Competition between Plasminogen and Procathepsin B as a Probe to Demonstrate thein VitroActivation of Procathepsin B by the Tissue Plasminogen Activator

Dalet-Fumeron, V.; Boudjennah, Laziz; Pagano, Maurice

doi:10.1006/abbi.1996.0516

Cited by 20 publications

(14 citation statements)

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“…Our collagen cultures additionally released active forms of these enzymes (Mason et al , 1985; Hanewinkel et al , 1987; Reilly et al , 1989), especially after treatment with IL‐1 β . In the case of cathepsin B, this conversion may have reflected processing by urokinase‐ and tissue‐type plasminogen activators (u‐PA and t‐PA; Dalet‐Fumeron et al , 1993, 1996), of which t‐PA is secreted in particularly high levels by gingival fibroblasts in response to IL‐1 and collagen (Lorimier et al , 1996; Xiao et al , 1998).…”

Section: Discussionmentioning

confidence: 99%

Collagen degradation by interleukin‐1β‐stimulated gingival fibroblasts is accompanied by release and activation of multiple matrix metalloproteinases and cysteine proteinases

et al. 2005

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Section: Discussionmentioning

confidence: 99%

Collagen degradation by interleukin‐1β‐stimulated gingival fibroblasts is accompanied by release and activation of multiple matrix metalloproteinases and cysteine proteinases

et al. 2005

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“…Additionally, interactions involve proteases of different families and can proceed in multiple different pathways, allowing for some proteases to compensate for the absence of others. References for proteolytic interactions not described in the main text: cathepsin D activates cathepsin L [18], cathepsin L activates cathepsin Z [90], cathepsin B activates cathepsin D, MMP2, and MMP3 [18, 75], tissue-type plasminogen activator (tPA) activates cathepsin B and plasmin [91], MMP14 can activate MMP2 [92], MMP2, MMP14, and plasmin can activate MMP13 [93], MMP14 activates MMP8 [94], MMP26 can activate KLK4 [26], and furin activates MMP11 and MMP14 [31]. …”

Section: Figurementioning

confidence: 99%

Proteolytic networks in cancer

Mason

Joyce

2011

Trends in Cell Biology

476

379

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Proteases are important for multiple processes during malignant progression including tumor angiogenesis, invasion and metastasis. Recent evidence reveals that tumor-promoting proteases function as part of an extensive multidirectional network of proteolytic interactions, in contrast to the unidirectional caspase cascade. These networks involve different constituents of the tumor microenvironment, and key proteases — such as cathepsin B, urokinase-type plasminogen activator and several matrix metalloproteinases — occupy central nodes for amplifying proteolytic signals passing through the network. The proteolytic network interacts with other important signaling pathways in tumor biology, involving chemokines, cytokines, and kinases. Viewing these proteolytic interactions as a system of activating and inhibiting reactions provides insight into tumor biology and reveals relevant pharmaceutical targets. This review will examine recent advances in understanding proteases in cancer, and summarize how their network of activity is co-opted to promote tumor progression.

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“…Cathepsin B can be activated by acidic pH or by various other proteases like cathepsin D, cathepsin G, urokinase plasminogen activator receptor (u-PAR). 12,21,22 Cathepsin B can act at as exopeptidases (carboxypeptidases) at low pH and as endopeptidases at neutral pH. 23,24 Various experimental studies have thrown light on the role of cathepsin B on tumorigenesis.…”

Section: Role Of Cathepsins In Cancer Progressionmentioning

confidence: 99%

Roles of cathepsins in pancreatic cancer

Singh¹,

Saraya²

2016

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Pancreatic cancer is an aggressive disease with rapid invasion and metastasis. Extracellular matrix degrading enzymes play an important role in cancer cell invasion and migration. Cathepsins are a group of proteolytic enzymes, which are responsible for the matrix turnover. Among the cathepsins, more number of studies have focused upon cysteine cathepsins. The function and activities of these enzymes are interwoven and their interplay causes the activation of one another by following a proteolytic cascade. This review focuses on differential expression of cathepsins in different types of pancreatic cancer and controls, importance of cathepsins in various phenomena responsible for tumorigenesis and its spread in experimental and human studies. Thus, cathepsins and its expression in pancreatic cancer may be used as potential biomarkers and may prove to be important therapeutic targets if tested clinically.

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Competition between Plasminogen and Procathepsin B as a Probe to Demonstrate thein VitroActivation of Procathepsin B by the Tissue Plasminogen Activator

Cited by 20 publications

References 0 publications

Collagen degradation by interleukin‐1β‐stimulated gingival fibroblasts is accompanied by release and activation of multiple matrix metalloproteinases and cysteine proteinases

Collagen degradation by interleukin‐1β‐stimulated gingival fibroblasts is accompanied by release and activation of multiple matrix metalloproteinases and cysteine proteinases

Proteolytic networks in cancer

Roles of cathepsins in pancreatic cancer

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