Ethyl-3,4-dihydroxybenzoate inhibits myoblast differentiation: evidence for an essential role of collagen.

Nandan, Devki; Clarke, Elke P.; Ball, Eric H.; Sanwal, B. D.

doi:10.1083/jcb.110.5.1673

Cited by 80 publications

(54 citation statements)

References 41 publications

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“…In particular, the synthesis of collagen and other extracellular matrix proteins has shown to be essential for myogenic differentiation (23). Here we provide the initial evidence that DDR1 may play an important role in the differentiation of cultured mouse skeletal muscle cells.…”

Section: Discussionmentioning

confidence: 56%

Discoidin Domain Receptor 1 Is Activated Independently of β1 Integrin

Vogel¹,

Brakebusch²,

Fässler³

et al. 2000

Journal of Biological Chemistry

142

135

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Various types of collagen have been identified as potential ligands for the two mammalian discoidin domain receptor (DDR) tyrosine kinases, DDR1 and DDR2. It is presently unclear whether collagen-induced DDR receptor activation, which occurs with very slow kinetics, involves additional proteins with kinase activity or membrane-anchored proteins serving as coreceptors. In particular, the role of the collagen-binding integrins ␣ 1 ␤ 1 or ␣ 2 ␤ 1 in the DDR activation process is undefined. Here, we provide three lines of evidence suggesting that DDR1 signaling is distinct from integrin activation. First we demonstrate that the enzymatic activity of DDR1 is essential for receptor tyrosine phosphorylation. Collagen-induced DDR receptor autophosphorylation can be blocked either by a dominant negative mutant or by a preparation of recombinant extracellular domain. Second, we show DDR1 signals independent of the epidermal growth factor (EGF) receptor. In cells that endogenously express both DDR1 and the EGF receptor, stimulation with EGF does not induce DDR activation. Third, we detected full DDR1 activation after collagen stimulation in cells that have been treated with blocking antibodies for ␣ 2 ␤ 1 integrin or in cells with a targeted deletion of the ␤ 1 integrin gene. Finally, we show that overexpression of dominant negative DDR1 in the myoblast cell line C2C12 blocks cellular differentiation and the formation of myofibers.The various functions of collagens include acting as a structural support in tissue and bone architecture but also serving as bioactive molecules in cellular signaling (1). In many cell types, specific integrins act as surface receptors for different types of collagen (2, 3). These integrins are heterodimers with an ␣ 1 , ␣ 2 , or ␣ 10 subunit linked to the ␤ 1 subunit and are localized to the focal adhesion complex (4,5). Within this complex, they cluster with serine/threonine kinases, tyrosine kinases, and cytoskeletal proteins (6). Recently, several types of collagen were identified as candidate ligands for the two discoidin domain receptors (DDR), 1 DDR1 and DDR2 (7,8). DDRs are tyrosine kinase receptors that are distinguished by a homology region to the Dictyostelium discoideum protein discoidin in their extracellular region (9, 10). Whereas DDR1 activation, measured by an increase in tyrosine kinase autophosphorylation, is achieved by all collagens so far tested (type I to type VI), DDR2 is only activated by fibrillar collagens, in particular by collagen type I and type III (7). In contrast to most other tyrosine kinase receptors, DDR activation follows slow kinetics, and it takes up to 18 h to reach full receptor activity (7,8). The b isoform of DDR1 has an additional 37-amino acid sequence inserted by alternatively splicing into the juxtamembrane domain that contains an LXNPXY sequence (9). Upon collagen-mediated receptor activation, the tyrosine in the LXNPXY sequence becomes phosphorylated and provides a binding site for the phosphotyrosine binding domain of Shc (7). After prolonged act...

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Section: Discussionmentioning

confidence: 56%

Discoidin Domain Receptor 1 Is Activated Independently of β1 Integrin

Vogel¹,

Brakebusch²,

Fässler³

et al. 2000

Journal of Biological Chemistry

142

135

View full text Add to dashboard Cite

show abstract

“…Inhibition of collagen synthesis reduced MRF expression and prevented myogenic differentiation in a manner that could be reversed with exogenous collagen in Matrigel (51,52). Similarly, the loss of proteoglycans in the extracellular matrix by synthesis inhibitors inhibited differentiation and could be rescued by exogenous extracellular matrix administration (53)(54)(55).…”

Section: Discussionmentioning

confidence: 91%

Hyaluronan Synthesis and Myogenesis

Hunt

Gorman

Kintakas

et al. 2013

Journal of Biological Chemistry

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Background:The role endogenously synthesized hyaluronan plays in myogenesis is not yet known. Results: Hyaluronan synthase genes were expressed during skeletal muscle growth and regeneration; inhibiting these synthases prevents myoblast differentiation and fusion. Conclusion: Endogenous hyaluronan synthesis is required for myogenic differentiation. Significance: The necessity for hyaluronan in myogenesis has implications when considering promoting muscle growth or regeneration.

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“…It is accepted that cell-matrix adhesion plays an important role in regulating differentiation. Studies have shown that inhibition of extracellular matrix synthesis [Nandan et al, 1990;Saitoh et al, 1992] as well as blockage of integrin function [Menko and Boettiger, 1987] inhibits the differentiation of myoblasts. Moreover, myoblasts in suspension fail to differentiate in the absence of substrate adhesion [Milasincic et al, 1996].…”

Section: Discussionmentioning

confidence: 99%

The immunoglobulin‐like cell adhesion molecule hepaCAM induces differentiation of human glioblastoma U373‐MG cells

Lee

Moh

Zhang

et al. 2009

J of Cellular Biochemistry

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Subsequent to our identification of a novel immunoglobulin-like cell adhesion molecule hepaCAM, we showed that hepaCAM is frequently lost in diverse human cancers and is capable of modulating cell motility and growth when re-expressed. Very recently, a molecule identical to hepaCAM (designated as GlialCAM) was found highly expressed in glial cells of the brain. Here, we demonstrate that hepaCAM is capable of inducing differentiation of the human glioblastoma U373-MG cells. Expression of hepaCAM resulted in a significant increase in the astrocyte differentiation marker glial fibrillary acid protein (GFAP), indicating that hepaCAM promotes glioblastoma cells to undergo differentiation. To determine the relationship between hepaCAM expression level and cell differentiation, we established two U373-MG cell lines expressing hepaCAM at different levels. The results revealed that high-level hepaCAM triggered a clear increase in GFAP expression as well as morphological changes characteristic of glioblastoma cell differentiation. Furthermore, high expression of hepaCAM significantly accelerated cell adhesion but inhibited cell proliferation and migration. Concomitantly, deregulation of cell cycle regulatory proteins was detected. Expectedly, the differentiation was noticeably less apparent in cells expressing low-level hepaCAM. Taken together, our findings suggest that hepaCAM induces differentiation of the glioblastoma U373-MG cells. The degree of cell differentiation is dependent on the expression level of hepaCAM.

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Ethyl-3,4-dihydroxybenzoate inhibits myoblast differentiation: evidence for an essential role of collagen.

Cited by 80 publications

References 41 publications

Discoidin Domain Receptor 1 Is Activated Independently of β1 Integrin

Discoidin Domain Receptor 1 Is Activated Independently of β1 Integrin

Hyaluronan Synthesis and Myogenesis

The immunoglobulin‐like cell adhesion molecule hepaCAM induces differentiation of human glioblastoma U373‐MG cells

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