The human cysteine protease cathepsin V can compensate for murine cathepsin L in mouse epidermis and hair follicles

Hagemann, Sascha; Günther, Thomas; Dennemärker, Julia; Lohmüller, Tobias; Brὂmme, Dieter; Schüle, Roland; Peters, Christoph; Reinheckel, Thomas

doi:10.1078/0171-9335-00404

Cited by 48 publications

(37 citation statements)

References 24 publications

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“…Expression of cathepsin V in the cathepsin L knock-out mouse rescues defects in T cell function (37) and keratinocyte proliferation (38,39). These findings indicate that human cathepsin V and mouse cathepsin L share similar functions, consistent with their high homology (74.6% protein sequence identity for cathepsin V and cathepsin L) (31).…”

Section: Substratesupporting

confidence: 65%

Human Cathepsin V Protease Participates in Production of Enkephalin and NPY Neuropeptide Neurotransmitters

Funkelstein

Koch

et al. 2012

Journal of Biological Chemistry

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Background: Proteases are required to generate peptide neurotransmitters. Results: Human cathepsin V participates in the production of enkephalin and NPY peptide neurotransmitters illustrated by gene expression and silencing. Conclusion: Human cathepsin V participates in producing enkephalin and NPY neurotransmitters in secretory vesicles. Significance: Elucidation of human-specific proteases participating in peptide neurotransmitter production is essential for understanding human health and disease.

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Section: Substratesupporting

confidence: 65%

Human Cathepsin V Protease Participates in Production of Enkephalin and NPY Neuropeptide Neurotransmitters

Funkelstein

Koch

et al. 2012

Journal of Biological Chemistry

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“…Inhibitors selective for cathepsin L and V are just emerging (113) and will prove useful in determining their individuals functions. Furthermore, the search for disease associations with expression or genetic polymorphisms of cathepsins (114)(115)(116), together with functional analysis of human cells and mouse experiments combining gene knockouts with transgenic expression of the human proteases, have already provided valuable insights into the specific in vivo functions of human cathepsins L and V (74,117,118). In summary, the complex phylogeny, the widespread expression of cathepsin L-like enzymes, and the multiple phenotypes of the gene knockout mice highlight the great importance of the cathepsin L-like proteases in physiology and disease processes.…”

Section: Cysteine Cathepsins In Humans and Micementioning

confidence: 99%

Specialized roles for cysteine cathepsins in health and disease

Reiser

Adair²,

Reinheckel³

2010

J. Clin. Invest.

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515

403

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A primer on cathepsin biology Cathepsin L transcription and translation. Substantial work has beendone to analyze the promoter regions of the human cathepsin L gene (CTSL) promoter as well as to understand the regulation of different splice variants within the 5′ untranslated region of the transcript (21,22). Of note, one of the splice variants contains a functional internal ribosomal entry site that enables ongoing translation of human cathepsin L under stress conditions, and hypoxia can shut down cap-dependent translation initiation (23). More recent work has focused on the regulation of cathepsin L alternative translation. According to the presence of different forms of cathepsin L in distinct subcellular and extracellular compartments, cathepsin L proteins can be initiated from downstream AUG sites (10), omitting the signal peptide that is normally present at the N terminus of lysosomal cathepsin L that routes the protein to the ER during its synthesis (Figure 2) (10, 24-26 Cathepsins were originally identified as proteases that act in the lysosome. Recent work has uncovered nontraditional roles for cathepsins in the extracellular space as well as in the cytosol and nucleus. There is strong evidence that subspecialized and compartmentalized cathepsins participate in many physiologic and pathophysiologic cellular processes, in which they can act as both digestive and regulatory proteases. In this review, we discuss the transcriptional and translational control of cathepsin expression, the regulation of intracellular sorting of cathepsins, and the structural basis of cathepsin activation and inhibition. In particular, we highlight the emerging roles of various cathepsin forms in disease, particularly those of the cardiac and renal systems.

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“…In contrast, the mouse genome contains only one CTSL gene, which is ubiquitously expressed (Brömme and Kaleta, 2002). All three enzymes, murine CTSL, human CTSL and human CTSL2, are highly homologous with about 75% amino acid identity, which complicates the assignment of biological functions to the human enzymes (Brömme and Kaleta, 2002;Hagemann et al, 2004). Thus we sought to study the expression of human CTSL in CTSL-deficient mice to assess in vivo functions of the human protease without interference of its highly related homologue.…”

Section: Introductionmentioning

confidence: 99%

Human cathepsin L rescues the neurodegeneration and lethality in cathepsin B/L double-deficient mice

Sevenich

Pennacchio

Peters

et al. 2006

Biological Chemistry

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The human cysteine protease cathepsin V can compensate for murine cathepsin L in mouse epidermis and hair follicles

Cited by 48 publications

References 24 publications

Human Cathepsin V Protease Participates in Production of Enkephalin and NPY Neuropeptide Neurotransmitters

Human Cathepsin V Protease Participates in Production of Enkephalin and NPY Neuropeptide Neurotransmitters

Specialized roles for cysteine cathepsins in health and disease

Human cathepsin L rescues the neurodegeneration and lethality in cathepsin B/L double-deficient mice

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