Modulation of hypotensive effects of kinins by cathepsin K

Lecaille, Fabien; Vandier, Christophe; Godat, Emmanuel; Hervé-Grépinet, Virginie; Brὂmme, Dieter; Lalmanach, Gilles

doi:10.1016/j.abb.2006.10.033

Cited by 20 publications

(18 citation statements)

References 44 publications

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“…It is also involved in osteosarcoma where its expression is correlated with metastasis (110) and has been shown to process SPARC, a known cancer-related protein, in bone metastasis of prostate cancer (111) . In addition, cathepsin K is associated with schizophrenia through the conversion of β -endorphin to enkephalin (112) and is involved in Toll-like receptor signaling (113) and cardiovascular homeostasis (114) .…”

Section: Cathepsin L-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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Section: Cathepsin L-like Peptidasesmentioning

confidence: 99%

Papain-like peptidases: structure, function, and evolution

Novinec

Lenarčič²

2013

BioMolecular Concepts

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“…While several thiol-dependent cathepsins have been shown to display kinin-forming or kinin-degrading properties [11][12][13][14], none of them was able to act as a carboxypeptidase removing the C-terminal arginine from bradykinin or kallidin.…”

Section: Introductionmentioning

confidence: 99%

A cysteine-type carboxypeptidase, cathepsin X, generates peptide receptor agonists

Nägler

Kraus

Feierler

et al. 2010

International Immunopharmacology

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“…Otherwise cathepsin K has an opposite effect: cathepsin K cleaves kinins, releases pharmacologically inactive kininderived metabolites, and impairs bradykinin B2 receptormediated contraction of bronchial smooth muscles of normal and chronic hypoxic rats [99]. Kininase properties of cathepsin K were confirmed in a rodent model, since the enzyme reduces the hypotensive effect of bradykinin by attenuating kallikrein-induced decrease of blood pressure [100]. Whereas bradykinin induces bronchoconstriction and airway hyperresponsiveness in asthmatic patients, pharmacological antagonists of BK receptors (e.g., Icatibant) reduce bronchoconstriction and improve their pulmonary function [101].…”

Section: Cathepsins and Lung Inflammationmentioning

confidence: 95%

Cysteine Cathepsins: Markers and Therapy Targets in Lung Disorders

Kasabova

Saidi

Naudin

et al. 2011

Clinic Rev Bone Miner Metab

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There is now growing evidence that lung cysteine cathepsins take part in several biological processes and pulmonary homeostasis, although their exact functions remain to be clarified. Their production is increased in most tumors and in chronic and acute inflammatory lung disorders such as silicosis, COPD (emphysema, chronic bronchitis), asthma, and bronchopulmonary dysplasia. Cathepsins aggravate the extent and severity of inflammation and contribute to the remodeling and/or degradation of the extracellular matrix and the basement membrane. Cysteine cathepsins and their inhibitors (stefins and cystatins) are both potential markers of the prognosis and diagnosis of cancer. Cathepsin S is a potential marker of asthma, while cathepsin K may be a useful immunohistological marker of lymphangioleiomyomatosis and of granulomas in interstitial lung diseases. This review covers selected aspects of our current knowledge about lung cysteine cathepsins and outlines some recent advances. We also examine the implications of using cathepsin inhibitors to treat a variety of bone and joint diseases like rheumatoid arthritis, osteoporosis, and bone metastasis for the risk of deleterious side effects on the lungs.

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Modulation of hypotensive effects of kinins by cathepsin K

Cited by 20 publications

References 44 publications

Papain-like peptidases: structure, function, and evolution

Papain-like peptidases: structure, function, and evolution

A cysteine-type carboxypeptidase, cathepsin X, generates peptide receptor agonists

Cysteine Cathepsins: Markers and Therapy Targets in Lung Disorders

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