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  • General Chemistry  (99)
  • Cell & Developmental Biology  (38)
  • 2010-2014
  • 2000-2004
  • 1995-1999  (137)
  • 1955-1959
  • 1950-1954
  • 1997  (137)
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  • 2010-2014
  • 2000-2004
  • 1995-1999  (137)
  • 1955-1959
  • 1950-1954
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  • 1
    Electronic Resource
    Electronic Resource
    Analysis of epitope structure of PSP94 (prostate secretory protein of 94 amino acids): (II) epitope mapping by monoclonal antibodies (1997)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 65 (1997), S. 186-197 
    Details
    ISSN: 0730-2312
    Keywords: epitope mapping ; monoclonal antibodies ; linear epitope ; immuno-dominant ; immuno-recessive ; ELISA ; competitive ELISA ; recombinant GST-PSP94 ; N-terminal and C-terminal peptides ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: PSP94 has shown potential to be a serum biomarker for evaluating prostate cancer. Studies of the epitope structure is crucial for this endeavour. In this article, we have used 15 different monoclonal antibodies (MAb) to analyse the epitope structure of PSP94 and to compare with the results obtained from our previous work using polyclonal antibody and recombinant PSP94. Firstly, we determined the relative activities of the 15 MAb population by direct and competitive ELISA. The two predominant MAbs (MAb PSP-6 and -19) in 15 MAbs were selected for further studies of the epitope structure. By comparing the binding activities of recombinant GST-PSP94 and natural PSP94 with MAbs, and by comparing their affinity with MAbs in an in vitro denaturing experiment, PSP94 was shown to have a similar, prevalently linear epitope structure as we demonstrated by polyclonal antibody. Using recombinant GST fusion protein with PSP94 and with each half of the N- and C-terminal 47 amino acids (GST-PSP-N47/C47) in E. coli cells, the different epitopes recognized by 15 monoclonal antibodies were delineated and the polar distribution of the epitope structure of PSP94 was characterized. Results of direct ELISA of recombinant N47 and C47 and their competitive binding against natural PSP94 (competitive ELISA) showed that the N- and C-termini represent the immuno-dominant and immuno-recessive area separately. A majority of the monoclonal antibodies (12/15) showed preferential binding of the N-terminal sequence of the PSP94 protein. Using GST-PSP-N47 as a standard protein, an epitope map of the 15 monoclonal antibodies was obtained. The results of this study will help to define the clinical utility of PSP94. J. Cell. Biochem. 65:186-197. © 1997 Wiley-Liss, Inc.
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  • 2
    Electronic Resource
    Electronic Resource
    Altered cell shape is linked to increased p34cdc2 gene expression in fibroblasts expressing a mutant E2F-1 transcription factor (1997)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 65 (1997), S. 83-94 
    Details
    ISSN: 0730-2312
    Keywords: E2F1 ; E2F1d87 ; NIH3TH ; fibroblasts ; p34cdc2 ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The E2F1 transcription factor or an amino terminal deletion mutant termed E2F1d87 was constitutively expressed in NIH3T3 fibroblasts. Cells expressing wild-type E2F1 display a morphology indistinguishable from that of normal fibroblasts. However, the E2F1d87-expressing cells exhibited a distinct rounding during culture in media containing 10% calf serum. The morphology change was most pronounced during S phase, which was considerably lengthened in the E2F1d87-expressing cells. Consistent with this rounded shape, the E2F1d87-expressing cells have significantly increased levels of both p34cdc2 mRNA and protein. Also observed was an increase in active p34cdc2 in immunoprecipitates from extracts of the E2F1d87 cell line, as assayed by histone H1 kinase assay. The upregulation of p34cdc2 expression occurs at the transcriptional level and requires ectopic E2F1d87 along with serum growth factor stimulation, since culture of these cells in low serum media results in a flattened shape and a drop in p34cdc2 expression compared to that of the control cells. J. Cell. Biochem. 65:83-94. © 1997 Wiley-Liss, Inc.
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  • 3
    Electronic Resource
    Electronic Resource
    [(TptBu, Me)CrR]: A New Class of Mononuclear, Coordinatively Unsaturated Chromium(II) Alkyls with cis-Divacant Octahedral Structure (1997)
    Weinheim : Wiley-Blackwell
    Chemistry - A European Journal 3 (1997), S. 1668-1674 
    Details
    ISSN: 0947-6539
    Keywords: alkenes ; chromium ; cis-divacant octahedral geometry ; polymerizations ; tris(pyrazolyl)borate complexes ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Reaction of CrCl2 with TptBu, MeK yielded [TptBu, MeCr(3-tBu, 5-MepzH)Cl] (1) and [TptBu, MeCrCl] (2), while the same reaction in the presence of pyridine gave 1 and [TptBu, MeCr(py)Cl] (3). Alkylation of 3 with Grignard reagents produced the chromium(II) alkyls [TptBu, MeCrR] (4, R = Et; 5, R = Ph; 6, R = CH2SiMe3), which reversibly added to pyridine to form the five-coordinate adducts [TptBu, MeCr(py)R] (7, R = Et; 8, R = Ph; 9, R = CH2SiMe3). 1, 2, 4, and 5 were structurally characterized by X-ray diffraction. The four-coordinate molecules 2, 4, and 5 adopt a highly unusual cis-divacant octahedral coordination geometry, while 1 is the first five-coordinate TptBu, Me-complex of a first-row transition metal. Despite their coordinative unsaturation, chromium alkyls 4-6 do not polymerize ethylene, or even react with it. This observation is inconsistent with the catalytic activity commonly ascribed to divalent chromium in heterogeneous polymerization catalysts. Attempts to oxidize 4-6 (e.g., with [Cp2Fe]BPh4) to cationic chromium(II) alkyls failed, yielding [TptBu, MeCr(thf)][BPh4] (10) instead.
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    URL: http://dx.doi.org/10.1002/chem.19970031016
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  • 4
    Electronic Resource
    Electronic Resource
    Detection of a proliferation specific gene during development of the osteoblast phenotype by mRNA differential display (1997)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 64 (1997), S. 106-116 
    Details
    ISSN: 0730-2312
    Keywords: osteoblasts ; proliferation ; growth control ; differential display ; differentiation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Fetal rat calvarial-derived osteoblasts in vitro (ROB) reinitiate a developmental program from growth to differentiation concomitant with production of a bone tissue-like organized extracellular matrix. To identify novel genes which may mediate this sequence, we isolated total RNA from three stages of the cellular differentiation process (proliferation, extracellular matrix maturation, and mineralization), for screening gene expression by the differential mRNA display technique. Of 15 differentially displayed bands that were analyzed by Northern blot analysis, one prominent 310 nucleotide band was confirmed to be proliferation-stage specific. Northern blot analysis showed a 600-650 nt transcript which was highly expressed in proliferating cells and decreased to trace levels after confluency and throughout the differentiation process. We have designated this transcript PROM-1 (for proliferating cell marker). A full length PROM-1 cDNA of 607 bp was obtained by 5′ RACE. A short open reading frame encoded a putative 37 amino acid peptide with no significant similarity to known sequences. Expression of PROM-1 in the ROS 17/2.8 osteosarcoma cell line was several fold greater than in normal diploid cells and was not downregulated when ROS 17/2.8 cells reached confluency. The relationship of PROM-1 expression to cell growth was also observed in diploid fetal rat lung fibroblasts. Hydroxyurea treatment of proliferating osteoblasts blocked PROM-1 expression; however, its expression was not cell cycle regulated. Upregulation of PROM-1 in response to TGF-β paralleled the stimulatory effects on growth as quantitated by histone gene expression. In conclusion, PROM-1 represents a small cytoplasmic polyA containing RNA whose expression is restricted to the exponential growth period of normal diploid cells; the gene appears to be deregulated in tumor derived cell lines. J. Cell. Biochem. 64:106-116. © 1997 Wiley-Liss, Inc.
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  • 5
    Electronic Resource
    Electronic Resource
    Differentiation of human trophoblast cells in vitro is inhibited by dimethylsulfoxide (1997)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 65 (1997), S. 460-468 
    Details
    ISSN: 0730-2312
    Keywords: placenta ; planar-polar compounds ; hCG ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Dimethyl sulfoxide (DMSO) exerts a number of biological effects, the most frequently cited being induction of cell differentiation. The compound also increases invasiveness and metastatic potential. In contrast to the many reports of DMSO-induced cell differentiation, we report here that DMSO inhibits the morphological differentiation of human cytotrophoblast cells to syncytiotrophoblast, as revealed by immunofluorescence staining for desmosomal protein and nuclei. Cytotrophoblast cells treated with DMSO under differentiation-inducing conditions remained mononucleated with intense desmosomal staining. The effect was dose dependent, with a maximal effect seen at 1.5% DMSO. Concentrations of ≤0.5% had no effect and concentrations 〉2% were cytotoxic. In addition to these morphological changes, DMSO inhibited secretion of human chorionic gonadotropin in a dose-dependent manner. At a concentration of 1.5%, DMSO inhibited secretion by 70%. If cytotrophoblast cells were cultured in the presence of DMSO and then switched to DMSO-free medium, they proceeded to differentiate normally. While the precise mechanism of action remains unknown, judicious use of DMSO may be a useful tool for studying and manipulating the differentiation of human trophoblast cells in vitro. The findings also indicate that care should be used in interpreting results obtained using DMSO as a carrier in drug and inhibitor studies. J. Cell Biochem. 65:460-468. © 1997 Wiley-Liss Inc.
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  • 6
    Electronic Resource
    Electronic Resource
    Subcellular partitioning of transcription factors during osteoblast differentiation: Developmental association of the AML/CBFα/PEBP2α-related transcription factor-NMP-2 with the nuclear matrix (1997)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 66 (1997), S. 123-132 
    Details
    ISSN: 0730-2312
    Keywords: AML-3 ; transcription factors ; partitioning ; osteoblast differentiation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The subnuclear location of transcription factors may functionally contribute to the regulation of gene expression. Several classes of gene regulators associate with the nuclear matrix in a cell type, cell growth, or cell cycle related-manner. To understand control of nuclear matrix-transcription factor interactions during tissue development, we systematically analyzed the subnuclear partitioning of a panel of transcription factors (including NMP-1/YY-1, NMP-2/AML, AP-1, and SP-1) during osteoblast differentiation using biochemical fractionation and gel shift analyses. We show that nuclear matrix association of the tissue-specific AML transcription factor NMP-2, but not the ubiquitous transcription factor YY1, is developmentally upregulated during osteoblast differentiation. Moreover, we show that there are multiple AML isoforms in mature osteoblasts, consistent with the multiplicity of AML factors that are derived from different genes and alternatively spliced cDNAs. These AML isoforms include proteins derived from the AML-3 gene and partition between distinct subcellular compartments. We conclude that the selective partitioning of the YY1 and AML transcription factors with the nuclear matrix involves a discriminatory mechanism that targets different classes and specific isoforms of gene regulatory factors to the nuclear matrix at distinct developmental stages. Our results are consistent with a role for the nuclear matrix in regulating the expression of bone-tissue specific genes during development of the mature osteocytic phenotype. J. Cell. Biochem. 66:123-132, 1997. © 1997 Wiley-Liss, Inc.
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  • 7
    Electronic Resource
    Electronic Resource
    Kips off to Myc: Implications for TGFβ signaling (1997)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 66 (1997), S. 427-432 
    Details
    ISSN: 0730-2312
    Keywords: TGFβ ; transforming growth factor β ; Cdk ; cyclin-dependent kinase ; Kip ; cdk-inhibitor ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Loss of sensitivity to the negative growth regulator transforming growth factor β (TGFβ) is a feature of many different tumor types and is likely involved in tumor progression. In some cases this loss of sensitivity to TGFβ has been shown to be manifest in the absence of membrane-associated TGFβ receptor complexes, thus preventing initiation of antiproliferative signals from the cell surface. In others, loss of sensitivity to TGFβ-induced inhibitory signals has been attributed to loss of function of intracellular effectors of TGFβ-induced inhibitory signals due to mutation or allelic loss of effector genes and their products. The intracellular effectors of TGFβ inhibitory signals have been shown to be involved in the normal regulation of progression through the cell cycle, specifically during G1 phase. In this manner, elucidation of the mechanisms by which TGFβ inhibits cell growth not only helps us identify steps involved in tumor progression, but also allows us to better understand how cells regulate progression through the cell cycle. J. Cell. Biochem. 66:427-432, 1997. © 1997 Wiley-Liss, Inc.
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  • 8
    Electronic Resource
    Electronic Resource
    Cell cycle-dependent modifications in activities of pRb-related tumor suppressors and proliferation-specific CDP/cut homeodomain factors in murine hematopoietic progenitor cells (1997)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 66 (1997), S. 512-523 
    Details
    ISSN: 0730-2312
    Keywords: cell cycle control ; H4 gene promoter ; G1/S phase transition point ; CDP/cut ; interferon regulatory factor 2 ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The histone H4 gene promoter provides a paradigm for defining transcriptional control operative at the G1/S phase transition point in the cell cycle. Transcription of the cell cycle-dependent histone H4 gene is upregulated at the onset of S phase, and the cell cycle control element that mediates this activation has been functionally mapped to a proximal promoter domain designated Site II. Activity of Site II is regulated by an E2F-independent mechanism involving binding of the oncoprotein IRF2 and the multisubunit protein HiNF-D, which contains the homeodomain CDP/cut, CDC2, cyclin A, and the tumor suppressor pRb. To address mechanisms that define interactions of Site II regulatory factors with this cell cycle control element, we have investigated these determinants of transcriptional regulation at the G1/S phase transition in FDC-P1 hematopoietic progenitor cells. The representation and activities of histone gene regulatory factors were examined as a function of FDC-P1 growth stimulation. We find striking differences in expression of the pRb-related growth regulatory proteins (pRb/p105, pRb2/p130, and p107) following the onset of proliferation. pRb2/p130 is present at elevated levels in quiescent cells and declines following growth stimulation. By contrast, pRb and p107 are minimally represented in quiescent FDC-P1 cells but are upregulated at the G1/S phase transition point. We also observe a dramatic upregulation of the cellular levels of pRb2/p130-associated protein kinase activity when S phase is initiated. Selective interactions of pRb and p107 with CDP/cut are observed during the FDC-P1 cell cycle and suggest functional linkage to competency for DNA binding and/or transcriptional activity. These results are particularly significant in the context of hematopoietic differentiation where stringent control of the cell cycle program is requisite for expanding the stem cell population during development and tissue renewal. J. Cell. Biochem. 66:512-523, 1997. © 1997 Wiley-Liss, Inc.
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  • 9
    Electronic Resource
    Electronic Resource
    α2-Macroglobulin synthesis by the human monocytic cell line THP-1 is differentiation state-dependent (1997)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 67 (1997), S. 492-497 
    Details
    ISSN: 0730-2312
    Keywords: interferon-γ ; PMA ; proteinase inhibitor ; cytokine ; low density lipoprotein receptor-related protein ; receptor-associated protein ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Human α2-macroglobulin (α2M) is a broad spectrum proteinase inhibitor and cytokine carrier synthesized by a number of cell types including monocytes and macrophages. In this study, we report on the expression of α2M by THP-1 cells. This monocytic cell line can be differentiated into a macrophage-like phenotype by treatment with interferon-γ (IFN-γ) or phorbol 12-myristate 13-acetate (PMA). α2M was synthesized by THP-1 cells at a rate of 75 ng/106 cells/24 h, as determined by Western blot analysis. After treating the cells with 500 U/ml of IFN-γ or with 100 ng/ml PMA, the synthesis rate increased to 219 ng/106 cells/24 h and to 179 ng/106 cells/24 h, respectively. The same agents also increased α2M expression, as determined by Northern blot analysis. When the α2M receptor antagonist, receptor associated protein (RAP), was included in the THP-1 medium, the amount of α2M recovered in the conditioned medium increased. This result suggests that THP-1-secreted proteinases react with secreted α2M and that the resulting complexes are catabolized by the α2M receptor, which is also called low density lipoprotein receptor-related protein (LRP). We conclude that α2M synthesis by THP-1 cells depends on the state of cellular differentiation. Reaction of α2M with secreted proteinases may have minimized previous estimates of the rate of synthesis of α2M by certain cells in culture. J. Cell. Biochem. 67:492-497, 1997. © 1997 Wiley-Liss, Inc.
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  • 10
    Electronic Resource
    Electronic Resource
    Runt homology domain proteins in osteoblast differentiation: AML3/CBFA1 is a major component of a bone-specific complex (1997)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 66 (1997), S. 1-8 
    Details
    ISSN: 0730-2312
    Keywords: AML/CBF/PEBP2 ; regulatory element ; AML-3 ; osteoblasts ; differentiation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The AML/CBFA family of runt homology domain (rhd) transcription factors regulates expression of mammalian genes of the hematopoietic lineage. AML1, AML2, and AML3 are the three AML genes identified to date which influence myeloid cell growth and differentiation. Recently, AML-related proteins were identified in an osteoblast-specific promoter binding complex that functionally modulates bone-restricted transcription of the osteocalcin gene. In the present study we demonstrate that in primary rat osteoblasts AML-3 is the AML family member present in the osteoblast-specific complex. Antibody specific for AML-3 completely supershifts this complex, in contrast to antibodies with specificity for AML-1 or AML-2. AML-3 is present as a single 5.4 kb transcript in bone tissues. To establish the functional involvement of AML factors in osteoblast differentiation, we pursued antisense strategies to alter expression of rhd genes. Treatment of osteoblast cultures with rhd antisense oligonucleotides significantly decreased three parameters which are linked to differentiation of normal diploid osteoblasts: the representation of alkaline phosphatase-positive cells, osteocalcin production, and the formation of mineralized nodules. Our findings indicate that AML-3 is a key transcription factor in bone cells and that the activity of rhd proteins is required for completion of osteoblast differentiation. J. Cell. Biochem. 66:1-8, 1997. © 1997 Wiley-Liss, Inc.
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