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Results: 251 to 255 of 255

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Transforming growth factors and related peptides in gastrointestinal neoplasia.
Coffey RJ, McCutchen CM, Graves-Deal R, Polk WH
(1992) J Cell Biochem Suppl 16G: 111-8
MeSH Terms: Animals, Cell Transformation, Neoplastic, Colon, Colonic Neoplasms, Female, Gastrointestinal Neoplasms, Humans, Male, Mice, Mice, Transgenic, Multigene Family, Proto-Oncogenes, Receptors, Cell Surface, Receptors, Transforming Growth Factor beta, Transforming Growth Factor alpha, Transforming Growth Factor beta
Show Abstract · Added March 27, 2014
Transforming growth factor alpha and beta 1 (TGF alpha and TGF beta 1) are representative members of two distinct and expanding families of polypeptide growth factors. TGF alpha is an epithelial cell mitogen, whereas TGF beta 1 inhibits epithelial cell growth; the role of these factors in contributing to the transformed phenotype is uncertain. Steady state mRNA expression for these growth factors and their receptors in a panel of human colon cancers and adjacent normal mucosa is presented. Based in part on results from transgenic mice in which TGF alpha is selectively overproduced in the mammary gland, a possible role for TGF alpha as a tumor promoter in the process of transformation is discussed.
1 Communities
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16 MeSH Terms
p120, a novel substrate of protein tyrosine kinase receptors and of p60v-src, is related to cadherin-binding factors beta-catenin, plakoglobin and armadillo.
Reynolds AB, Herbert L, Cleveland JL, Berg ST, Gaut JR
(1992) Oncogene 7: 2439-45
MeSH Terms: 3T3 Cells, Amino Acid Sequence, Animals, Armadillo Domain Proteins, Base Sequence, Cadherins, Cell Adhesion Molecules, Cloning, Molecular, Cytoskeletal Proteins, DNA, DNA Probes, Desmoplakins, Drosophila, Drosophila Proteins, Gene Library, Humans, Insect Hormones, Mice, Molecular Sequence Data, Oncogene Protein pp60(v-src), Phosphoproteins, Polymerase Chain Reaction, Protein-Tyrosine Kinases, Proteins, Receptors, Cell Surface, Sequence Homology, Amino Acid, Sequence Homology, Nucleic Acid, Substrate Specificity, Trans-Activators, Transcription Factors, Xenopus, Xenopus Proteins, beta Catenin, gamma Catenin
Show Abstract · Added March 5, 2014
A novel protein tyrosine kinase (PTK) substrate, p120, has been previously implicated in ligand-induced signaling through the epidermal growth factor, platelet-derived growth factor and colony-stimulating factor 1 receptors, and in cell transformation by p60v-src. We have isolated a near full-length cDNA encoding murine p120. The encoded protein lacks significant homology with any reported protein, but it contains four copies of an imperfect 42 amino acid repeat that occurs 12.5 times in the protein encoded by Drosophila armadillo (arm), and its direct homologs, human plakoglobin (plak) and Xenopus laevis beta-catenin (beta-cat). The presence of this motif implies that p120 may share at least one aspect of its function with the arm protein and its homologs.
1 Communities
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34 MeSH Terms
Evidence for transforming growth factor-beta expression in human leptomeningeal cells and transforming growth factor-beta-like activity in human cerebrospinal fluid.
Johnson MD, Gold LI, Moses HL
(1992) Lab Invest 67: 360-8
MeSH Terms: Agar, Arachnoid, Blotting, Northern, Cells, Cultured, Culture Media, Conditioned, Gene Expression, Humans, Immunohistochemistry, Isomerism, Microscopy, Electron, Pia Mater, RNA, Messenger, Receptors, Cell Surface, Receptors, Transforming Growth Factor beta, Transforming Growth Factor beta
Show Abstract · Added February 17, 2014
BACKGROUND - Little is known about the factors regulating growth and maintenance of human leptomeningeal cells. The influence of cerebrospinal fluid on these functions is also unknown. Possible mediators include the transforming growth factor-beta (TGF beta) family, three closely related peptides that regulate proliferation and numerous other physiologic processes in most mesenchymal cells.
EXPERIMENTAL DESIGN - Expression of both mRNA and protein for TGF beta isoforms TGF beta 1, TGF beta 2, and TGF beta 3 as well as TGF beta-competing activity were evaluated in primary human leptomeningeal cultures by Northern blot analysis, immunohistochemistry, and a radioreceptor assay, respectively. TGF beta 1, TGF beta 2, and TGF beta 3 immunoreactivity was also evaluated in brain sections containing leptomeninges from which these cell cultures were established. An additional study analyzed human cerebrospinal fluid for TGF beta-like activity.
RESULTS - Transcripts for TGF beta 1, TGF beta 2 and TGF beta 3 were detected in RNA from each of the eight leptomeningeal cultures. Significant TGF beta 1 immunoreactivity was detected in leptomeningeal tissue from five of eight cases. TGF beta 2 and TGF beta 3 immunostaining was seen in eight and seven of the cases, respectively. Similarly, cells cultured from these meninges exhibited variable TGF beta 1 and extensive TGF beta 2 and TGF beta 3 immunoreactivity. Radioreceptor assays of conditioned media from four cultures demonstrated significant latent TGF beta-like activity. TGF beta radioreceptor competing activity was also detected by radioreceptor assay in normal blood-free cerebrospinal fluid from 32 patients without neurological disease. In addition, pooled cerebrospinal fluid (from six additional patients) exhibited dose dependent TGF beta-like activity in the radioreceptor assay, stimulation of AKR-2B cell growth in soft agar and inhibition of growth in CCL-64 cell assays suggesting that cerebrospinal fluid contains TG beta-like activity.
CONCLUSIONS - These findings suggest that the human leptomeninges synthesize TGF beta 1, TGF beta 2 and TGF beta 3 and secrete latent TGF beta s at least in vitro. Human cerebrospinal fluid may also contain TGF beta isoforms. Collectively, these observations raise the possibility that members of the TGF beta family contribute to biologic processes of the leptomeninges.
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15 MeSH Terms
Transforming growth factor-beta and transforming growth factor beta-receptor expression in human meningioma cells.
Johnson MD, Federspiel CF, Gold LI, Moses HL
(1992) Am J Pathol 141: 633-42
MeSH Terms: Blotting, Northern, Cross-Linking Reagents, Humans, Immunohistochemistry, Meningeal Neoplasms, Meningioma, Radioligand Assay, Receptors, Cell Surface, Thymidine, Transforming Growth Factor beta, Tumor Cells, Cultured
Show Abstract · Added February 17, 2014
The transforming growth factor-beta (TGF beta) family in mammals includes three closely related peptides that influence proliferation and numerous physiologic processes in most mesenchymal cells. In this study, Northern blots, immunohistochemistry, TGF beta radioreceptor assays, TGF beta receptor affinity labeling and [3H] thymidine incorporation were used to evaluate whether primary cell cultures of human meningiomas synthesize the three TGF beta isoforms, bear TGF beta receptors, and respond to TGF beta. Transcripts for TGF beta 1 and 2 were detected in the three cases analyzed. Transforming growth factor-beta 1 immunoreactivity was detected in three of six cases, and TGF beta 2 and 3 immunoreactivity were detected in each case analyzed. Media conditioned by cells cultured from six meningiomas also contained latent TGF beta-like activity. Transforming growth factor-beta receptor cross-linking studies identified TGF beta binding sites corresponding to the type 1, type 2, and type 3 receptors on meningioma cells. Treatment with active TGF beta 1 produced a statistically significant reduction in [3H] thymidine incorporation after stimulation with 10% fetal calf serum and epidermal growth factor in all six cases studied.
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11 MeSH Terms
Identification and analysis of transforming growth factor beta receptors on primary osteoblast-enriched cultures derived from adult human bone.
Kells AF, Schwartz HS, Bascom CC, Hoover RL
(1992) Connect Tissue Res 27: 197-209
MeSH Terms: Cell Line, Cross-Linking Reagents, DNA, Humans, Iodine Radioisotopes, Osteoblasts, Receptors, Cell Surface, Receptors, Transforming Growth Factor beta, Regression Analysis, Software, Transforming Growth Factor beta
Show Abstract · Added March 5, 2014
Primary human osteoblast-enriched (PHO) cultures derived from adult trabecular bone were analyzed to determine the presence or absence of transforming growth factor beta (TGF-beta) receptors. Saturation binding studies were performed with 125I-TGF-beta in the absence or presence of 200-fold excess cold TGF-beta. Cross-linking experiments utilizing 125-I-TGF-beta were performed to identify specific cell surface binding proteins for TGF-beta. The saturation binding studies demonstrated saturable binding for TGF-beta on PHO cells. TGF-beta was cross-linked to cell surface binding proteins of 50 to 110 KDa and a high molecular weight component. Thus, these receptors appear to be similar in affinity, number per cell, and molecular weight to those previously identified with other cell types. The potential biological effects of TGF-beta on the growth of PHO cultures were evaluated by both 3H-thymidine incorporation and cell number determination. Growth of PHO cells in the presence of TGF-beta resulted in an approximately two-fold stimulation in cell number as compared to control cells while the 3H-thymidine experiments demonstrated a two to four-fold increase in thymidine uptake in the presence of TGF-beta. Radiographic emulsion studies revealed that the alkaline phosphatase positive and negative cell populations were responsive to the TGF-beta mitogenic stimulation. The cumulative findings of saturable binding, specific cell surface binding proteins, and biological effects suggest that functional TGF-beta cell surface receptors are present on primary osteoblast-enriched cultures derived from adult human trabecular bone.
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11 MeSH Terms