Fibronectin phosphorylation by ecto-protein kinase

Imada, Sumi

doi:10.1016/0014-4827(88)90293-5

Cited by 25 publications

(13 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…They have been identified on a wide variety of cell types (21)(22)(23)(24). Whereas some ectoprotein kinases are detectable in conditioned medium (24), we were unable to detect any kinase activity directed against IGFBP-3 in T-47D cell-conditioned medium.…”

Section: Fig 6 Glycosylated Igfbp-3 Competes With Nonglycosylated Icontrasting

confidence: 75%

“…Ectoprotein kinases are membrane-associated kinases that are thought to be important in the phosphorylation of extracellular proteins (21), including matrix proteins such as fibronectin and cell adhesion molecules (22,23). They have been identified on a wide variety of cell types (21)(22)(23)(24).…”

Section: Fig 6 Glycosylated Igfbp-3 Competes With Nonglycosylated Imentioning

confidence: 99%

See 1 more Smart Citation

Phosphorylation of Insulin-Like Growth Factor (IGF) Binding Protein-3 by Breast Cancer Cell Membranes Enhances IGF-I Binding

Mishra

Murphy

2003

Endocrinology

View full text Add to dashboard Cite

Cross-linking of nonglycosylated biotinylated IGF binding protein (IGFBP)-3 to T-47D cell membranes identifies complexes with Mr of 32, 50, 70, and 100 kDa. Nonbiotinylated glycosylated IGFBP-3 competed for binding to each of these sites. The 32-kDa band approximated the size of intact nonglycosylated IGFBP-3, but its abundance was enhanced by cross-linking, and it had a more acidic isoelectric point on isoelectric focusing, suggesting that it had undergone phosphorylation. Immobilized IGFBP-3 was phosphorylated in the presence of (32)P-gamma ATP by both T-47D cell membranes and by intact cells treated with phenylarsine oxide to inhibit internalization. MCF-7 and COS-1 cells were also able to bind and phosphorylated IGFBP-3. IGF-I inhibited both IGFBP-3 binding to membranes and phosphorylation. However, incubation of T-47D cells with IGFBP-3 enhanced binding of (125)I-IGF-I to the cell monolayer indicating that membrane bound IGFBP-3 was able to bind IGF-I. Immobilized IGFBP-3 when phosphorylated by T-47D membranes bound significantly more (125)I-IGF-I than nonphosphorylated IGFBP-3. Treatment with alkaline phosphatase significantly reduced (125)I-IGF-I binding to phosphorylated immobilized IGFBP-3 and also reduced (125)I-IGF-I to T-47D cell monolayers preincubated with IGFBP-3. Phosphorylation of IGFBP-3 by T-47D membranes was partially blocked by inhibitors of both protein kinase A and C. These data demonstrate that binding of IGFBP-3 to breast cancer membranes is accompanied by phosphorylation at the plasma membrane and that both processes are inhibited by IGF-I. However, once phosphorylated the ability of IGFBP-3 to bind IGF-I is enhanced, resulting in increased association of the IGF-I with the cell membrane.

show abstract

Section: Fig 6 Glycosylated Igfbp-3 Competes With Nonglycosylated Icontrasting

confidence: 75%

Section: Fig 6 Glycosylated Igfbp-3 Competes With Nonglycosylated Imentioning

confidence: 99%

Phosphorylation of Insulin-Like Growth Factor (IGF) Binding Protein-3 by Breast Cancer Cell Membranes Enhances IGF-I Binding

Mishra

Murphy

2003

Endocrinology

View full text Add to dashboard Cite

show abstract

“…Furthermore, some of extracellular matrix proteins are known to be phosphorylated [26,[30][31][32]. Yalak and Vogel identified 770 different phosphorylation sites in 66 extracellular proteins or in proteins with extracellular domain by annotation of secreted phosphorylated protein data available in public repositories [33].…”

Section: Protein Phosphorylation 140mentioning

confidence: 99%

“…In addition, fibronectin [30] and neuronal cell adhesion molecules [29] are known to be phosphorylated. However, effects of their phosphorylation are unknown.…”

Section: Vitronectinmentioning

confidence: 99%

Ecto-Phosphorylation and Regeneration of the Adult Central Nervous System

Takei¹,

Amagase²

2017

Protein Phosphorylation

View full text Add to dashboard Cite

Phosphorylation of ecto-domains of membrane proteins and extracellular matrix proteins, which is termed ecto-phosphorylation, activates intracellular signalling and has roles in several physiological processes including cell adhesion, fertilisation and fibrinolysis. We demonstrated that ecto-phosphorylation can promote endogenous neurogenesis in the damaged central nervous system (CNS), augmenting its functional recovery. Thus, regulation of ecto-phosphorylation could be a platform for development of therapeutic methods against CNS injury. Regeneration of the damaged CNS is long-awaited. While transplantation of neuronal progenitor cells is expected to be the first platform to develop the therapy, the potential of endogenous neurogenesis as a source of new neurons has been expected to be an inexpensive and non-invasive regenerative medicine for CNS injury. In this review, we focused on the spinal cord as a model of CNS recovery from traumatic injury. The spinal cord is the simplest part of the CNS and its function is well known. Therefore, estimation of recovery is easier than other part of the CNS. Firstly, we introduce endogenous neural stem cells (NSCs) in the adult spinal cord and their behaviour after injury and then discuss effects of ecto-phosphorylation, which induces regeneration of the adult spinal cord.

show abstract

“…Aberrant regulation of phosphorylation often results in various disease states such as cancer, diabetes, and neurodegenerative diseases [2]. Phosphorylation of extracellular matrix such as fibronectin, vitronectin, and collagen type IV has also been demonstrated [3][4][5][6][7]. Interestingly, this ectophosphorylation can influence cell adhesion and migration, as shown for vitronectin [8].…”

Section: Introductionmentioning

confidence: 97%

Phosphorylation of Extracellular Matrix Tenascin-X Detected by Differential Mass Tagging Followed by NanoLC-MALDI-TOF/TOF-MS/MS Using ProteinPilot Software

Matsumoto

2011

Connective Tissue Research

View full text Add to dashboard Cite

Reversible protein phosphorylation represents a major mechanism of signal transduction in a variety of cellular functions. An understanding of proteome-wide phosphorylation dynamics is important to obtain an overview of the whole signal transduction network. However, a systematic analysis for differentially expressed phosphoproteins under serum-stimulated response is lacking. Here, an easy and fast approach for the identification of differentially expressed phosphoproteins was used. After enrichment of phosphoproteins from serum-stimulated cell lysates by immobilized metal affinity chromatography, a quantitative proteomic approach with isobaric tag for absolute and relative quantitation labeling in combination with nanoLC-MALDI-TOF/TOF-MS/MS followed by ProteinPilot analysis was used. Consequently, 506 differentially expressed phosphoproteins were identified. Among them, 22 proteins that had a reproducible phosphorylation site at Ser or Thr were identified. Out of these 22 phosphoproteins, 7 are mainly involved in splicing. Among the 22 proteins, it was found that extracellular matrix tenascin-X is phosphorylated, although there is little quantitative change by the serum stimulation. MS/MS analysis revealed a novel phosphorylation site of tenascin-X, Thr1841, located in the loop region between the 10th and 11th fibronectin type III repeats. The phosphorylation of tenascin-X would be considered in clarifying its function in the future.

show abstract

Fibronectin phosphorylation by ecto-protein kinase

Cited by 25 publications

References 18 publications

Phosphorylation of Insulin-Like Growth Factor (IGF) Binding Protein-3 by Breast Cancer Cell Membranes Enhances IGF-I Binding

Phosphorylation of Insulin-Like Growth Factor (IGF) Binding Protein-3 by Breast Cancer Cell Membranes Enhances IGF-I Binding

Ecto-Phosphorylation and Regeneration of the Adult Central Nervous System

Phosphorylation of Extracellular Matrix Tenascin-X Detected by Differential Mass Tagging Followed by NanoLC-MALDI-TOF/TOF-MS/MS Using ProteinPilot Software

Contact Info

Product

Resources

About