gopubmed logo
 
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Cathepsin L1

cathepsin L
The protein encoded by this gene is a lysosomal cysteine proteinase that plays a major role in intracellular protein catabolism. Its substrates include collagen and elastin, as well as alpha-1 protease inhibitor, a major controlling element of neutrophil elastase activity. The encoded protein has been implicated in several pathologic processes, including myofibril necrosis in myopathies and in myocardial ischemia, and in the renal tubular response to proteinuria. This protein, which is a member of the peptidase C1 family, is a dimer composed of disulfide-linked heavy and light chains, both produced from a single protein precursor. At least two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Cathepsins, CAN, ACID, HAD, V1a
Papers using cathepsin L antibodies
In search of an "autophagomometer"
Supplier
Halayko A J et al., In Cell Death & Disease, 2008
... Rabbit anti-NOXA, anti-ATF6, anti-ATF4, anti-XBP1, anti-caspase-4, Cathepsin-B and mouse anti-Cathepsin L were obtained from Abcam (Cambridge, MA, USA) ...
Ca2+-independent cytotoxicity of Vibrio parahaemolyticus thermostable direct hemolysin (TDH) on Intestine 407, a cell line derived from human embryonic intestine.
Supplier
Gilmore Michael S., In PLoS Pathogens, 1994
... Protease inhibitors, calpeptin and cathepsin L inhibitor I were purchased from Calbiochem (Merck KgaA, Darmstadt, Germany) and ...
Papers on cathepsin L
Analyses of Histone Proteoforms Using Front-End Electron Transfer Dissociation-Enabled Orbitrap Instruments.
New
Hunt et al., United States. In Mol Cell Proteomics, Feb 2016
Results of follow-up in vitro experiments suggest that some of the truncated histone H2A proteoforms we observed can be generated by Cathepsin L, an enzyme known to also catalyze clipping of histone H3.
Factor H uptake regulates intracellular C3 activation during apoptosis and decreases the inflammatory potential of nucleosomes.
New
Blom et al., Lund, Sweden. In Cell Death Differ, Feb 2016
Here we report that FH is actively internalized by apoptotic cells to enhance cathepsin L-mediated cleavage of endogenously expressed C3, which results in increased surface opsonization with iC3b.
Screening and Characterization of Genes Involved in the Processing of Lipid-Containing Droplets in C. elegans Embryos.
New
Döring et al., Kiel, Germany. In Genetics, Feb 2016
The genes include cpl-1 (cathepsin L-like cysteine protease), ccz-1 (guanine nucleotide exchange factor subunit), and asm-3 (acid sphingomyelinase), which is closely related to the human Niemann-Pick disease-causing gene, SMPD1.
IL-6 down-regulates HLA class II expression and IL-12 production of human dendritic cells to impair activation of antigen-specific CD4(+) T cells.
New
Taketomi et al., Sapporo, Japan. In Cancer Immunol Immunother, Feb 2016
Arginase-1 (ARG1), lysosomal protease, cathepsin L (CTSL), and cyclooxygenase-2 (COX2) were involved in the reduction of surface HLA-DR expression.
Cathepsin L of the sea cucumber Apostichopus japonicus-molecular characterization and transcriptional response to Vibrio splendidus infection.
New
Wang et al., Zhoushan, China. In Fish Shellfish Immunol, Feb 2016
UNASSIGNED: Cathepsin L, a lysosomal endopeptidase, has been noted for its involvement in the innate immune response in invertebrates.
Cathepsin L targeting in cancer treatment.
Review
New
Siemann et al., Gainesville, United States. In Pharmacol Ther, Nov 2015
One such enzyme is cathepsin L (CTSL), a lysosomal cysteine protease.
Trichomonas vaginalis Cysteine Proteinases: Iron Response in Gene Expression and Proteolytic Activity.
Review
Ortega-López et al., Mexico. In Biomed Res Int, 2014
In particular, we examined the effect of iron on the gene expression regulation and function of cathepsin L-like and asparaginyl endopeptidase-like CPs as virulence factors.
The Potential Role of the Proteases Cathepsin D and Cathepsin L in the Progression and Metastasis of Epithelial Ovarian Cancer.
Review
Whatmore et al., Exeter, United Kingdom. In Biomolecules, 2014
In this review we examine the role of some of these alternative factors, specifically cathepsin D and cathepsin L.
C1A cysteine protease-cystatin interactions in leaf senescence.
Review
Díaz et al., Madrid, Spain. In J Exp Bot, 2014
C1A cysteine proteases, grouped as cathepsin L-, B-, H-, and F-like according to their gene structures and phylogenetic relationships, are the most abundant enzymes responsible for the proteolytic activity during leaf senescence.
Intracellular complement activation sustains T cell homeostasis and mediates effector differentiation.
Impact
Kemper et al., Saint Louis, United States. In Immunity, 2014
We found that the T cell-expressed protease cathepsin L (CTSL) processed C3 into biologically active C3a and C3b.
Induction of protective immune responses against schistosomiasis using functionally active cysteine peptidases.
Review
Donnelly et al., Cairo, Egypt. In Front Genet, 2013
We have shown that sub-cutaneous injection of recombinant and functionally active Schistosoma mansoni cathepsin B1 (SmCB1), or a cathepsin L from a related parasite Fasciola hepatica (FhCL1), elicits highly significant protection (up to 73%) against an experimental challenge worm infection in murine models of schistosomiasis.
Cathepsins L and Z are critical in degrading polyglutamine-containing proteins within lysosomes.
GeneRIF
Goldberg et al., Boston, United States. In J Biol Chem, 2012
Cathepsins L and Z are critical in degrading polyglutamine-containing proteins within lysosomes.
Regulation of cathepsins S and L by cystatin F during maturation of dendritic cells.
GeneRIF
Kos et al., Ljubljana, Slovenia. In Eur J Cell Biol, 2012
Regulation of cathepsins S and L by cystatin F during maturation of dendritic cells.
Cathepsins B and L activate Ebola but not Marburg virus glycoproteins for efficient entry into cell lines and macrophages independent of TMPRSS2 expression.
GeneRIF
Pöhlmann et al., Hannover, Germany. In Virology, 2012
Cathepsins B and L activate Ebola but not Marburg virus glycoproteins for efficient entry into cell lines and macrophages independent of TMPRSS2 expression.
Transient expression of progesterone receptor and cathepsin-l in human granulosa cells during the periovulatory period.
GeneRIF
Devoto et al., Santiago, Chile. In Fertil Steril, 2012
Report transient expression of progesterone receptor and cathepsin-l in human granulosa cells during the periovulatory period.
Cathepsin cleavage potentiates the Ebola virus glycoprotein to undergo a subsequent fusion-relevant conformational change.
GeneRIF
White et al., Charlottesville, United States. In J Virol, 2012
Cathepsin L cleavage potentiates the Ebola virus GP to undergo a fusion-relevant conformational change.
NLRP3 inflammasomes are required for atherogenesis and activated by cholesterol crystals.
Impact
Latz et al., Worcester, United States. In Nature, 2010
Similarly, when injected intraperitoneally, cholesterol crystals induce acute inflammation, which is impaired in mice deficient in components of the NLRP3 inflammasome, cathepsin B, cathepsin L or IL-1 molecules.
Proteolytic cleavage in an endolysosomal compartment is required for activation of Toll-like receptor 9.
Impact
Ploegh et al., Cambridge, United States. In Nat Immunol, 2008
Although cathepsin L generated the requisite TLR9 cleavage products in a cell-free in vitro system, several proteases influenced TLR9 cleavage in intact cells.
Cathepsin L proteolytically processes histone H3 during mouse embryonic stem cell differentiation.
Impact
Allis et al., New York City, United States. In Cell, 2008
We map the sites of H3 cleavage and identify Cathepsin L as a protease responsible for proteolytically processing the N-terminal H3 tail.
The actin cytoskeleton of kidney podocytes is a direct target of the antiproteinuric effect of cyclosporine A.
Impact
Mundel et al., Miami, United States. In Nat Med, 2008
Preservation of this interaction, in turn, protects synaptopodin from cathepsin L-mediated degradation.
share on facebooktweetadd +1mail to friends