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  • Cell & Developmental Biology  (18)
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  • 1995-1999  (11)
  • 1965-1969  (16)
  • 1
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Gland cells of the gastrodermis of Hydra when isolated from the epidermis are capable of dedifferentiating into interstitial cells. Under proper environmental conditions these interstitial cells are capable of undergoing meiotic divisions and forming normal gametes. This dedifferentiation and redifferentiation sequence has been studied at the level of the light and electron microscope. It is concluded that in Hydra there is no specific germinal cell line determined during embryogeny, and that a somatic cell under proper environmental conditions can be induced to undergo meiosis.
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Journal of Morphology 125 (1968), S. 61-70 
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Two complete composite photographs of the optic nerve of Limulus, made by electron microscopy, reveal the presence of neurosecretory granules in the large axons of the rudimentary eye neurons. The number of intermediate sized, (3-7 μ), of eccentric cells corresponds with the number of ommatidia as expected, but only their sheath of Schwann cells show an intimate interfolding. Based on the number of fine axons within the nerve each ommatidium has an average of 12-13 retinular cells. The diameter of their fibers is between 0.2 and 3 μ although the majority are between 1 and 1.5 μ. They are aggregated into bundles of six to seven fibers by the sheath cells although some bundles contain only two, others as many as 181 fibers. There is no indication in these studies that retinular cell axons within a bundle are associated with the same, adjacent, or other pattern of ommatidia. The photographs suggest that physiological activity in retinular cell axons might be detected most easily in the smallest bundles because they contain the fewest, but the larger retinular cell axons.
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  • 3
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Function and ultrastructure of the excretory organs (antennal glands) of the shore crab Uca mordax were investigated. The crabs were maintained at three different salinities: 50%, 100% and 200% seawater. In spite of previous reports to the contrary, the investigation showed that the powerful osmoregulatory ability found in Uca mordax is not due to participation of the antennal glands. Freezing point depression of urine under all conditions was found to be slightly less than that of the hemolymph, indicating a slightly hypoosmotic urine. It was further found that the antennal gland is extremely effective in resorbing sodium from the filtrate. The higher the salinity to which the crabs were acclimated the lower the sodium concentration in the urine. No water was resorbed from the filtrate as shown by the fact that the inulin U/P ratio remained unity regardless of the salinity to which the crabs were adapted. Electronmicroscopy of the antennal glands revealed that the coelomosac cells are similar to the podocytes described in the crayfish by Kümmel ('64), and the coelomosac appears to be a typical filtration organ. The cells of the labyrinth showed brush border and very elaborate basal infoldings with numerous mitochondria. The deep cytoplasmic infoldings which represent interdigitations with neighboring cells may be correlated with the effective sodium reabsorption in the labyrinth, but apparently not with water movement.
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Journal of Morphology 124 (1968), S. 79-82 
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A total of 1125 normal chick embryos, representing 25 each of the 45 stages of Hamburger and Hamilton, were removed, fixed in Bouin's solution, stored in 70% ethanol and weighed with a semi-micro analytical balance. Entire blastoderms of stages 1-8 were weighed, whereas only embryos-proper were weighed in stages 9-45. As a consequence, results constituted two groups, each of which showed a geometric rate of growth marked only by minor deviations which were related to specific events of normal growth and development.
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 30 (1995), S. 285-300 
    ISSN: 0886-1544
    Keywords: microtubule dynamics ; β-tubulin ; mitosis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Microtubule (MT) dynamics vary both spatially and temporally within cells and are thought to be important for proper MT cellular function. Because MT dynamics appear to be closely tied to the guanosine triphosphatase (GTPase) activity of β-tubulin subunits, we examined the importance of MT dynamics in the budding yeast S. cerevisiae by introducing a T107K point mutation into a region of the single β-tubulin gene, TUB2, known to affect the assembly-dependent GTPase activity of MTs in vitro. Analysis of MT dynamic behavior by video-enhanced differential interference contrast microscopy, revealed that T107K subunits slowed both the growth rates and catastrophic disassembly rates of individual MTs in vitro. In haploid cells tub2-T107K is lethal; but in tub2-T107K/tub2-590 heterozygotes the mutation is viable, dominant, and slows cell-cycle progression through mitosis, without causing wholesale disruption of cellular MTs. The correlation between the slower growing and shortening rates of MTs in vitro, and the slower mitosis in vivo suggests that MT dynamics are important in budding yeast and may regulate the rate of nuclear movement and segregation. The slower mitosis in mutant celis did not result in premature cytokinesis and cell death, further suggesting that cell-cycle control mechanisms “sense” the mitotic slowdown, possibly by monitoring MT dynamics directly. © 1995 Wiley-Liss, Inc.
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  • 6
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 64 (1997), S. 499-504 
    ISSN: 0730-2312
    Keywords: protein kinase CK2 ; nuclear matrix ; cytoskeleton ; chromatin ; intermediate filaments ; core filaments ; carcinoma ; prostate ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Nuclear matrix (NM) plays roles of fundamental structural and functional significance as the site of replication, transcription, and RNA processing and transport, acting as an anchor or attachment site for a variety of enzymes and other proteins involved in these activities. We have previously documented that protein kinase CK2 translocates from the cytosol to the nucleus, where it associates preferentially with chromatin and NM, in response to certain growth stimuli. Considering that characteristics of the isolated NM can depend on the procedure employed for its isolation, we compared three standard methods for NM preparation to confirm the association of intrinsic CK2 with this structure. Our data suggest that the method used for isolating the NM can quantitatively influence the measurable NM-associated CK2. However, all three methods employed yielded qualitatively similar results with respect to the stimulus-mediated modulation of NM-associated CK2, thus further supporting the notion that NM is an important site for physiologically relevant functions of CK2. In addition, core filaments and cytoskeleton that were isolated by two of the preparative methods had a small but significant level of associated CK2 activity. J. Cell. Biochem. 64:499-504. © 1997 Wiley-Liss, Inc. This article is a U.S. Government work and, as such, is in the public domain in the United States of America.
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  • 7
    ISSN: 0730-2312
    Keywords: phosphorylation ; interferon regulatory factor 2 ; transcription factor ; oncogene ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: IRF2 is a transcription factor, possessing oncogenic potential, responsible for both the repression of growth-inhibiting genes (interferon) and the activation of cell cycle-regulated genes (histone H4). Surprisingly little is known about the post-translational modification of this factor. In this study, we analyze the phosphorylation of IRF2 both in vivo and in vitro. Immunoprecipitation of HA-tagged IRF2 expressed in 32P-phosphate labelled COS-7 cells demonstrates that IRF2 is phosphorylated in vivo. Amino acid sequence analysis reveals that several potential phosphorylation sites exist for a variety of serine/threonine protein kinases, including those of the mitogen activated protein (MAP) kinase family. Using a battery of these protein kinases we show that recombinant IRF2 is a substrate for protein kinase A (PKA), protein kinase C (PKC), and casein kinase II (CK2) in vitro. However, other serine/threonine protein kinases, including the MAP kinases JNK1, p38, and ERK2, do not phosphorylate IRF2. Two-dimensional phosphopeptide mapping of the sites phosphorylated by PKA, PKC, and CKII in vitro demonstrates that these enzymes are capable of phosphorylating IRF2 at multiple distinct sites. Phosphoaminoacid analysis of HA-tagged IRF2 immunoprecipitated from an asynchronous population of proliferating, metabolically phosphate-labelled cells indicates that this protein is phosphorylated exclusively upon serine residues in vivo. These results suggest that the oncogenic protein IRF2 may be regulated via multiple pathways during cellular growth. J. Cell. Biochem. 66:175-183, 1997. © 1997 Wiley-Liss, Inc.
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  • 8
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 65 (1997), S. 308-324 
    ISSN: 0730-2312
    Keywords: PO-B ; HL-60 ; differentiation ; AP-1 ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: PO-B was originally characterized as a transcriptional regulatory factor of the pro-opiomelanocortin (POMC) gene; however, it has become increasingly clear that this protein may be active in tissues outside the pituitary, since it is present in diverse cell types, including differentiated HL-60 promyelocytic leukemia cells. We previously showed that PO-B DNA-binding is progressively induced during differentiation of promyelomonocytic leukemia HL-60 cells to the macrophage-like lineage (with phorbol esters). We now report that PO-B DNA-binding in HL-60 cells is similarly induced during differentiation to the granulocytic lineage (with either retinoic acid or dimethylsulfoxide). Either a genetic or pharmacologic blockade of HL-60 differentiation prohibited these inductive effects. These studies have prompted our interest in the dynamics of other transcription factor changes during HL-60 differentiation. Of these, we observed that another transcription factor (AP-1) is also robustly induced at the DNA-binding level during macrophagelike HL-60 differentiation, but not during granulocytic differentiation. Conversely, the DNA-binding of the transcription factor AP-2 was slightly reduced by TPA-induced HL-60 differentiation but unchanged during granulocyte differentiation. From these data, we conclude that the induction of PO-B DNA binding is a general marker of HL-60 myelomonocytic differentiation, but that qualitative aspects of the induction of additional distinct transcription factors, such as AP-L may contribute to lineage-specific determinants of cell fate. J. Cell. Biochem. 65:308-324. © 1997 Wiley-Liss, Inc.
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  • 9
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 69 (1998), S. 211-220 
    ISSN: 0730-2312
    Keywords: nuclear matrix ; protein kinase CK2 ; disulfide bonds ; sodium tetrathionate ; iodoacetamide ; sulfhydryl crosslinking ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Nuclear matrix (NM) appears to be an intranuclear locale for significant and dynamic association of the ubiquitous multifunctional messenger-independent serine/threonine protein kinase CK2 that has been implicated in growth control [Tawfic et al. (1996): J Cell Biochem 61:165-171]. We have examined the nature of the association of CK2 with the NM. Nuclei prepared in the presence of a sulfhydryl-blocking reagent such as iodoacetamide demonstrate a reduction in the amount of CK2 associated with the NM to less than 5% of the control. On the other hand, when nuclei are treated with the sulfhydryl crosslinking reagent sodium tetrathionate, NM-associated CK2 increases severalfold. Treatment of nuclei with sodium tetrathionate followed by 2-mercaptoethanol blocks this increase. Nuclei isolated from rat liver and prostate behaved similarly, suggesting an identical mode of association of CK2 with the NM regardless of the organ. These results indicate a role of sulfhydryl interactions such that NM anchoring of CK2 occurs via its β subunit, which contains several vicinal cysteine residues. Further, various sulfhydryl-blocking reagents inhibited CK2 activity in a concentration-dependent manner, and the inhibitory effect was reversed by agents such as dithiothreitol, implying that cysteine residues in the CK2 play a role in its catalytic activity. J. Cell. Biochem. 69:211-220, 1998. Published 1998 Wiley-Liss, Inc.
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  • 10
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 67 (1997), S. 1-12 
    ISSN: 0730-2312
    Keywords: DPP ; Drosophila ; mutations ; dorsal closure signaling pathway ; JNK pathway ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The dorsal surface of the Drosophila embryo is formed by the migration of the lateral epithelial cells to cover the amnioserosa. The Drosophila cJun-N-terminal kinase (DJNK) is essential for this process. Mutations in DJNK or the DJNK activator hemipterous (HEP) lead to incomplete dorsal closure, resulting in a hole in the dorsal cuticle. The molecules downstream of DJNK in this signaling pathway have not been established. Here we demonstrate that the basket1 (bsk1) mutation of DJNK causes decreased interaction with DJUN. Expression of decapentaplegic (DPP), a TGF-β homologue, in the leading edge of the dorsal epithelium, is identified as a genetic target of the JNK pathway. A constitutive allele of JUN is able to rescue the dorsal closure defect of bsk1 and restores DPP expression. Furthermore, ectopic DPP rescues the defects in dorsal closure caused by bsk1. These data indicate that the interaction of DJNK with DJUN contributes to the dorsal closure signaling pathway and targets DPP expression. J. Cell. Biochem. 67:1-12, 1997. © 1997 Wiley-Liss, Inc.
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