Thrombin-Cleaved COOH-Terminal Osteopontin Peptide Binds with Cyclophilin C to CD147 in Murine Breast Cancer Cells

Mi, Zhiyong; Oliver, Tim; Guo, Hongtao; Gao, Chengjiang; Kuo, Paul C.

doi:10.1158/0008-5472.can-06-4066

Cited by 58 publications

(49 citation statements)

References 24 publications

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“…First, the parent proteins listed are not functionally exclusive to coagulation or fibrinolysis. This observation is consistent with previous studies, where a thrombin is implicated as a proteolytic agent in other biological processes (30)(31)(32). Second, only a very few of the cleavage sites match the R-G motif commonly expected for a thrombin, and there are a few missed R-G sites included in the observed peptides.…”

Section: Variability Of Serum Protein and Peptide Contentsupporting

confidence: 92%

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Thrombin induces broad spectrum proteolysis in human serum samples

O'Mullan¹,

Craft²,

Yi³

et al. 2009

Clinical Chemistry and Laboratory Medicine

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Background: During clotting, a thrombin cleaves fibrinogen releasing fibrinopeptide A (FPA). FPA is easily identified in serum using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry (MS). Using MALDI-TOF MS, we observed multiple, progressively shorter fragments of serum FPA. Following ambient incubation of serum, variations in the content of FPA fragments occur over time. Denaturation of a thrombin by heating the serum sample appears to minimize this variation. These observations suggest that intrinsic proteolytic and peptidolytic activity is elevated in serum and perhaps originates from the coagulation cascade enzymes themselves, especially a thrombin. Methods: Extrinsic addition of a thrombin to a subset (3-30 kDa) of plasma proteins was carried out to induce proteolysis and to examine the resultant peptides to reveal a thrombin susceptible parent proteins. One of these identified proteins, hemopexin, was directly digested by a thrombin and the peptides examined to confirm the observations from the initial plasma protein digestion. Results: Extrinsic addition of a thrombin to a subset (3-30 kDa) of plasma proteins results in wide-spread digestion of proteins unrelated to coagulation, revealing a substrate range encompassing more than fibrinogen. Direct digestion of one of these proteins, hemopexin, by a thrombin confirms these observations. Conclusions: The resulting peptides indicate broad tolerance beyond the consensus R-G cleavage site of fibrinogen; in fact, there appears to be no bias for the amino acid following the R/K residue. These data support our hypothesis that the enzymatic activities inherent to coagulation, or at least to thrombin, contribute to destabilization of the protein and peptide content of serum. Clin Chem Lab Med 2009;47:685-93.

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Section: Variability Of Serum Protein and Peptide Contentsupporting

confidence: 92%

“…Enzymes in the clotting cascade, though specific in biological role, have been shown to have promiscuous activity (4,5,(30)(31)(32), outside their expected catalytic function. The data presented here provide direct evidence of this substrate promiscuity, acting broadly upon the protein and peptide content of the plasma/serum itself.…”

Section: Discussionmentioning

confidence: 99%

Thrombin induces broad spectrum proteolysis in human serum samples

O'Mullan¹,

Craft²,

Yi³

et al. 2009

Clinical Chemistry and Laboratory Medicine

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“…As shown in the present study, interference with Basigin expression suppressed the proliferative potential of GC cells in vitro. In agreement with a recently published study (17,18), we found up-regulated expression of Basigin mRNA in GC cells, suggesting its participation in the process of proliferation as an essential component of cell surface signaling transduction. Li et al (19) and Xu and Hemler (20) showed a strong association between cell proliferation and the Basigin-CD98 cell surface super complex, which plays a critical role in energy metabolism.…”

Section: Discussionsupporting

confidence: 93%

Tumor-enhancing activity of Basigin expression in gallbladder carcinoma and its prognostic role

Tang¹

2009

Mol Med Rep

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Abstract. Basigin (EMMPRIN/CD147) is a multifunctional membrane glycoprotein that is overexpressed in many solid tumors and is involved in tumor invasion and angiogenesis. The main purpose of this study was to investigate the tumorenhancing activity of Basigin in a gallbladder carcinoma (GC) cell line and in primary GC tissues. A system that blocks Basigin in the human primary GC cell line GBC-SD was developed using RNA interference. GBC-SD cells were transfected with the small interfering RNA that target Basigin, then the proliferative, invasive and migration activities of the cells were assayed in vitro. Additionally, tissue samples from 98 patients with GC and 26 patients with chronic cholecystitis were stained with anti-Basigin antibody for immunohistochemical analysis. Furthermore, the association of Basigin expression with the clinicopathological characteristics and prognosis of the patients was analyzed. siRNA-treated GBC-SD cells exhibited significantly decreased growth ability, invasion and migration capacities compared to control cells in vitro. Moreover, clinicopathological analysis demonstrated that the intensity of Basigin staining in cancerous tissue was significantly associated with the histological type (p=0.02), distant metastasis (p<0.01) and Nevin stage (p<0.01) of GC. A proportional hazards model revealed the survival rate of patients with stronger Basigin expression to be the lowest (p<0.01). These results suggest that Basigin is a prognostic marker and potential therapeutic target for patients with GC.

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“…However, its mechanism of action is unknown. OPN was previously shown to promote tumor adhesion and metastasis, potentially through direct binding to integrins and regulation of epidermal growth factor receptor and hepatocyte growth factor receptor (17,(28)(29)(30)(31)(32). These findings and our observations from a previous study (15) prompted us to hypothesize that OPN is critically involved in leukocyte migration and perpetuation of synovitis in RA.…”

Section: Discussionmentioning

confidence: 59%

Role of osteopontin in induction of monocyte chemoattractant protein 1 and macrophage inflammatory protein 1β through the NF‐κB and MAPK pathways in rheumatoid arthritis

Zheng¹,

R²,

Pan³

et al. 2009

Arthritis & Rheumatism

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Objective. Osteopontin (OPN) is a proinflammatory protein with a critical role in leukocyte migration. Although OPN has been implicated in rheumatoid arthritis (RA), its underlying mechanism remains unknown. In this study, we investigated the role and molecular mechanism of OPN in the induction of 2 key chemokines, monocyte chemoattractant protein 1 (MCP-1) and macrophage inflammatory protein 1␤ (MIP-1␤), in RA.Methods. Enzyme-linked immunosorbent assay and quantitative polymerase chain reaction were used to determine chemokine expression. Leukocyte migration in the presence of OPN was measured by chemotaxis assay. Signaling and molecular events were analyzed by immunoblotting and chromatin immunoprecipitation.Results. The effect of OPN on inflammatory cell migration was mediated through its unique property of inducing the expression of MCP-1 and MIP-1␤ in CD14؉ monocytes. The concentration of OPN was significantly elevated in RA patients and appeared to correlate with the serum levels of inflammation markers and increased expression of MCP-1 or MIP-1␤ in monocytes in RA patients. Endogenous production of OPN in RA synovial fluid was attributable to increased production of MCP-1 or MIP-1␤, and this effect could be blocked by an anti-OPN antibody. Furthermore, the structural motif responsible for this property resided within residues 50-83 of human OPN, sparing the known RGD or SVVYGLR sequences. It was evident that the effect of OPN on chemokine expression was mediated through both the NF-B and MAPK pathways, involving the activation of IKK␤, p38, and JNK.Conclusion. These results support a unique role of OPN in leukocyte migration, in the context of perpetuation of rheumatoid synovitis through the induction of MCP-1 and MIP-1␤.

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Thrombin-Cleaved COOH-Terminal Osteopontin Peptide Binds with Cyclophilin C to CD147 in Murine Breast Cancer Cells

Cited by 58 publications

References 24 publications

Thrombin induces broad spectrum proteolysis in human serum samples

Thrombin induces broad spectrum proteolysis in human serum samples

Tumor-enhancing activity of Basigin expression in gallbladder carcinoma and its prognostic role

Role of osteopontin in induction of monocyte chemoattractant protein 1 and macrophage inflammatory protein 1β through the NF‐κB and MAPK pathways in rheumatoid arthritis

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