Human brain cathepsin H as a neuropeptide and bradykinin metabolizing enzyme

Brguljan, Pika Meško; Türk, Vito; Cimerman, Nina; Brzin, Jože; Križaj, Igor; Popović, Tatjana

doi:10.1016/j.peptides.2003.09.018

Cited by 15 publications

(13 citation statements)

References 49 publications

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“…Despite this, it has remained rather an enigma with respect to its biological functions. As an aminopeptidase, it has been shown to process several neuropeptides (147,148) as well as granzyme B (149) . It is also involved in surfactant protein B maturation in the lung, but not indispensable for this process (150) .…”

Section: Cathepsin Hmentioning

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 Hmentioning

confidence: 99%

Papain-like peptidases: structure, function, and evolution

Novinec

Lenarčič²

2013

BioMolecular Concepts

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“…Cathepsin K has been previously shown to degrade BK, but has a very limited distribution (mostly osteoclasts) [23]. BK is reportedly not inactivated by cathepsins B, C, L and S [23][24][25], while conflicting evidence has been produced for cathepsin H [23,26].…”

Section: Intracellular Inactivation Of Maximakinin and Effects On Sigmentioning

confidence: 99%

Prolonged signalling and trafficking of the bradykinin B2 receptor stimulated with the amphibian peptide maximakinin: Insight into the endosomal inactivation of kinins

Bawolak

Roy

Gera

et al. 2012

Pharmacological Research

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Maximakinin, a 19-residue peptide from the amphibian Bombina maxima, incorporates the full sequence of bradykinin (BK) at its C-terminus with a hydrophilic 10-residue N-terminal Maximakinin is the first known natural kinin sequence that elicits a prolonged cellular signalling, thus suggesting a possible basis for a venomous action and a naturally selected one for the design of B 2 R-transported biotechnological cargoes.

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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%