Редактирование: CTSL

Procathepsin L precursor (EC 3.4.22.15) (Cathepsin L1) (Major excreted protein) (MEP) [Contains: Cathepsin L; Cathepsin L heavy chain; Cathepsin L light chain] [CTSL1]

==Publications==

{{medline-entry
|title=Myocardial cathepsin D is downregulated in sudden cardiac death.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/32176724
|abstract=Cathepsins are the major lysosomal proteases that maintain intracellular homeostasis. Herein, we investigated the alterations in myocardial cathepsin expression during aging, cardiac hypertrophy, and sudden cardiac death ([[SCD]]). Cardiac tissue and blood were sampled from autopsy cases. Subjects were classified into three groups: [[SCD]] with cardiac hypertrophy (SCH), compensated cardiac hypertrophy (CCH), and control. Immunoblotting was performed for the major cardiac cathepsins and their targets: cathepsin B, D, and L ([[CTSB]]/D/L), p62, ATP synthase subunit c (ATPSC), and α-synuclein (ASNC). Immunohistochemical analysis and ELISA using serum samples were performed for [[CTSD]]. Cardiac [[CTSB]] and [[CTSD]] were upregulated with age (r = 0.63 and 0.60, respectively), whereas the levels of [[CTSL]], p62, ATPSC, and ASNC remained unchanged. In age-matched groups, cardiac [[CTSD]] was significantly downregulated in SCH (p = 0.006) and [[CTSL]] was moderately downregulated in CCH (p = 0.021); however, p62, ATPSC, and ASNC were not upregulated in cardiac hypertrophy. Immunohistochemistry also revealed decreased myocardial [[CTSD]] levels in SCH, and serum [[CTSD]] levels were relatively lower in SCH cases. Overall, these results suggest that upregulation of cardiac [[CTSB]] and [[CTSD]] with age may compensate for the elevated proteolytic demand, and that downregulation of [[CTSD]] is potentially linked to SCH.
|mesh-terms=* Adult
* Aged
* Aged, 80 and over
* Aging
* Cathepsin D
* Death, Sudden, Cardiac
* Down-Regulation
* Female
* Humans
* Male
* Middle Aged
* Myocardium
* Substrate Specificity

|full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7075574
}}
{{medline-entry
|title=Cathepsin L deficiency results in reactive oxygen species (ROS) accumulation and vascular cells activation.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/29041825
|abstract=Recent evidence suggests a link between cathepsin L ([[CTSL]]) and vascular diseases. However, its contribution to reactive oxygen species (ROS) homeostasis in the vasculature remains unknown. p66shc is a redox enzyme implicated in mitochondrial ROS generation and translation of oxidative signals. In this study, we explored the relationship between [[CTSL]] and oxidative damage in vasculature and whether the oxidative damage is mediated by p66shc.Carotid arteries from aged mice (24 months old) showed a reduction in [[CTSL]] expression compared with young wild-type mice (4 months old). Local knockdown of [[CTSL]] in carotid arteries of young mice by adenoviral vector encoding the short hairpin RNA targeting [[CTSL]] leading to premature vascular aging, as shown by mitochondrial disruption, increased β-galactosidase-positive cells, reduced telomerase activity, and up-regulation of p66shc. Knockdown of [[CTSL]] decreased the expression of mitochondrial oxidative phosphorylation (OXPHOS) complexes I, III, and IV, leading to increased mitochondrial ROS and hyperpolarization of the mitochondrial membrane in vitro. Furthermore, knockdown of [[CTSL]] also stimulated ROS production and senescence in vascular cells, accompanied by the up-regulation of p66shc.However, p66shc knockdown blunted the alteration in ROS production, and senescence in [[CTSL]] knockdown vascular cells. This study suggests that [[CTSL]] knockdown partially induces vascular cells damage via increased ROS production and up-regulation of p66shc.
|mesh-terms=* Animals
* Cathepsin L
* Cells, Cultured
* Humans
* Male
* Mice
* Mice, Inbred C57BL
* Muscle, Smooth, Vascular
* Reactive Oxygen Species
|keywords=* Cathepsin L
* p66shc
* reactive oxygen species
* senescence
* vascular cells
|full-text-url=https://sci-hub.do/10.1080/10715762.2017.1393665
}}
{{medline-entry
|title=Involvement of lysosomal dysfunction in autophagosome accumulation and early pathologies in adipose tissue of obese mice.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/28121218
|abstract=Whether obesity accelerates or suppresses autophagy in adipose tissue is still debatable. To clarify dysregulation of autophagy and its role in pathologies of obese adipose tissue, we focused on lysosomal function, protease maturation and activity, both in vivo and in vitro. First, we showed that autophagosome formation was accelerated, but autophagic clearance was impaired in obese adipose tissue. We also found protein and activity levels of [[CTSL]] (cathepsin L) were suppressed in obese adipose tissue, while the activity of [[CTSB]] (cathepsin B) was significantly enhanced. Moreover, cellular senescence and inflammasomes were activated in obese adipose tissue. In 3T3L1 adipocytes, downregulation of [[CTSL]] deteriorated autophagic clearance, upregulated expression of [[CTSB]], promoted cellular senescence and activated inflammasomes. Upregulation of [[CTSB]] promoted additional activation of inflammasomes. Therefore, we suggest lysosomal dysfunction observed in obese adipose tissue leads to lower autophagic clearance, resulting in autophagosome accumulation. Simultaneously, lysosomal abnormalities, including deteriorated [[CTSL]] function and compensatory activation of [[CTSB]], caused cellular senescence and inflammasome activation. Our findings strongly suggest lysosomal dysfunction is involved in early pathologies of obese adipose tissue.
|mesh-terms=* 3T3-L1 Cells
* Adipocytes
* Adipose Tissue, White
* Animals
* Autophagosomes
* Autophagy-Related Proteins
* Cathepsins
* Cellular Senescence
* Diet, High-Fat
* Inflammasomes
* Lysosomes
* Male
* Mice
* Mice, Inbred C57BL
* Mice, Obese
* Obesity
* Up-Regulation
|keywords=* adipose tissue
* autophagy
* cathepsin
* inflammasome
* lysosome
* obesity
* senescence
|full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5388215
}}