Ask about this productRelated genes to: LANCL3 antibody
- Gene:
- LANCL3 NIH gene
- Name:
- LanC like 3
- Previous symbol:
- -
- Synonyms:
- FLJ42925
- Chromosome:
- Xp21.1
- Locus Type:
- gene with protein product
- Date approved:
- 2005-01-12
- Date modifiied:
- 2016-01-06
Related products to: LANCL3 antibody
Related articles to: LANCL3 antibody
- Lanthionine synthetase C-like protein (Lancl) gene family members 1-3 play roles in responses to oxidative stress and cellular metabolic processes. Lancl1 in particular functions as a neuroprotective factor in the central nervous system (CNS), but it is unknown whether experimentally upregulating Lancl1 in neurons could also repair injured circuits by regenerating damaged axons. We recently identified Lancl1 as a gene upregulated in response to an axon-regenerating treatment, which prompted us to ask here if Lancl1 could directly repair injured axons. First, we characterized expression of Lancl1-3 family genes in single-cell RNA-seq (scRNA-seq)-profiled retinal ganglion cell (RGC) CNS projection neurons, then we investigated through gain-of-function experiments whether Lancl1 promotes axon regeneration after CNS injury in vivo, and finally we tested if Lancl1 transgene activates the mTOR pathway's pS6 marker, which is associated with Pten knockout-promoted axon regeneration. We show that within the retina, Lancl1 and Lancl2 are enriched in the RGCs, whereas Lancl3 is not considerably expressed in retinal cell types. Within the RGCs, there is moderate subtype-to-subtype variability in Lancl1 and Lancl2 expression, whereas Lancl3 is enriched in αRGCs but expressed at modest levels. We then found that after optic nerve injury, Lancl1 transgene targeted to RGCs through intravitreal AAV2 promotes neuroprotection and axon regeneration, with axons extending through the full-length of the optic nerve when co-treated with a fibronectin-based recombinant small protein. However, we did not find that Lancl1 transgene activates the mTOR pathway's pS6 marker in injured RGCs. Thus, Lancl1 is a novel axon regeneration-promoting factor with a therapeutic potential for treating CNS injury and disease, and future studies need to investigate downstream mechanisms of its neurotherapeutic efficacy. - Source: PubMed
Publication date: 2026/04/17
Lukomska AgnieszkaFrost Matthew PBrady JacobKearney AnjaBalaji Arnav JD'Souza ClydeTrakhtenberg Ephraim F - Enzyme-mediated damage repair or mitigation, while common for nucleic acids, is rare for proteins. Examples of protein damage are elimination of phosphorylated Ser/Thr to dehydroalanine/dehydrobutyrine (Dha/Dhb) in pathogenesis and aging. Bacterial LanC enzymes use Dha/Dhb to form carbon-sulfur linkages in antimicrobial peptides, but the functions of eukaryotic LanC-like (LanCL) counterparts are unknown. We show that LanCLs catalyze the addition of glutathione to Dha/Dhb in proteins, driving irreversible C-glutathionylation. Chemo-enzymatic methods were developed to site-selectively incorporate Dha/Dhb at phospho-regulated sites in kinases. In human MAPK-MEK1, such "elimination damage" generated aberrantly activated kinases, which were deactivated by LanCL-mediated C-glutathionylation. Surveys of endogenous proteins bearing damage from elimination (the eliminylome) also suggest it is a source of electrophilic reactivity. LanCLs thus remove these reactive electrophiles and their potentially dysregulatory effects from the proteome. As knockout of LanCL in mice can result in premature death, repair of this kind of protein damage appears important physiologically. - Source: PubMed
Publication date: 2021/04/30
Lai Kuan-YuGalan Sébastien R GZeng YiboZhou Tianhui HinaHe ChangRaj RituRiedl JitkaLiu ShiChooi K PhinGarg NehaZeng MinJones Lyn HHutchings Graham JMohammed ShabazNair Satish KChen JieDavis Benjamin Gvan der Donk Wilfred A - McLeod syndrome (MLS) is hematologically defined by the absence of the red blood cell (RBC) antigen Kx on the transmembrane RBC protein, XK, representing a highly specific diagnostic marker. Direct molecular assessment of XK therefore represents a desirable diagnostic tool. Whereas pathogenic point mutations may be simply identified, partial and complete deletions of XK on Xp21.1, eventually covering adjacent genes and causing multifaceted "continuous gene syndromes," are difficult to localize. - Source: PubMed
Publication date: 2017/05/28
Gassner ChristophBrönnimann ChantalMerki YvonneMattle-Greminger Maja PSigurdardottir SonjaMeyer EduardoEngström CharlotteO'Sullivan John DJung Hans HFrey Beat M - LanC-like (LanCL) proteins are mammalian homologs of bacterial LanC enzymes, which catalyze the addition of the thiol of Cys to dehydrated Ser residues during the biosynthesis of lanthipeptides, a class of natural products formed by post-translational modification of precursor peptides. The functions of LanCL proteins are currently unclear. A recent proposal suggested that LanCL1 catalyzes the addition of the Cys of glutathione to protein- or peptide-bound dehydroalanine (Dha) to form lanthionine, analogous to the reaction catalyzed by LanC in bacteria. Lanthionine has been detected in human brain as the downstream metabolite lanthionine ketimine (LK), which has been shown to have neuroprotective effects. In this study, we tested the proposal that LanCL1 is involved in lanthionine biosynthesis by constructing LanCL1 knock-out mice and measuring LK concentrations in their brains using a mass spectrometric detection method developed for this purpose. To investigate whether other LanCL proteins (LanCL2/3) may confer a compensatory effect, triple knock-out (TKO) mice were also generated and tested. Very similar concentrations of LK (0.5-2.5 nmol/g tissue) were found in LanCL1 knock-out, TKO and wild type (WT) mouse brains, suggesting that LanCL proteins are not involved in lanthionine biosynthesis. - Source: PubMed
Publication date: 2017/01/20
He ChangZeng MinDutta DebapriyaKoh Tong HeeChen Jievan der Donk Wilfred A