Transforming growth factor-β1 mRNA in neonatal ovine molars visualized by in situ hybridization: Potential role for the stratum intermedium

1992 ◽  
Vol 37 (8) ◽  
pp. 645-653 ◽  
Author(s):  
S. Jepsen ◽  
P. Schiltz ◽  
D.D. Strong ◽  
S.H. Scharla ◽  
M.L. Snead ◽  
...  
Keyword(s):  
In Situ Hybridization ◽  
Growth Factor ◽  
Potential Role ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β1

Role of Transforming Growth Factor-β1 in Invasion and Metastasis in Gastric Carcinoma

1999 ◽  
Vol 17 (2) ◽  
pp. 607-607 ◽  
Author(s):  
Yoshihiko Maehara ◽  
Yoshihiro Kakeji ◽  
Akira Kabashima ◽  
Yasunori Emi ◽  
Akihiro Watanabe ◽  
...  
Keyword(s):  
Gastric Cancer ◽  
In Situ Hybridization ◽  
Growth Factor ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β1 ◽  
Invasion And Metastasis ◽  
Serosal Invasion ◽  
Tgf Β1

PURPOSE: Transforming growth factor-beta1 (TGF-β1) is a major modulator of cellular proliferation and extracellular matrix formation. We determined the role of TGF-β1 in invasion and metastasis in gastric cancer. MATERIALS AND METHODS: We detected TGF-β1 expression in primary and lymph node metastatic lesions of gastric cancer, using an antibody and in situ hybridization. The plasma TGF-β1 levels in the peripheral vein and in the tumor drainage vein were assayed. RESULTS: In the cytoplasm of cancer cells, TGF-β1 was immunostained in 35.9% (78 of 217) of primary gastric carcinomas, and this expression was confirmed by in situ hybridization. Of 59 gastric carcinomas with a TGF-β1–negative primary tumor, metastatic lymph nodes were positive for TGF-β1 staining in 32 cases (54.2%). Positive staining of TGF-β1 in gastric cancer tissues was closely related to serosal invasion, infiltrative growth, and lymph node metastasis. Multivariate analysis showed that the expression of TGF-β1 was an independent risk factor for serosal invasion and infiltrative growth of the tumor. The plasma level of TGF-β1 did not differ between TGF-β1–negative and –positive groups. There were also no differences in plasma TGF-β1 levels among each tumor stage, between the peripheral and the tumor drainage veins, and between preoperative and postoperative testings. CONCLUSION: Transforming growth factor-β1 is closely related to the invasion and metastasis of gastric cancer, and production of TGF-β1 in the tumor does not contribute to the total amount of TGF-β1 in the blood circulation. We interpret our observations to mean that in a tumor microenvironment, TGF-β1 alters the biologic behavior of the tumor.

Expression of transforming growth factor alpha during development

1988 ◽  
Vol 66 (8) ◽  
pp. 1113-1121 ◽  
Author(s):  
V. K. M. Han ◽  
A. J. D'Ercole ◽  
D. C. Lee
Keyword(s):  
In Situ Hybridization ◽  
Growth Factor ◽  
Mrna Expression ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Alpha ◽  
Egf Receptors ◽  
Hybridization Histochemistry ◽  
In Situ Hybridization Histochemistry ◽  
Factor Alpha

Transforming growth factors (TGFs) are polypeptides that are produced by transformed and tumour cells, and that can confer phenotypic properties associated with transformation on normal cells in culture. One of these growth-regulating molecules, transforming growth factor alpha (TGF-α), is a 50 amino acid polypeptide that is related to epidermal growth factor (EGF) and binds to the EGF receptor. Previous studies have shown that TGF-α is expressed during rodent embryogenesis between 7 and 14 days gestation. To investigate the cellular sites of TGF-α mRNA expression during development, we have performed Northern analyses and in situ hybridization histochemistry on the conceptus and maternal tissues at various gestational ages. Contrary to previous reports, both Northern analyses and in situ hybridization histochemistry indicate that TGF-α mRNA is predominantly expressed in the maternal decidua and not in the embryo. Decidual expression is induced following implantation, peaks at day 8, and declines through day 15 when the decidua is being resorbed. In situ hybridization revealed that expression of TGF-α mRNA is highest in the region of decidua adjacent to the embryo and is low or nondetectable in the uterus, placenta, and embryo. In addition, we could not detect TGF-α mRNA expression in other maternal tissues, indicating that the induction of TGF-α transcripts in the decidua is tissue specific, and not a pleiotropic response to changes in hormonal milieu that occur during pregnancy. The developmentally regulated expression of TGF-α mRNA in the decidua, together with the presence of EGF receptors in this tissue, suggests that this peptide may stimulate mitosis and angiogenesis locally by an autocrine mechanism. Because EGF receptors are also present in the embryo and placenta, TGF-α may act on these tissues by a paracrine or endocrine mechanism.

scholarly journals Synthesis of transforming growth factor-beta 1 by megakaryocytes and its localization to megakaryocyte and platelet alpha-granules

Blood ◽  
1990 ◽  
Vol 76 (10) ◽  
pp. 1946-1955 ◽  
Author(s):  
RA Fava ◽  
TT Casey ◽  
J Wilcox ◽  
RW Pelton ◽  
HL Moses ◽  
...  
Keyword(s):  
In Situ Hybridization ◽  
Growth Factor ◽  
Transforming Growth Factor Beta ◽  
Messenger Rna ◽  
Transforming Growth Factor ◽  
Immunoperoxidase Technique ◽  
Storage Site ◽  
Tgf Beta ◽  
Growth Factor Beta

We have directly demonstrated that megakaryocytes are a major site of synthesis and storage of transforming growth factor-beta 1 (TGF/beta 1) by combined immunohistochemical, immunocytochemical, and in situ hybridization methods. The presence of TGF/beta 1 messenger RNA (mRNA) in mature megakaryocytes in adult rat spleen and bone marrow (BM) was established by in situ hybridization. Localization of TGF/beta 1 protein to intact alpha-granules of megakaryocytes, its putative storage site, was accomplished in glycol-methacrylate embedded porcine BM with an immunoperoxidase technique and light microscopy. The TGF/beta 1 was sequestered in intracytoplasmic granules in a pattern virtually identical to that of another alpha-granule marker protein, fibrinogen. This observation strongly suggests packaging of TGF/beta 1 into this organelle within megakaryocytes. That TGF/beta 1 mRNA was localized to megakaryocytes suggests that the TGF/beta 1 found in the alpha-granules in platelets originates with megakaryocyte synthesis. The alpha-granule localization of TGF/beta 1, as well as fibrinogen, was also demonstrated in isolated platelets at the ultrastructural level by electronmicroscopy (EM) and postembedding colloidal-gold immunocytochemistry, thus directly demonstrating that alpha-granules are the final storage site for TGF/beta 1 in mature platelets.

Transforming growth factor-α and oral fibroma: immunohistochemical and in situ hybridization study

2003 ◽  
Vol 61 (12) ◽  
pp. 1449-1454 ◽  
Author(s):  
Horatiu Rotaru ◽  
Je-Yong Choi ◽  
Sam-Pyo Hong ◽  
Yong-Chan Lee ◽  
Kyoung-In Yun ◽  
...  
Keyword(s):  
In Situ Hybridization ◽  
Growth Factor ◽  
Transforming Growth Factor ◽  
Hybridization Study ◽  
Transforming Growth Factor Α ◽  
Factor Α

scholarly journals The fate of the primary cilium during myofibroblast transition

2014 ◽  
Vol 25 (5) ◽  
pp. 643-657 ◽  
Author(s):  
Matthew Rozycki ◽  
Monika Lodyga ◽  
Jessica Lam ◽  
Maria Zena Miranda ◽  
Károly Fátyol ◽  
...  
Keyword(s):  
Growth Factor ◽  
Sonic Hedgehog ◽  
Primary Cilium ◽  
Potential Role ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β1 ◽  
Related Transcription Factor ◽  
Necessary And Sufficient ◽  
Organ Fibrosis

Myofibroblasts, the culprit of organ fibrosis, can originate from mesenchymal and epithelial precursors through fibroblast–myofibroblast and epithelial–myofibroblast transition (EMyT). Because certain ciliopathies are associated with fibrogenesis, we sought to explore the fate and potential role of the primary cilium during myofibroblast formation. Here we show that myofibroblast transition from either precursor results in the loss of the primary cilium. During EMyT, initial cilium growth is followed by complete deciliation. Both EMyT and cilium loss require two-hit conditions: disassembly/absence of intercellular contacts and transforming growth factor-β1 (TGFβ) exposure. Loss of E-cadherin–dependent junctions induces cilium elongation, whereas both stimuli are needed for deciliation. Accordingly, in a scratch-wounded epithelium, TGFβ provokes cilium loss exclusively along the wound edge. Increased contractility, a key myofibroblast feature, is necessary and sufficient for deciliation, since constitutively active RhoA, Rac1, or myosin triggers, and down-regulation of myosin or myocardin-related transcription factor prevents, this process. Sustained myosin phosphorylation and consequent deciliation are mediated by a Smad3-, Rac1-, and reactive oxygen species–dependent process. Transitioned myofibroblasts exhibit impaired responsiveness to platelet-derived growth factor-AA and sonic hedgehog, two cilium-associated stimuli. Although the cilium is lost during EMyT, its initial presence contributes to the transition. Thus myofibroblasts represent a unique cilium-less entity with profoundly reprogrammed cilium-related signaling.

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