Caveolin-1 mediates the expression and localization of cathepsin B, pro-urokinase plasminogen activator and their cell-surface receptors in human colorectal carcinoma cells

Cavallo-Medved, Dora; Mai, Jianxin; Dosescu, Julie; Sameni, Mansoureh; Sloane, Bonnie F.

doi:10.1242/jcs.02278

Cited by 117 publications

(103 citation statements)

References 63 publications

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“…Cathepsin B can be localized in caveolae through the association with annexin II heterotetramers (Fig. 1;Cavallo-Medved et al 2005), and, interestingly, annexin II is also involved in the biosynthesis of multivesicular endosomes, in which procathepsin L is stored in association with the tetraspanin CD63 (Collette et al 2004).…”

Section: Regulation Of Protease Trafficking and Pericellular Proteolysismentioning

confidence: 99%

Pericellular proteolysis in cancer

2014

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Pericellular proteases have long been associated with cancer invasion and metastasis due to their ability to degrade extracellular matrix components. Recent studies demonstrate that proteases also modulate tumor progression and metastasis through highly regulated and complex processes involving cleavage, processing, or shedding of cell adhesion molecules, growth factors, cytokines, and kinases. In this review, we address how cancer cells, together with their surrounding microenvironment, regulate pericellular proteolysis. We dissect the multitude of mechanisms by which pericellular proteases contribute to cancer progression and discuss how this knowledge can be integrated into therapeutic opportunities.

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Section: Regulation Of Protease Trafficking and Pericellular Proteolysismentioning

confidence: 99%

Pericellular proteolysis in cancer

2014

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“…In addition, the CSD can hold H-Ras in an inactive state (31,40). Activating mutations in H-Ras (such as G12V) prevent its interaction with caveolin and keep the protein in an active conformation; because such mutations are found in a number of human cancers, agents able to mimic this inhibitory action of caveolin may have therapeutic potential (42,43).…”

Section: Gpcr/g Proteinsmentioning

confidence: 99%

Caveolae as Organizers of Pharmacologically Relevant Signal Transduction Molecules

Patel¹,

Murray²,

Insel

2008

Annu. Rev. Pharmacol. Toxicol.

405

363

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Caveolae, a subset of membrane (lipid) rafts, are flask-like invaginations of the plasma membrane that contain caveolin proteins, which serve as organizing centers for cellular signal transduction. Caveolins (-1, -2, and -3) have cytoplasmic N and C termini, palmitolylation sites, and a scaffolding domain that facilitates interaction and organization of signaling molecules so as to help provide coordinated and efficient signal transduction. Such signaling components include upstream entities (e.g., G protein-coupled receptors (GPCRs), receptor tyrosine kinases, and steroid hormone receptors) and downstream components (e.g., heterotrimeric and low-molecularweight G proteins, effector enzymes, and ion channels). Diseases associated with aberrant signaling may result in altered localization or expression of signaling proteins in caveolae. Caveolin-knockout mice have numerous abnormalities, some of which may reflect the impact of total body knockout throughout the life span. This review provides a general overview of caveolins and caveolae, signaling molecules that localize to caveolae, the role of caveolae/caveolin in cardiac and pulmonary pathophysiology, pharmacologic implications of caveolar localization of signaling molecules, and the possibility that caveolae might serve as a therapeutic target.

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“…The common denominator in both pathologies is the degradation of extracellular matrix by cathepsin B, which occurs in an environment that favors the endoproteolytic activity of cathepsin B. In numerous tumors, cathepsin B expression is upregulated (23) and mature cathepsin B is secreted from the cells where it is associated with the plasma membrane in caveolae (38) . Localization of cathepsin B on the cell surface was recently confirmed by live imaging of human umbilical vein endothelial cells, which have been proposed to utilize cathepsin B for extracellular matrix degradation in angiogenesis (39) .…”

Section: Cathepsin B-like Peptidasesmentioning

confidence: 99%

Papain-like peptidases: structure, function, and evolution

Novinec

Lenarčič²

2013

BioMolecular Concepts

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Papain-like cysteine peptidases are a diverse family of peptidases found in most known organisms. In eukaryotes, they are divided into multiple evolutionary groups, which can be clearly distinguished on the basis of the structural characteristics of the proenzymes. Most of them are endopeptidases; some, however, evolved into exopeptidases by obtaining additional structural elements that restrict the binding of substrate into the active site. In humans, papain-like peptidases, also called cysteine cathepsins, act both as non-specific hydrolases and as specific processing enzymes. They are involved in numerous physiological processes, such as antigen presentation, extracellular matrix remodeling, and hormone processing. Their activity is tightly regulated and dysregulation of one or more cysteine cathepsins can result in severe pathological conditions, such as cardiovascular diseases and cancer. Other organisms can utilize papainlike peptidases for different purposes and they are often part of host-pathogen interactions. Numerous parasites, such as Plasmodium and flukes, utilize papain-like peptidases for host invasion, whereas plants, in contrast, use these enzymes for host defense. This review presents a state-of-the-art description of the structure and phylogeny of papain-like peptidases as well as an overview of their physiological and pathological functions in humans and in other organisms.

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Caveolin-1 mediates the expression and localization of cathepsin B, pro-urokinase plasminogen activator and their cell-surface receptors in human colorectal carcinoma cells

Cited by 117 publications

References 63 publications

Pericellular proteolysis in cancer

Pericellular proteolysis in cancer

Caveolae as Organizers of Pharmacologically Relevant Signal Transduction Molecules

Papain-like peptidases: structure, function, and evolution

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