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  • 1
    Electronic Resource
    Electronic Resource
    Modulation of collagen and fibronectin synthesis in fibroblasts by normal and malignant cells (1992)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 48 (1992), S. 150-161 
    Details
    ISSN: 0730-2312
    Keywords: tumor cells ; cell-cell interaction ; desmoplasia ; extracellular matrix ; stroma reaction ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The influence of various normal and malignant human cells on the level of collagen synthesis by human fibroblasts was tested in coculture. As revealed by immunoperoxidase staining, in cocultures with breast adenocarcinoma cells (MCF7, SA52, T47D) fibroblasts synthesized collagen while tumor cells did not. Fibroblasts displayed increased collagen production without change in the overall protein synthesis. Several other types of cells derived from normal human tissues (keratinocytes, normal mammary cells) or from fibrosarcoma, melanoma, cervical carcinoma, choriocarcinoma, or other breast adenocarcinoma (SW613, MDA, BT20) did not affect collagen synthesis of fibroblasts. Although to a lesser extent, this stimulating effect was reproduced by using the conditioned medium (CM) of the active cells but not with CM of the other cell types. A slight stimulation was also obtained when tumoral MCF7 cells and fibroblasts shared the same medium but were physically separated, suggesting that close contact was required for optimal stimulation of collagen synthesis. The collagen synthesis stimulating activity was not related to a modification of fibroblast proliferation rate. The production of collagen types I, III, and VI and fibronectin were increased in cocultures of fibroblasts with MCF7 cells. The increased synthesis of collagen types I and III and fibronectin was paralleled by similar changes in the steady-state level of their mRNAs. On the contrary, the increased production of collagen type VI appeared regulated at a post-transcriptional level.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240480207
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  • 2
    Electronic Resource
    Electronic Resource
    Ontogeny of Ha-ras and c-myc mRNA levels in rabbit embryo and extraembryonic tissues by quantitative in situ hybridization (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 31 (1992), S. 1-8 
    Details
    ISSN: 1040-452X
    Keywords: Oncogenes ; Development ; Embryo ; Placenta ; Rabbit ; In situ hybridization ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A large variety of proto-oncogenes are known to be of key importance in cellular growth and differentiation during embryonic development. Using quantitative during in situ hybridization, we studied in detail the levels of the proto-oncogenes Ha-ras and c-myc mRNA in embryos and extraembryonic tissues (maternal and embryonic placentas, trophoblast, and endometrial epithelium) during prental life of rabbit. cDNA probes encoding for Ha-ras (fragment Kpn 1-BstE II of 883 bp) and c-myc (fragment Pst 1-Pst 1 of 490 bp) were used to detect specific transcripts in fixed cryostat sections. High levels of Ha-ras and c-myc mRNA were detected in the rabbit embryo as well as in the decidua and in the trophoblast as early as day 9 of gestation. At 12 and 15 days of gestation, Ha-ras and c-myc mRNA levels decreased in both embryonic and maternal placenta while in the embryo a significant increase of Ha-ras and c-myc expression was detected with particular evidence in the central nervous system. Finally, at 25 days of gestation the expression of the two proto-oncogenes, Ha-ras and c-myc, was greatly decreased in both the embryo and extraembryonic tissues, and was undetectable by 30 days of gestation. These results show that in rabbit the expression of the two proto-oncogenes Ha-ras and c-myc is localized in the same tissues with similar intensity and follows an unparallel temporal modulation in the embryo and in the extraembryonic tissues during prental development.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080310102
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  • 3
    Electronic Resource
    Electronic Resource
    In vitro-cultured bovine granulosa and oviductal cells secrete sperm motility-maintaining factor(s) (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 37 (1994), S. 54-60 
    Details
    ISSN: 1040-452X
    Keywords: Cattle ; Cumulus oophorus ; Folicular fluid ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Since bovine cumulus oophorous and oviductual cell cultures are known to support and maintain frozen-thawed bovine sperm viability and motility for extended time periods, we investigated whether granulosa cell (GC)- and oviductual cell (OC)-conditioned media have similar effects. GC and OC were cultured for 3 days in TCM-199 medium supplemented with 10% fetal calf serum. At that time, the supernatant was discarded from GC and the monolayers were covered with Sp-TALP medium containing 6 mg/ml bovine serum albumin, while the OC were recovered by centrifugation and transferred to culture bottles containing Sp-TALP. Two days later, GC-conditioned and OC-conditioned Sp-TALP were recovered and dialyzed, and their retentates were lyophilized. Bovine follicular fluid (BFF) was also dialyzed, and its retentate was lyophilized. When sperm were incubated in GC- or OC-conditioned media, motility remained above 62% and 42% at 6 hr and 30 hr, respectively, and motility was higher than that of the control both at 6 hr (39%; P 〈 0.001) and at 30 hr (9%; P 〈 0.0001). Similarly, when sperm were incubated in the lyophilized retentates of GC- and OC-conditioned media and in BFF at a dose of 0.1, 0.5, or 1.0 mg/ml, the motility rates were higher both at 6 hr (P 〈 0.05) and at 30 hr (P 〈 0.01) compared to the control. The increase in motility was dose dependent; a 1.0 mg/ml dose improved (P 〈 0.05) motility compared to a 0.1 mg mg/ml dose. Heat treatment of the retentates of GC, OC, and BFF at 55°C for 30 min did not destroy their ability to support and maintain motility. However, heating at 100°C for 5 min destroyed their ability to support motility. Molecular sieving of retentates on Sephancryl S-300 yielded fractions that were highly effective (P 〈 0.01) in enhancing and maintaining motility compared to the other fractions. In conclusion, GC and OC secrete nondialyzable, heat-labile factor(s), which support and maintain sperm viability and motility for up to 30 hr. © 1994 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080370108
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  • 4
    Electronic Resource
    Electronic Resource
    Structure of the bovine follicle-stimulating hormone receptor complementary DNA and expression in bovine tissues (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 39 (1994), S. 127-135 
    Details
    ISSN: 1040-452X
    Keywords: Receptor ; Follicle-stimulating hormone ; Granulosa cells ; Follicle ; Bovine ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We report the complementary DNA structure obtained by reverse transcription and polymerase chain reaction amplification encoding the complete amino acid sequence for the bovine follicle-stimulating hormone receptor (bFSHr). The deduced amino acid sequence for the cDNA revealed a mature polypeptide consisting of 678 amino acids (theoretical weight of 76.4 kDa) and a 17 amino acid putative leading signal peptide. The receptor consists of a large NH2-terminal extracellular membrane domain of 349 aa with 3 potential N-linked glycosylation sites, a transmembrane domain (264 aa) consisting of 7 putative membrane spanning segments, and an intracytoplasmic COOH-terminal domain (65 aa). Four potential phosphorylation sites were found in the transmembrane domain and the COOH-terminal domain. The amino acid sequence is 97%, 89%, and 88% homologous to the ovine, human, and rat FSHr respectively, with complete conservation of the 22 cysteine residues in the whole protein and the 3 N-linked glycosylation sites on the extracellular membrane domain. Northern blot analysis of total mRNA in bovine tissues revealed a major mRNA transcript of 2.55 kb for the bFSHr in the ovary without corpus luteum, and in the testis. No expression was found in other tissues analyzed. Total RNA from bovine granulosa cells collected from pregnant mare serum gonadotropin (PMSG)-treated prepubertal heifers showed 2 major mRNA transcripts of 6.8 and 2.55 kb, and 3 minor transcripts of 3.8, 3.3, and 1.6 kb. Bovine granulosa cells cultured with porcine FSH (0, 2, 10 ng/ml) for 4 days showed a decrease in the steady state level of the FSHr mRNA. This decrease was shown to be independent of the size of the transcript. Therefore, expression of the bovine FSHr by bovine granulosa cells is downregulated at the message level when exposed to constant concentrations of FSH. ©1994 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080390202
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  • 5
    Electronic Resource
    Electronic Resource
    Attachment of the ascidian sperm surface egg receptor N-acetylglucosaminidase to the cell membrane (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 38 (1994), S. 453-458 
    Details
    ISSN: 1040-452X
    Keywords: Ascidian sperm glycosidase ; Solubilization ; Hydrophilic ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Ascidian sperm bind to vitelline coat N-acetylglucosamine groups of the egg bvia sperm surface N-acetylglucosaminidase. This sperm surface egg receptor remains anchored throughout penetration. Localization to the sperm surface was verified by biotinylation of intact sperm followed by solubilization in Triton X-100 and binding to streptavidin agarose. The enzyme was determined to be an integral membrane protein as judged by resistance to release by KI and high pH. Linkage of the enzyme to the sperm surface was probed through differential solubilization followed by measuring released enzymatic activity with a fluorogenic substrate. Nonionic detergents released 90% of the activity. Proteases released about 40%. No activity was released by a phosphatidyl-inositol specific phospholipase C. This finding, combined with the similarity of release level by all the detergents, including triton X-114 phase separation experiment. This observation, coupled with the finding of release by nonionic detergents, suggests that the protein is hydrophilic once released from the membrane. Thus, although clearly an integral membrane protein, the enzyme has limited bydrophobicity such as would be present in a single transmembrane sequence or extensive glycosylation. © 1994 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080380413
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  • 6
    Electronic Resource
    Electronic Resource
    Phosphorylation of HSP27 during development and decay of thermotolerance in Chinese hamster cells (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 147 (1991), S. 93-101 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The small molecular weight heat shock protein HSP27 was recently shown to confer a stable thermoresistant phenotype when expressed constitutively in mammalian cells after structural gene transfection. These results suggested that HSP27 may also play an important role in the development of thermotolerance, the transient ability to survive otherwise lethal heat exposure after a mild heat shock. In Chinese hamster O23 cells increased thermoresistance is first detected at 2 h after a triggering treatment of 20 min at 44°C, attains a maximum at 5 hours, and decays thereafter with a half-life of 10 h. We found that the development and decay of transient thermotolerance cannot be solely explained on the basis of changes in the cellular concentration of HSP27. The cellular HSP27 concentration is not increased appreciably at 2 h after heat shock and attains a maximum at 14 h. Similar results were obtained in the case of another heat shock protein, HSP70. HSP70 follows slightly faster kinetics of accumulation (peaks at 10 h) and decays much more rapidly (t1/2 = 4h) than HSP27 (t1/2 = 13h). HSP27 has 3 isoelectric variants A, B, and C of which B and C are phosphorylated. In cells maintained at normal temperature, HSP27A represents more than 90% of all HSP27. Shifting the cell culture temperature from 37 to 44°C induces the incorporation of 32P into the more acidic B and C forms, a process that occurs very rapidly since the reduction in the concentration of the A form and a corresponding increase in the level of B and C is detectable by immunoblot analysis within 2.5 min at 44°C. Analyses performed at various times during development and decay of transient thermo-tolerance revealed a close relationship between the effect of heat shock on HSP27 phosphorylation and cell ability to survive. For example, fully thermotolerant cells (5 h post-induction) are refractory to induction of HSP27 phosphorylation by a 20-min heat shock. The induction of HSP27 phosphorylation was also studied in a family of clonal cell lines of O23 cells that are thermoresistant as a result of the constitutive expression of a transfected human HSP27 gene. In these thermore-sistant cells, phosphorylation of the endogenous hamster HSP27 is induced to a level comparable to that found in the thermosensitive parental cells. However, phosphorylation of the exogencus human protein, which represents more than 80% of total HSP27 in these cells, was much less induced. Although different mechanisms are involved in the maintenance of a high level of unphosphorylated HSP27 in induced-thermotolerant and thermoresistant transfectant O23 cells, our results suggest that the degree of HSP27 phosphorylation could be a determinant of the ability of cells to survive hyperthermia.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041470113
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  • 7
    Electronic Resource
    Electronic Resource
    Proinflammatory cytokines (interleukin-1β and tumor necrosis factor-α) down regulate synthesis and secretion of thrombospondin by human endothelial cells (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 160 (1994), S. 367-377 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We examined the effects of proinflammatory cytokines on the expression of two extracellular matrix proteins, e.g., thrombospondin (TSP) and fibronectin (FN) by cultured human umbilical vein endothelial cells (HUVECs). Treatment of HUVECs with human recombinant interleukin- 1β (IL-1β) or human tumor necrosis factor-α (TNF-α) caused a time- and dose-dependent decline in TSP production whereas FN production was not modified. At low concentrations, IL-1β and TNF-α in combination had a greater effect than either agent alone. Interferon-γ (IFN-γ) was without effect. The decline in TSP synthesis resulted in a decreased secretion of this glycoprotein into the extracellular matrix. Endothelial cell monolayers cultured on porous filters were used to study the polarity of TSP secretion. Approximately two thirds of the synthesized protein was secreted to the apical side medium and one third to the basal side medium and both types of secretion were inhibited to a similar extent by cytokine treatment. Immunoprecipitation experiments revealed no apparent degradation of secreted TSP, either in the apical or in the basal compartment. Treatment of HUVECs with IL-1β, either alone or in combination with TNF-α, had no significant effect on the steady-state TSP mRNA levels, suggesting a posttranscriptional regulation. Our results indicate that IL-1β and TNF-α can selectively modulate the composition of the extracellular matrix by decreasing TSP deposition and suggest different regulatory mechanisms for the expression of various secreted proteins by endothelial cells.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041600218
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  • 8
    Electronic Resource
    Electronic Resource
    Ultrastructure of sperm, spermiogenesis, and sperm-egg interactions in selected invertebrates and lower vertebrates which use external fertilization (1990)
    New York, NY : Wiley-Blackwell
    Journal of Electron Microscopy Technique 16 (1990), S. 115-154 
    Details
    ISSN: 0741-0581
    Keywords: Sperm-egg ultrastructure ; Acrosome ; Sperm binding ; Sperm penetration ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: This review discusses the ultrastructure of sperm with reference to their development, the surface morphology of the egg, and the processes of sperm binding and penetration during fertilization. These topics are treated for selected invertebrates and lower vertebrates which live in aquatic environments and fertilize their eggs externally. Specifically, sperm and eggs from cnidarians, echinoderms, decapod crustaceans, ascidians, lampreys, bony fishes, and amphibians are discussed. Sperm from the majority of these groups exhibit the classical head-midregion-tail configuration characteristic of primitive sperm. Specific variations within this general morphology have been described. The notable exceptions to the primitive-sperm paradigm are the sperm of decapod crustaceans and amphibians. Eggs from all of the animals considered are covered by complex vitelline envelopes except those of cnidarians. In general, the ultrastructural analysis of these egg envelopes shows that they are composed of fibrous subunits. Sperm bind to the vitelline envelope and then penetrate through it to fertilize the egg in all groups reviewed except fishes. In fishes, the sperm reaches the egg surface via micropyles. Finally, we discuss the specific changes in sperm ultrastructure which occur during penetration of the egg envelopes in both flagellated and non-flagellated sperm. These changes, which involve membrane fusion and reorganization as well as movement of membranous organelles, aid the sperm in reaching the actual site of gamete fusion.
    Additional Material: 77 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1060160204
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  • 9
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    Regenerative proliferation in inner ear sensory epithelia from adult guinea pigs and humans (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-12
    Description: Supporting cells in the vestibular sensory epithelia from the ears of mature guinea pigs and adult humans proliferate in vitro after treatments with aminoglycoside antibiotics that cause sensory hair cells to die. After 4 weeks in culture, the epithelia contained new cells with some characteristics of immature hair cells. These findings are in contrast to expectations based on previous studies, which had suggested that hair cell loss is irreversible in mammals. The loss of hair cells is responsible for hearing and balance deficits that affect millions of people.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Warchol, M E -- Lambert, P R -- Goldstein, B J -- Forge, A -- Corwin, J T -- New York, N.Y. -- Science. 1993 Mar 12;259(5101):1619-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Otolaryngology-Head and Neck Surgery, University of Virginia School of Medicine, Charlottesville 22908.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8456285" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aging/physiology ; Animals ; Autoradiography ; Bromodeoxyuridine ; Cell Division/drug effects ; Cells, Cultured/drug effects ; DNA Replication ; Epithelial Cells ; Epithelium/physiology ; Gentamicins/pharmacology ; Guinea Pigs ; Hair Cells, Auditory/*cytology/drug effects/*physiology ; Humans ; Neomycin/pharmacology ; Regeneration ; Saccule and Utricle/cytology/*physiology ; Thymidine/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 10
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    Isolation of the cyclosporin-sensitive T cell transcription factor NFATp (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-10-29
    Description: Nuclear factor of activated T cells (NFAT) is a transcription factor that regulates expression of the cytokine interleukin-2 (IL-2) in activated T cells. The DNA-binding specificity of NFAT is conferred by NFATp, a phosphoprotein that is a target for the immunosuppressive compounds cyclosporin A and FK506. Here, the purification of NFATp from murine T cells and the isolation of a complementary DNA clone encoding NFATp are reported. A truncated form of NFATp, expressed as a recombinant protein in bacteria, binds specifically to the NFAT site of the murine IL-2 promoter and forms a transcriptionally active complex with recombinant protein fragment react with T cell NFATp. The molecular cloning of NFATp should allow detailed analysis of a T cell transcription factor that is central to initiation of the immune response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McCaffrey, P G -- Luo, C -- Kerppola, T K -- Jain, J -- Badalian, T M -- Ho, A M -- Burgeon, E -- Lane, W S -- Lambert, J N -- Curran, T -- CA42471/CA/NCI NIH HHS/ -- GM46227/GM/NIGMS NIH HHS/ -- NS25078/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1993 Oct 29;262(5134):750-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Tumor Virology, Dana-Farber Cancer Institute, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235597" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; DNA, Complementary ; DNA-Binding Proteins/genetics/*isolation & purification/physiology ; Immunosuppressive Agents/pharmacology ; Interleukin-2/genetics ; Mice ; Molecular Sequence Data ; NFATC Transcription Factors ; *Nuclear Proteins ; Phosphoproteins/genetics/isolation & purification/physiology ; Promoter Regions, Genetic ; Proto-Oncogene Proteins c-fos/physiology ; Proto-Oncogene Proteins c-jun/physiology ; RNA, Messenger/analysis ; Recombinant Proteins ; T-Lymphocytes/*chemistry ; Transcription Factors/genetics/*isolation & purification/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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