Ignet

Gene Information

Gene symbol: CTSD

Gene name: cathepsin D

HGNC ID: 2529

Synonyms: CLN10

Related Genes

#	Gene Symbol	Number of hits
1	ACPP	1 hits
2	APLP2	1 hits
3	ATP6V1C1	1 hits
4	C17orf88	1 hits
5	CD63	1 hits
6	CTSB	1 hits
7	CTSC	1 hits
8	CTSL1	1 hits
9	CTSL2	1 hits
10	DCTN5	1 hits
11	EEA1	1 hits
12	F10	1 hits
13	HEXA	1 hits
14	IFI30	1 hits
15	LAMP1	1 hits
16	LAMP3	1 hits
17	LGMN	1 hits
18	M6PR	1 hits
19	MAGEH1	1 hits
20	NDP	1 hits
21	REN	1 hits
22	SERPINA3	1 hits

Related Sentences

#	PMID	Sentence
1	454380	They were distinguished by their different distributions in the gradient and different sensitivities to disruption by digitonin and were termed:type A, containing lysozyme; type B, containing N-acetyl-beta-glucosaminidase, beta-glactosidase, beta-glucuronidase and possibly some lysozyme; type C, containing cathepsin D.
2	1212427	The reduced incidence of amyloidosis following BAPN adminsitration cannot be due to lysosomal enzyme degradation of the amyloid as the activity of cathepsin D and acid phosphatase is decreased during this process.
3	3913477	The antibody inhibited the enzyme activities of hog kidney renin and mouse submaxillary gland renin at concentrations 1 000 times higher than required for rat kidney renin but did not inhibit human renal renin or rat kidney cathepsin D.
4	3913477	The antibody can be used for characterizing the physiological and pathophysiological role of renin in blood pressure regulation, for the histochemical localization of renin in rat tissues and for distinguishing specific renin activity from the nonspecific renin-like activity of cathepsin D.
5	3913477	The antibody inhibited the enzyme activities of hog kidney renin and mouse submaxillary gland renin at concentrations 1 000 times higher than required for rat kidney renin but did not inhibit human renal renin or rat kidney cathepsin D.
6	3913477	The antibody can be used for characterizing the physiological and pathophysiological role of renin in blood pressure regulation, for the histochemical localization of renin in rat tissues and for distinguishing specific renin activity from the nonspecific renin-like activity of cathepsin D.
7	8834614	Aim of the present study was to evaluate cathepsin D, base protease, antiplasmin, antitrypsin and antichymotrypsin activities and protein content in the 24h culture medium of the alveolar macrophages (AM) deriving from the rats treated BCG-vaccine and from rats with papain-induced emphysema.
8	9278305	There was colocalization of the FITC-labeled Ags with early (cathepsin D) and late endosomal markers (anti-mannose-6-phosphate receptor), lysosomal markers (CD-63), and acidic compartment markers (3-(2,4-dinitroanilino)-3'-amino-N-methyldipropylamine) in the uninfected cells, but the level of colocalized Ag was reduced in the 43HIV cells and HIV-1BaL-infected monocytes.
9	10214692	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.
10	12197114	The 3 A. caninum antigens selected were Ac-TMP, an adult-specific secreted tissue inhibitor of metalloproteases; Ac-AP, an adult-specific secreted factor Xa serine protease inhibitor anticoagulant; and Ac-ARR-1, a cathepsin D-like aspartic protease.
11	12552433	Hookworm aspartic protease, Na-APR-2, cleaves human hemoglobin and serum proteins in a host-specific fashion.
12	12552433	Na-APR-2 is more similar to a family of nematode-specific, aspartic proteases than it is to cathepsin D or pepsin, and the term "nemepsins" for members of this family of nematode-specific hydrolases is proposed.
13	12552433	Recombinant Na-APR-2 cleaved human hemoglobin (Hb) and serum proteins almost twice as efficiently as the orthologous substrates from the nonpermissive dog host.
14	12552433	Moreover, only 25% of the Na-APR-2 cleavage sites within human Hb were shared with those generated by the related N. americanus cathepsin D, Na-APR-1.
15	12552433	Hookworm aspartic protease, Na-APR-2, cleaves human hemoglobin and serum proteins in a host-specific fashion.
16	12552433	Na-APR-2 is more similar to a family of nematode-specific, aspartic proteases than it is to cathepsin D or pepsin, and the term "nemepsins" for members of this family of nematode-specific hydrolases is proposed.
17	12552433	Recombinant Na-APR-2 cleaved human hemoglobin (Hb) and serum proteins almost twice as efficiently as the orthologous substrates from the nonpermissive dog host.
18	12552433	Moreover, only 25% of the Na-APR-2 cleavage sites within human Hb were shared with those generated by the related N. americanus cathepsin D, Na-APR-1.
19	15036539	Both RB51 strains were transiently observed in phagosomes characterized by the presence of the early endosomal marker EEA1 and then were found in cathepsin D-enriched lysosomal compartments, in which they eventually underwent degradation at later post-infection times.
20	15155622	We assessed the maturation of the F. tularensis phagosome by examining its acquisition of the lysosome-associated membrane glycoproteins (LAMPs) CD63 and LAMP1 and the acid hydrolase cathepsin D.
21	15155622	Two to four hours after infection, vacuoles containing live F. tularensis cells acquired abundant staining for LAMPs but little or no staining for cathepsin D.
22	15155622	These results indicate that F. tularensis initially enters a nonacidified phagosome with LAMPs but without cathepsin D and that the phagosomal membrane subsequently becomes morphologically disrupted, allowing the bacteria to gain direct access to the macrophagic cytoplasm.
23	15155622	We assessed the maturation of the F. tularensis phagosome by examining its acquisition of the lysosome-associated membrane glycoproteins (LAMPs) CD63 and LAMP1 and the acid hydrolase cathepsin D.
24	15155622	Two to four hours after infection, vacuoles containing live F. tularensis cells acquired abundant staining for LAMPs but little or no staining for cathepsin D.
25	15155622	These results indicate that F. tularensis initially enters a nonacidified phagosome with LAMPs but without cathepsin D and that the phagosomal membrane subsequently becomes morphologically disrupted, allowing the bacteria to gain direct access to the macrophagic cytoplasm.
26	15155622	We assessed the maturation of the F. tularensis phagosome by examining its acquisition of the lysosome-associated membrane glycoproteins (LAMPs) CD63 and LAMP1 and the acid hydrolase cathepsin D.
27	15155622	Two to four hours after infection, vacuoles containing live F. tularensis cells acquired abundant staining for LAMPs but little or no staining for cathepsin D.
28	15155622	These results indicate that F. tularensis initially enters a nonacidified phagosome with LAMPs but without cathepsin D and that the phagosomal membrane subsequently becomes morphologically disrupted, allowing the bacteria to gain direct access to the macrophagic cytoplasm.
29	16920965	Processing and presentation of a mycobacterial antigen 85B epitope by murine macrophages is dependent on the phagosomal acquisition of vacuolar proton ATPase and in situ activation of cathepsin D.
30	16920965	Macrophages were infected with GFP-expressing mycobacterial strains and analyzed for in situ localization of vacuolar proton ATPase (v-ATPase) and cathepsin D (Cat D) using Western blot analysis and immunofluorescence.
31	16920965	Processing and presentation of a mycobacterial antigen 85B epitope by murine macrophages is dependent on the phagosomal acquisition of vacuolar proton ATPase and in situ activation of cathepsin D.
32	16920965	Macrophages were infected with GFP-expressing mycobacterial strains and analyzed for in situ localization of vacuolar proton ATPase (v-ATPase) and cathepsin D (Cat D) using Western blot analysis and immunofluorescence.
33	18343923	We also show that GILT expression influences the generation of active forms of cysteinyl proteases, cathepsins B, L and S, as well as an aspartyl protease cathepsin D in melanoma cells.
34	18343923	GILT expression in melanoma cells also elevated HLA-DM molecules, which favor epitope loading onto class II in the endolysosomal compartments, enhancing CD4+ T cell recognition.
35	18343923	These data suggest that GILT-expressing melanoma cells could prove to be very promising for direct antigen presentation and CD4+ T cell recognition, and may have direct implications for the design of cancer vaccines.
36	19349423	Comparison of the migR and fevR mutants in monocyte-derived macrophages (MDMs) and epithelial cell lines revealed a reduced ability for each mutant to grow in MDMs, yet only the fevR mutant exhibited impaired replication in epithelial cell lines.
37	19349423	Confocal analysis of infected MDMs revealed that although neither mutant reached the MDM cytosol, the fevR mutant was trapped in lamp-1-positive phagosomes, whereas the migR mutant resided in mature phagolysosomes enriched with both lamp-1 and cathepsin D.
38	19349423	Disruption of migR and fevR also impaired the ability of F. tularensis to prevent neutrophil oxidant production.
39	24231271	Using molecular modeling we showed that S. mansoni cathepsin D possesses a predicted surface exposed α-helix (A₂₆₃K) that corresponds to an immunodominant helix and target of enzyme-neutralizing antibodies against Necator americanus APR-1 (Na-APR-1), the orthologous protease and vaccine antigen from blood-feeding hookworms.
40	25684420	In this study, we have developed vaccine candidates that composed of three components: a B-cell epitope derived from S. mansoni cathepsin D protein (Sm-CatD) flanked by GCN4 helix promoting peptide; a promiscuous T-helper epitope (P25); and a lipid core peptide system, in attempt to develop self-adjuvanting vaccine candidates against the schistosome.