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Reversible inhibition of normal human prokeratinocyte proliferation by type beta transforming growth factor-growth inhibitor in serum-free medium.

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TLDR
Normal prokeratinocytes are demonstrated to secrete TGF beta/GI-like molecules into the culture medium and to have specific cell surface receptors for this molecule, and a human squamous cell carcinoma, SCC-25, does not arrest growth when exposed to TGFbeta/GI.
Abstract
Type beta transforming growth factor-growth inhibitor (TGF beta/GI) causes normal human prokeratinocytes to arrest growth predominantly in the G1 phase of the cell cycle within 48 h after log phase cultures are exposed to the factor in serum-free medium. The growth arrest induced by TGF beta/GI is reversible because the cells from treated cultures can be replated into fresh medium and grown into large colonies. Normal prokeratinocytes are demonstrated to secrete TGF beta/GI-like molecules into the culture medium and to have specific cell surface receptors for this molecule. In contrast, a human squamous cell carcinoma, SCC-25, does not arrest growth when exposed to TGF beta/GI. These cells, unlike the normal prokeratinocytes, do not exhibit detectable cell surface receptors for the factor.

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Citations
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Some recent advances in the chemistry and biology of transforming growth factor-beta.

TL;DR: It is clear that there is no one principal action for TGF-beta; moreover, the almost universal cellular distribution of its receptor encompasses a very broad spectrum of target tissues.
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Transforming growth factor-beta: biological function and chemical structure

TL;DR: TGF-beta's marked ability to enhance formation of connective tissue in vivo suggests several therapeutic applications.
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Expression cloning of the TGF-β type II receptor, a functional transmembrane serine/threonine kinase

TL;DR: A chimeric protein containing the intracellular domain of the type II receptor and expressed in E. coli can phosphorylate itself on serine and threonine residues in vitro, indicating that the cytoplasmic domain of that receptor is a functional kinase, implicates serine/threonine phosphorylation as an important mechanism of TGF-beta receptor-mediated signaling.
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Transforming Growth Factor-β

TL;DR: Transforming growth factor-β (TGF-β) as mentioned in this paper is the cytokine with the broadest range of activities in repair of injured tissue, based both on the variety of cell types that produce and/or respond to it and on the spectrum of its cellular responses.
Book ChapterDOI

The Transforming Growth Factor-βs

A. B. Roberts, +1 more
TL;DR: This chapter summary of current knowledge of the chemistry and complex biology of the growing family of TGF-βs suggests that it has a pivotal control function in many physiological and pathological processes.
References
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Journal ArticleDOI

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Journal ArticleDOI

Calcium-Regulated Differentiation of Normal Human Epidermal Keratinocytes in Chemically Defined Clonal Culture and Serum-Free Serial Culture

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Journal ArticleDOI

New class of transforming growth factors potentiated by epidermal growth factor: isolation from non-neoplastic tissues.

TL;DR: Proteins potentiated by epidermal growth factor to induce a transformed phenotype in non-neoplastic rat kidney fibroblasts in cell culture have been isolated from many non-Neoplastic tissues of the adult mouse, including submaxillary gland, kidney, liver, muscle, heart, and brain.
Journal ArticleDOI

Rat transforming growth factor type 1: structure and relation to epidermal growth factor

TL;DR: The complete amino acid sequence of rat transforming growth factor type 1 has been determined and this growth factor, obtained from retrovirus-transformed fibroblasts, is structurally and functionally related to mouse epidermal growth factor and human urogastrone.
Journal Article

Transforming Growth Factor Production by Chemically Transformed Cells

TL;DR: Evidence is presented indicating that the chemically transformed AKR-MCA and C3H/MCA-58 murine cell lines produce "transforming growth factor(s)" capable of inducing a transformed morphology and the ability to grow in soft agar in nontransformed, anchorage-dependent indicator cells.
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