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Cathepsin L2

cathepsin V, cathepsin L2, CTSL2
The protein encoded by this gene, a member of the peptidase C1 family, is a lysosomal cysteine proteinase that may play an important role in corneal physiology. This gene is expressed in colorectal and breast carcinomas but not in normal colon, mammary gland, or peritumoral tissues, suggesting a possible role for this gene in tumor processes. Alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Jan 2011] (from NCBI)
Top mentioned proteins: Cathepsins, ACID, CAN, HAIR, HAD
Papers on cathepsin V
Neuropeptidomics Mass Spectrometry Reveals Signaling Networks Generated by Distinct Protease Pathways in Human Systems.
New
Bandeira et al., San Diego, United States. In J Am Soc Mass Spectrom, Nov 2015
Of particular interest is the finding that human-specific cathepsin V participates in producing enkephalin and likely other neuropeptides, indicating unique proteolytic mechanisms for generating human neuropeptides.
The HIV protease inhibitor saquinavir inhibits HMGB1 driven inflammation by targeting the interaction of cathepsin V with TLR4/MyD88.
New
Billiar et al., Galveston, United States. In Mol Med, Oct 2015
We further report on the identification of mammalian cathepsin V, a protease, as a novel target of these inhibitors.
Corneal angiogenesis modulation by cysteine cathepsins: In vitro and in vivo studies.
New
Carmona et al., São Paulo, Brazil. In Exp Eye Res, May 2015
Cathepsin V, which is highly expressed in the cornea, can hydrolyze human plasminogen to release angiostatin fragments.
Evolutionary History of Cathepsin L (L-like) Family Genes in Vertebrates.
Cai et al., Shenzhen, China. In Int J Biol Sci, 2014
Severe positive selection was also observed in cathepsin V (L2) of primates, indicating that this enzyme had some special functions.
Endostatin and cathepsin-V in bronchoalveolar lavage fluid of patients with pulmonary sarcoidosis.
Nikliński et al., Białystok, Poland. In Adv Exp Med Biol, 2014
There is no data about cathepsin V (Cath V) in bronchoalveolar lavage fluid (BALF) in humans.
Effects of methionine supplementation on the expression of protein deposition-related genes in acute heat stress-exposed broilers.
Oliveira Neto et al., Maringá, Brazil. In Plos One, 2014
The objective of this study was to evaluate the effect of heat stress and methionine supplementation on the gene expression of insulin-like growth factor I (IGF-I), growth hormone receptor (GHR), phosphatidylinositol 3-kinase, and regulatory 1 (PI3KR1) in the liver, as well as the expression of the atrogin 1 and cathepsin L2 (CTSL2) genes in the breast muscle of broilers.
Corticomedullary differentiation and maturational arrest in thymomas.
Marx et al., Göttingen, Germany. In Histopathology, 2014
The cortical markers used were B5T, PRSS16, and cathepsin V.
The marine cyanobacterial metabolite gallinamide A is a potent and selective inhibitor of human cathepsin L.
Gerwick et al., San Diego, United States. In J Nat Prod, 2014
Preincubation-dilution and activity-probe experiments revealed an irreversible mode of inhibition, and comparative IC50 values display a 28- to 320-fold greater selectivity toward cathepsin L than closely related human cysteine cathepsin V or B. Molecular docking and molecular dynamics simulations were used to determine the pose of gallinamide in the active site of cathepsin L. These data resulted in the identification of a pose characterized by high stability, a consistent hydrogen bond network, and the reactive Michael acceptor enamide of gallinamide A positioned near the active site cysteine of the protease, leading to a proposed mechanism of covalent inhibition.
Adaptive evolution and divergence of SERPINB3: a young duplicate in great Apes.
Seixas et al., Porto, Portugal. In Plos One, 2013
We detected evidence of strong positive selection throughout SERPINB4/B3 primate tree and target proteases, cathepsin L2 (CTSL2) and G (CTSG) and chymase (CMA1).
Elastin degradation by cathepsin V requires two exosites.
Brömme et al., In J Biol Chem, 2013
Cathepsin V is a highly effective elastase and has been implicated in physiological and pathological extracellular matrix degradation.
Plasma levels of cathepsins L, K, and V and risks of abdominal aortic aneurysms: a randomized population-based study.
Shi et al., Wuhan, China. In Atherosclerosis, 2013
BACKGROUND: Cathepsin L (CatL), cathepsin K (CatK), and cathepsin V (CatV) are potent elastases implicated in human arterial wall remodeling.
Tumor necrosis factor alpha stimulates cathepsin K and V activity via juxtacrine monocyte-endothelial cell signaling and JNK activation.
GeneRIF
Platt et al., Atlanta, United States. In Mol Cell Biochem, 2012
inflammatory cues and monocyte-endothelial cell interactions upregulate cathepsin K and V activity via a JNK signaling axis
Expression of cysteine protease cathepsin L is increased in endometrial cancer and correlates with expression of growth regulatory genes.
GeneRIF
Treeck et al., Regensburg, Germany. In Cancer Invest, 2012
CTSL2 might be involved in progression of endometrial cancer.
Human cathepsin V protease participates in production of enkephalin and NPY neuropeptide neurotransmitters.
GeneRIF
Hook et al., San Diego, United States. In J Biol Chem, 2012
Findings indicate the unique function of cathepsin V for producing enkephalin and neuropeptide Y (NPY) neuropeptides required for neurotransmission in health and neurological diseases.
Expression of human cathepsin L or human cathepsin V in mouse thymus mediates positive selection of T helper cells in cathepsin L knock-out mice.
GeneRIF
Reinheckel et al., Freiburg, Germany. In Biochimie, 2010
functions of CTSL and CTSV in the positive selection of CD4+ T cells
Nuclear cysteine cathepsin variants in thyroid carcinoma cells.
GeneRIF
Brix et al., Bremen, Germany. In Biol Chem, 2010
A proteolytically active variant of cathepsin V is localized to cell nucleus (in peri-nucleolar pattern) in thyroid carcinoma cells.
The biology of cystatin M/E and its cognate target proteases.
Review
Schalkwijk et al., Nijmegen, Netherlands. In J Invest Dermatol, 2009
Cystatin M/E directly controls the activity of cathepsin V, cathepsin L, and legumain, thereby regulating the processing of transglutaminases.
Fasciola hepatica cathepsin L-like proteases: biology, function, and potential in the development of first generation liver fluke vaccines.
Review
Donnelly et al., Dublin, Ireland. In Int J Parasitol, 2003
The major proteases, cathepsin L1 (FheCL1) and cathepsin L2 (FheCL2) are members of a lineage that gave rise to the human cathepsin Ls, Ks and Ss, but while they exhibit similarities in their substrate specificities to these enzymes they differ in having a wider pH range for activity and an enhanced stability at neutral pH.
Characteristics of the human ocular surface epithelium.
Review
Okubo et al., Kyoto, Japan. In Prog Retin Eye Res, 2001
We also provide a summary of several genes abundantly or uniquely expressed in the human corneal epithelium, namely clusterin, keratin 3, keratin 12, aldehyde dehydrogenase 3 (ALDH3), troponin-I fast-twitch isoform, ssig-h3, cathepsin L2 (cathepsin V), uroplakin Ib, and Ca(2+)-activated chloride channel.
Proteinases and associated genes of parasitic helminths.
Review
Dalton et al., Dublin, Ireland. In Adv Parasitol, 1998
For example, proteinases expressed by the various stages of the schistosome life-cycle, in particular the well-characterized cercarial elastase which is involved in the penetration of the host skin and the variety of proteinases, such as cathepsin B (Sm31), cathepsin L1, cathepsin L2, cathepsin D, cathepsin C and legumain (Sm32), which are believed to be involved in the catabolism of host haemoglobin.
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