelia. © 1994 Wiley-Liss, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041580310
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  • 20
    Electronic Resource
    Electronic Resource
    Common senescent cell-specific antibody epitopes on fibronectin in species and cells of varied origin (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 150 (1992), S. 545-551 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The phenomenon of in vitro cellular senescence has been demonstrated in cultured cells derived from humans and various other species. We have previously shown that monoclonal antibodies SEN-1, SEN-2, and SEN-3 react to epitopes on fibronectin that are exposed when human diploid fibroblasts become senescent. We here present results demonstrating that exposure of these epitopes is specific to senescence for a variety of human cells: epidermal keratinocytes, mammary epithelial cells, as well as fibroblasts. Fibronectin from 11 additional species was also analyzed by Western immunoblot for ability to bind the SEN antibodies. SEN-1 bound only human and gorilla fibronectin, whereas SEN-2 and SEN-3 bound fibronectin from those two species as well as the horse, cow, sheep, goat, dog, and chick. None of the antibodies reacted with fibronectin from the rabbit, rat, or mouse. These data indicated a correlation between the ability of the SEN antibodies to bind fibronectin from a particular species and the ability of cells from that species to exhibit a stable senescent phenotype in vitro. Therefore, exposure of this region of fibronectin may be important in the establishment and maintenance of cellular senescence. In addition, the ability of the SEN antibodies to react with fibronectin from a variety of senescent cells emphasizes their usefulness as markers for cellular senescence.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041500315
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