RGD-CAP (βig-h3) enhances the spreading of chondrocytes and fibroblasts via integrin α1β1

Ohno, Shigeru; Noshiro, Mitsuhide; Makihira, Seicho; Kawamoto, Takeshi; Shen, Ming; Yan, Weiqun; Kawashima-Ohya, Yoshie; Fujimoto, Katsumi; Tanne, Kazuo; Kato, Yukio

doi:10.1016/s0167-4889(99)00093-2

Cited by 92 publications

(69 citation statements)

References 37 publications

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“…The full list of the proteins detected from CAL33 and UM-SCC-1 deroofed cells is provided in supplemental Tables S3 and S4, respectively. Western blots of selected proteins that are known to be involved in tumor progression through their roles in regulating cell-cell adhesion (desmoglein 2 and PG) (41,42), cell-matrix interactions (␤ 4 integrin and ␤Ig-h3) (43)(44)(45), motility and invasion (Rac1) (46), and cell growth and death regulation (␤Ig-h3) (47,48) revealed differential expression and corroborated the mass spectrometry findings (Fig. 4B).…”

Section: Differential Expression Of Basal Cell Proteins In Human Squasupporting

confidence: 73%

Detection of Differentially Expressed Basal Cell Proteins by Mass Spectrometry

Todorović

Desai

Eigenheer

et al. 2010

Molecular & Cellular Proteomics

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The ability of cells to modulate interactions with each other and the substrate is essential for epithelial tissue remodeling during processes such as wound healing and tumor progression. However, despite strides made in the field of proteomics, proteins involved in adhesion have been difficult to study. Here, we report a method for the enrichment and analysis of proteins associated with the basal surface of the cell and its underlying matrix. The enrichment involves deroofing the cells with 20 mM ammonium hydroxide and the removal of cytosolic and organellar proteins by stringent water wash. Proteomic profiling was achieved by LC-FTMS, which allowed comparison of differentially expressed or shared proteins under different cell states. First, we analyzed and compared the basal cell components of mouse keratinocytes lacking the cell-cell junction molecule plakoglobin with their control counterparts. Changes in the molecules involved in motility and invasion were detected in plakoglobin-deficient cells, including decreased detection of fibronectin, integrin ␤ 4 , and FAT tumor suppressor. Second, we assessed the differences in basal cell components between two human oral squamous cell carcinoma lines originating from different sites in the oral cavity (CAL33 and UM-SCC-1). The data show differences between the two lines in the type and abundance of proteins specific to cell adhesion, migration, and angiogenesis. Therefore, the method described here has the potential to serve as a platform to assess proteomic changes in basal cell components including extracellular and adhesion-specific proteins involved in wound healing, cancer, and chronic and acquired adhesion-related disorders. Molecular & Cellular Proteomics 9:351-361, 2010.

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Section: Differential Expression Of Basal Cell Proteins In Human Squasupporting

confidence: 73%

Detection of Differentially Expressed Basal Cell Proteins by Mass Spectrometry

Todorović

Desai

Eigenheer

et al. 2010

Molecular & Cellular Proteomics

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“…We confirmed that MRC-5 cells express the ␣v␤5 integrin on their cell surface. Ohno et al (9) previously reported that ␤ig-h3 mediates MRC-5 fibroblast cell adhesion through the ␣1␤1 integrin. However, we consistently found that ␣1 and ␤1 integrin-function blocking antibodies did not significantly block MRC-5 cell adhesion to ␤ig-h3.…”

Section: Although D-iv-l D-iv-r D-iv-laa D-iv-aar and D-iv-lyhrmentioning

confidence: 98%

Identification of Motifs in the Fasciclin Domains of the Transforming Growth Factor-β-induced Matrix Protein βig-h3 That Interact with the αvβ5 Integrin

Kim

Jeong

Nam

et al. 2002

Journal of Biological Chemistry

168

163

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␤ig-h3 is a TGF-␤-induced matrix protein known to mediate the adhesion of several cell types. In this study, we found that all four of the fas-1 domains in ␤ig-h3 mediate MRC-5 fibroblast adhesion and that this was specifically inhibited by a function-blocking monoclonal antibody specific for the ␣v␤5 integrin. Using deletion mutants of the fourth fas-1 domain revealed the MRC-5 cell adhesion motif (denoted the YH motif) is located in amino acids 548 -614. Experiments with substitution mutants showed that tyrosine 571, histidine 572, and their flanking leucine and isoleucine amino acids, which are all highly conserved in many fas-1 domains, are essential for mediating MRC-5 cell adhesion. A synthetic 18-amino acid peptide encompassing these conserved amino acids could effectively block MRC-5 cell adhesion to ␤ig-h3. Using HEK293 cells stably transfected with the ␤5 integrin cDNA, we confirmed that the ␣v␤5 integrin is a functional receptor for the YH motif. In conclusion, we have identified a new ␣v␤5 integrininteracting motif that is highly conserved in the fas-1 domains of many proteins. This suggests that fas-1 domain-containing proteins may perform their biological functions by interacting with integrins. ␤ig-h3 is an extracellular matrix protein whose expression in several cell types, including fibroblasts, is strongly induced by TGF-␤.1 The gene encoding ␤ig-h3 was first identified by Skonier et al. (1), who isolated it by screening a cDNA library made from a human lung adenocarcinoma cell line (A549) that had been treated with TGF-␤. The ␤ig-h3 protein comprises 683 amino acids containing four homologous internal repeat domains. These domains are homologous to similar motifs in the Drosophila protein fasciclin-I and thus are denoted fas-1 domains. The fas-1 domain has highly conserved sequences found in secretory and membrane proteins of several species, including mammals, insects, sea urchins, plants, yeast, and bacteria (2).Mutations in ␤ig-h3 have been shown to be responsible for 5q31-linked human autosomal dominant corneal dystrophies. It has a fibrillar structure and interacts with several extracellular matrix proteins such as fibronectin and collagen (3). In addition, ␤ig-h3 has been reported to be involved in cell growth and differentiation, wound healing, and cell adhesion (4 -9). ␤ig-h3 mediates the adhesion of many different cell types, including corneal epithelial cells, chondrocytes, and fibroblasts (8 -10). We reported previously that ␤ig-h3 mediates corneal epithelial cell adhesion by binding to ␣3␤1 integrin. Two motifs interacting with the ␣3␤1 integrin were located within the second and the fourth fas-1 domains of ␤ig-h3. Interestingly, however, we found that these two motifs are not involved in ␤ig-h3-mediated fibroblastic cell adhesion. Furthermore, all four fas-1 domains of ␤ig-h3 mediate fibroblastic cell adhesion, whereas corneal epithelial cell adhesion is supported by just the second and the fourth fas-1 domains. This suggests that ␤ig-h3 has additional motifs that can mediate the ...

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“…Periostin is especially highly homologous to ßig-h3, a member of the fasciclin I family which has been isolated as a transforming growth factor ß (TGF-ß)-responsive gene (7). ßig-h3 promotes cell adhesion and fibroblast spreading via integrin α1ß2 (8,9) and suppresses the ability of Chinese hamster ovary (CHO) cells to develop into tumors in nude mice (10). The expression of periostin is also increased by TGF-ß (1), and periostin mRNA expression is down-regulated by the introduction of Wnt-3 and by the inhibition of glycogen synthase kinase 3ß (GSK-3ß) (11), suggesting that loss of periostin expression could promote oncogenesis.…”

Section: Introductionmentioning

confidence: 99%

Role of alternative splicing of periostin in human bladder carcinogenesis

Kim

Isono²,

Tambe³

et al. 2008

Int J Oncol

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Abstract.We have previously reported that the expression of periostin mRNA is significantly repressed in human bladder cancer tissues, and that periostin plays a role as a suppressive factor for invasion and metastasis in the progression of human bladder cancers. In this study, to clarify the role of alternative splicing of periostin in human bladder carcinogenesis, we examined the expression of wild-type (WT) and spliced variants of periostin mRNA in normal bladder and bladder cancer tissues. Although both WT and spliced periostin mRNA were expressed in all normal bladder tissues examined, no WT periostin mRNA was detected in the examined transitional cell carcinomas (TCCs) of the bladder (0/23) or in bladder cancer cell lines (0/6). Spliced variants of periostin were detected in 48% (11/23) of TCC tissues and 33% (2/6) of bladder cancer cell lines. Two types of spliced periostin (Variants I and II) were successfully isolated from bladder cancer tissues, but Variant I, which is predominantly expressed in bladder cancer tissues, did not show suppressor activity on in vitro invasiveness and in vivo metastasis of cancer cells. Immunohistochemical analysis indicated that strong belt-like expression of periostin protein was observed in the stroma just beneath the normal bladder epithelium, while it was mostly attenuated in bladder cancer tissues. These results indicate that the loss of WT periostin by down-regulation and/or alternative splicing, which produces Variant I, is closely correlated with the development of bladder cancer.

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RGD-CAP (βig-h3) enhances the spreading of chondrocytes and fibroblasts via integrin α1β1

Cited by 92 publications

References 37 publications

Detection of Differentially Expressed Basal Cell Proteins by Mass Spectrometry

Detection of Differentially Expressed Basal Cell Proteins by Mass Spectrometry

Identification of Motifs in the Fasciclin Domains of the Transforming Growth Factor-β-induced Matrix Protein βig-h3 That Interact with the αvβ5 Integrin

Role of alternative splicing of periostin in human bladder carcinogenesis

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