Publication for Ctsl and Lgmn

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
mmu	Ctsl	cathepsin L	13039			[link]
mmu	Lgmn	legumain	19141

Pubmed ID	Priority	Text
26343333	0.98	catL-serpinB1-AEP module.
	0.98	catL, serpinB1 and AEP form an intracellular regulatory module that contributes to the control of Th17 differentiation.
	0.98	catL (Fig. 4), serpinB1 (Fig. 1E) and AEP (Fig. 6A).
	0.98	AEP localized to endosomes separate from the lysosomes containing the bulk of cathepsins, we speculate that the two forms of catL localize in Th17 cells to different compartments: SC-catL in endosomes and TC-catL in lysosomes.
	0.97	catL is biologically active in promoting Th17 generation and is counter-regulated by serpinB1 and secondarily by AEP.
	0.97	cathepsin L (catL), an endosomal/lysosomal cysteine protease, together with asparagine endopeptidase/legumain (AEP), which converts single chain catL (SC-catL) to the two-chain form, and serpinB1, a protease inhibitor previously characterized as a protective anti-inflammatory immune modulator.
	0.97	catL is antagonized by the suppressive action of SerpinB1, possibly by direct inhibition (although this has not been tested) and secondarily by degradation by AEP.
	0.96	catL and identified AEP as an additional suppressive regulator.
	0.94	asparagine endopeptidase (AEP) blocked conversion of SC-catL to TC-catL and increased generation of serpinb1-/- Th17 cells, but not wild-type Th17 cells.
	0.94	catL in Th17 cells (Fig. 4D) suggested that AEP is also expressed.
	0.94	AEP may function by regulating the effective lifetime of biologically active endosomal SC-catL. Collectively, the current study implicates a novel protease module as contributor to adaptive Th17 cell differentiation.
	0.93	AEP, an E64-insensitive cysteine protease that hydrolyses substrates C-terminal of asparagine residues, converts SC-catL to disulfide bonded TC-catL; both forms are generally thought to be biochemically active.
	0.90	Cathepsin L processing by asparagine endopeptidase (AEP) in Th17 differentiation
	0.89	catL-serpinB1-AEP module, once it is better defined, might offer a strategy to treat Th17 cell-driven inflammation and autoimmune diseases.
	0.78	cathepsin L processing by AEP on Th17 differentiation.
27182703	0.98	AEP-/-, CatL-/- and CatS-/- mice are as resistant to L. major infection as WT mice, suggesting that these proteases are not individually involved in TLR9 processing.
	0.97	asparagine endopeptidase (AEP) and other cysteine proteases such as cathepsins B (CatB), L (CatL) or S (CatS).
	0.95	AEP-/-, CatL-/-, CatS-/- or CatB-/- mice reproduced the susceptibility of TLR9-/- to L. major infection in terms of lesion size and parasite clearance we concluded that these proteases are not individually involved in TLR9 functional maturation.
	0.94	asparagine endopeptidase (AEP) or cysteine protease cathepsins B (CatB), L (CatL) and S (CatS) to host resistance during Leishmania major (L. major) infection in C57BL/6 (WT) mice and whether they would impact on TLR9 signaling.
	0.93	AEP, CatB, CatL and CatS affect the immune response during L. major infection with the aim of assessing if TLR9-dependent responses are affected by these proteases.
	0.89	AEP, CatB, CatL and CatS, we observed that only CatB-deficient mice were more resistant to infection, meaning they resolve lesions and reduce parasite burdens faster than C57BL/6 (WT) mice.
	0.83	AEP, CatL and CatS are not individually implicated in the maturation of TLR9 and do not play a major role in L. major infection.
	0.52	AEP-/-, and CatL-/-mice had similar lesion sizes and parasite burdens as compared to WT mice (Fig 1A-1C and S1 Fig).
30559339	0.98	CtsL, the still intact promoter region of the AEP gene and other hydrolase genes in AEP-/- compared with WT cells (Fig. 6a, b and Supplementary Fig. 6a).
	0.98	AEP, CtsB, CtsL, CtsD and CtsH (Fig. 6e and Supplementary Fig. 7) consistent with an increase in protease activity levels (Fig. 6g).
	0.98	AEP status since kidneys from STAT3c mice also showed striking increases in many of the proteins that were induced by AEP-deficiency or protein overload including CtsD and CtsL, Ym1, Gns and AEP (Fig. 8d).
	0.97	CtsL, which accumulates in its active single chain (SC) form when AEP is absent, and other hydrolases such as the active single chain form of CtsD were higher in AEP-null kidney (Fig. 1c).
	0.97	AEP inhibition increased mRNA levels of AEP, CtsD and CtsL while genetic deletion of AEP induced even more substantial mRNA increases for CtsD and CtsL (Fig. 1g).
26308073	0.98	legumain, also inhibits osteoclastogenesis, in part through modulation of cathepsin L activity.
	0.98	legumain is responsible for cleavage and activation of cathepsin L in osteoclasts.
	0.93	Legumain inhibitors promote osteoclastogenesis through modulation of cathepsin L activation
28596234	0.98	cathepsin L (CtsL) and CTSV and the asparaginyl endopeptidase legumain (LGMN).
	0.98	Lgmn-/-, and Cst6-/-Ctsl-/- double-knockout mice and have shown that a tightly regulated balance between the protease CtsL and Cst6 is essential for tissue integrity of the epidermis and for maintenance of corneal epithelium.
24065969	0.98	AEP-deficient mice exhibit a defect in the maturation of Cat B, Cat D, Cat H, and Cat L in kidney and bone marrow derived dendritic cells (BMDCs) and an increase in Cat K expression.
25279834	0.98	Ctsl, Ctss, Lgmn) and for a reducing agent important in antigen processing (Ifi30/Gilt) were also up-regulated particularly in SF neutrophils ( Fig. 2E ).
29088746	0.98	asparaginyl endopeptidase (legumain)) to sub-pM (cathepsin L) affinity.
30405635	0.98	AEP has been shown to be involved in the processing of single-chain CTSL into the double-chain form in mice.
29872438	0.97	Cathepsin L (Ctsl) and Legumain (Lgmn) was seen in spleens 1-5 days after experimental stroke in comparison to sham-operated controls (Figure 4I) and increased expression of Ctsl mRNA was confirmed by RT-qPCR suggesting there was no impairment in proteolytic processing of endocytosed material in the spleen after experimental stroke (Figure 4J).
31092553	0.88	CtsL), and AEP can generate these peptides, with the majority attributable to cysteine cathepsins.