Suppression of Growth-Associated Phosphorylation of Proteins of Fibroblasts by Collagen Fibrils

Koseki, N.; Sato, Hisaya; Yoshizato, Katsutoshi

doi:10.3109/15419069609081023

Cited by 6 publications

(4 citation statements)

References 43 publications

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“…Previous studies have identified striking changes in two‐dimensional gel electrophoresis of proteins synthesized by fibroblasts, some of which could be attributed to posttranslational modifications. 43,44 Application of this type of approach to epithelial cells showed similar dramatic changes in overall protein patterns, and we could identify more than 100 protein changes in human salivary gland epithelial cell lines cultured on fibronectin or collagen in comparison to tissue culture plastic. 45 This latter process could be shown to be integrin‐dependent, since adhesion to substrates in the presence of 10% serum (i.e., to substrates coated with adsorbed vitronectin) could be blocked with antivitronectin receptor; adhesion to fibronectin could be blocked by antibodies to the α5 and β1 subunits of the major fibronectin receptor; and adhesion to type I collagen gels could be blocked with antibodies against β1 integrins and partially blocked by antibodies to α2 and α3 collagen receptors.…”

Section: Integrin Signaling To the Nucleusmentioning

confidence: 96%

Fibronectin and Integrins in Cell Adhesion, Signaling, and Morphogenesis

Miyamoto

Kathz

Lafrenie

et al. 1998

Annals of the New York Academy of Sciences

215

138

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Fibronectin and integrins play crucial roles in a variety of morphogenetic processes, in which they mediate cell adhesion, migration, and signal transduction. They induce hierarchical transmembrane organization of cytoskeletal and signaling molecules into multimolecular complexes of more than 30 proteins. Organization of these complexes is a synergistic process dependent on integrin aggregation and occupancy, as well as tyrosine phosphorylation. Integrins also cooperate with growth-factor receptors to enhance signaling. Fibronectin and integrins induce a variety of downstream effects, including enhanced transcription factor activity, induction of over 30 genes (> half novel), and altered expression of over 100 proteins. Fibronectin and integrins therefore trigger a hierarchy of signaling responses involved in regulating processes crucial for normal morphogenesis, including cell adhesion, migration, and specific gene expression.

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Section: Integrin Signaling To the Nucleusmentioning

confidence: 96%

Fibronectin and Integrins in Cell Adhesion, Signaling, and Morphogenesis

Miyamoto

Kathz

Lafrenie

et al. 1998

Annals of the New York Academy of Sciences

215

138

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“…In addition to serum stimulation, cell adhesion to different matrix molecules can also alter gene expression and protein synthesis (4,120,121,143). Cell adhesion also modulates signaling initiated by growth factors (109,163).…”

Section: Activation Of Fibroblastsmentioning

confidence: 99%

Cell biology of gingival wound healing

HÄKKINEN¹,

Uitto²,

Larjava³

2000

Periodontol 2000

194

127

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“…Currently, 2-D PAGE is the only method capable of simultaneously resolving several thousands of proteins [7][8][9][10] including protein variants produced by the co-or posttranslational processing such as phosphorylation, glycosylation, and sulfation [11]. Therefore, 2-D PAGE is well suited for the comprehensive analysis of protein phosphorylation in cells and tissues.…”

Section: Introductionmentioning

confidence: 99%

Mapping of phosphorylated proteins on two-dimensional polyacrylamide gels using protein phosphatase

Yamagata¹,

Kristensen²,

Takeda³

et al. 2002

Proteomics

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This study developed an enzymatic method for high-throughput mapping of phosphoproteins on two-dimensional (2-D) polyacrylamide gels. Proteins of cultured rat skin fibroblasts were divided into two aliquots, one of which was dephosphorylated using recombinant lambda protein phosphatase and the other was not treated with the enzyme. The two aliquots were then subjected to 2-D electrophoresis. Phosphoproteins could be mapped on the 2-D gel of the nontreated aliquot by comparing the gels of the two aliquots, because the phosphoproteins in the treated aliquot shifted to more basic positions on the gel. This technique revealed that approximately 5% of the detectable proteins were phosphorylated. Fourteen phosphoproteins were identified by mass spectrometry, including proteasome component C8 and small glutaminerich tetratricopeptide repeat-containing protein. Furthermore, the extent of phosphorylation of two actin modulating proteins, destrin and cofilin, was found to be significantly reduced when the cells were chemically or enzymatically detached from the culture dishes. The method developed by this study can generally be applied to all biological materials and is useful for high-throughput mapping of phosphoproteins in proteome research.

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Suppression of Growth-Associated Phosphorylation of Proteins of Fibroblasts by Collagen Fibrils

Cited by 6 publications

References 43 publications

Fibronectin and Integrins in Cell Adhesion, Signaling, and Morphogenesis

Fibronectin and Integrins in Cell Adhesion, Signaling, and Morphogenesis

Cell biology of gingival wound healing

Mapping of phosphorylated proteins on two-dimensional polyacrylamide gels using protein phosphatase

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