Figura, Kurt von

[["dc.bibliographiccitation.firstpage","1733"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Journal of Clinical Investigation"],["dc.bibliographiccitation.lastpage","1745"],["dc.bibliographiccitation.volume","111"],["dc.contributor.author","Friedrich, Bianca"],["dc.contributor.author","Tepel, C."],["dc.contributor.author","Reinheckel, T."],["dc.contributor.author","Deussing, J. M."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Herzog, V."],["dc.contributor.author","Peters, C."],["dc.contributor.author","Saftig, P."],["dc.contributor.author","Brix, K."],["dc.date.accessioned","2018-11-07T10:38:39Z"],["dc.date.available","2018-11-07T10:38:39Z"],["dc.date.issued","2003"],["dc.description.abstract","Thyroid function depends on processing of the prohormone thyroglobulin by sequential proteolytic events. From in vitro analysis it is known that cysteine proteinases mediate proteolytic processing of thyroglobulin. Here, we have analyzed mice with deficiencies in cathepsins B, K, L, B and K, or K and L in order to investigate which of the cysteine proteinases is most important for proteolytic processing of thyroglobulin in vivo. Immunolabeling demonstrated a rearrangement of the endocytic system and a redistribution of extracellularly located enzymes in thyroids of cathepsin-deficient mice. Cathepsin L was upregulated in thyroids of cathepsin K-/- or B-/-/K-/- mice, suggesting a compensation of cathepsin L for cathepsin K deficiency. Impaired proteolysis resulted in the persistence of thyroglobulin in the thyroids of mice with deficiencies in cathepsin B or L. The typical multilayered appearance of extracellularly stored thyroglobulin was retained in cathepsin K-/- mice only. These results suggest that cathepsins B and L are involved in the solubilization of thyroglobulin from its covalently cross-linked storage form. Cathepsin K-/-/L-/- mice had significantly reduced levels of free thyroxine, indicating that utilization of luminal thyroglobulin for thyroxine liberation is mediated by a combinatory action of cathepsins K and L."],["dc.identifier.doi","10.1172/JCI200315990"],["dc.identifier.isi","000183313400017"],["dc.identifier.pmid","12782676"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/45858"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1558-8238"],["dc.relation.issn","0021-9738"],["dc.title","Thyroid functions of mouse cathepsins B, K, and L"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1713"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","American Journal Of Pathology"],["dc.bibliographiccitation.lastpage","1728"],["dc.bibliographiccitation.volume","167"],["dc.contributor.author","Koike, M."],["dc.contributor.author","Shibata, M."],["dc.contributor.author","Waguri, S."],["dc.contributor.author","Yoshimura, K."],["dc.contributor.author","Tanida, I."],["dc.contributor.author","Kominami, E."],["dc.contributor.author","Gotow, T."],["dc.contributor.author","Peters, C."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Mizushima, N."],["dc.contributor.author","Saftig, P."],["dc.contributor.author","Uchiyama, Y."],["dc.date.accessioned","2018-11-07T10:53:39Z"],["dc.date.available","2018-11-07T10:53:39Z"],["dc.date.issued","2005"],["dc.description.abstract","In cathepsin D-deficient (CD-/-) and cathepsins B and L double-deficient (CB-/-CL-/-) mice, abnormal vacuolar structures accumulate in neurons of the brains. Many of these structures resemble autophagosomes in which part of the cytoplasm is retained but their precise nature and biogenesis remain unknown. We show here how autophagy contributes to the accumulation of these vacuolar structures in neurons deficient in cathepsin D or both cathepsins B and L by demonstrating an increased conversion of the molecular form of MAP1-LC3 for autophagosome formation from the cytosolic form (LC3-I) to the membrane-bound form (LC3-II). in both CD-/- and CB-/-CL-/- mouse brains, the membrane-bound LC3-II form predominated whereas MAP1-LC3 signals accumulated in granular structures located in neuronal perikarya and axons of these mutant brains and were localized to the membranes of autophagosomes, evidenced by immunofluorescence microscopy and freeze-fracture-replica immunoelectron microscopy. Moreover, as in CD-/- neurons, autofluorescence and subunit c of mitochondrial ATP synthase accumulated in CB-/-CL-/- neurons. This suggests that not only CD-/- but also CB-/-CL-/- mice could be useful animal models for neuronal ceroid-lipofuscinosis/Batten disease. These data strongly argue for a major involvement of autophagy in the pathogenesis of Batten disease/lysosomal storage disorders."],["dc.identifier.doi","10.1016/S0002-9440(10)61253-9"],["dc.identifier.isi","000233573600022"],["dc.identifier.pmid","16314482"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/49395"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Investigative Pathology, Inc"],["dc.relation.issn","0002-9440"],["dc.title","Participation of autophagy in storage of lysosomes in neurons from mouse models of neuronal ceroid-lipofuscinoses (Batten disease)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","7526"],["dc.bibliographiccitation.issue","19"],["dc.bibliographiccitation.journal","Journal of Neuroscience"],["dc.bibliographiccitation.lastpage","7533"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Nakanishi, H."],["dc.contributor.author","Zhang, J."],["dc.contributor.author","Koike, M."],["dc.contributor.author","Nishioku, T."],["dc.contributor.author","Okamoto, Y."],["dc.contributor.author","Kominami, E."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Peters, C."],["dc.contributor.author","Yamamoto, K."],["dc.contributor.author","Saftig, P."],["dc.contributor.author","Uchiyama, Y."],["dc.date.accessioned","2018-11-07T08:36:23Z"],["dc.date.available","2018-11-07T08:36:23Z"],["dc.date.issued","2001"],["dc.description.abstract","Cathepsin D (CD) deficiency has been shown to induce ceroid-lipofuscin storage in lysosomes of mouse CNS neuron (Koike et a[., 2000). To understand the behavior of microglial cells corresponding to these neuronal changes, CD-deficient (CD-/-) mice, which die at approximately postnatal day (P) 25 by intestinal necrosis, were examined using morphological as well as biochemical approaches. Light and electron microscopic observations revealed that microglia showing large round cell bodies with few processes appeared in the cerebral cortex and thalamus after P16. At P24, microglia often encircled neurons that were occupied with autolysosomes, indicating increased phagocytic activity. These morphologically transformed microglia markedly expressed inducible nitric oxide synthase (iNOS), which was also detected in the intestine of the mice. To assess the role of microglial nitric oxide (NO) in neuropathological changes in CD-/- mice, L-N-G-nitro-arginine methylester (L-NAME), a competitive NOS inhibitor, or S-methylisothiourea hemisulfate (SMT), an iNOS inhibitor, was administered intraperitoneally for 13 consecutive days. The total number of terminal deoxynucleotidyl transferase-mediated biotinylated UTP nick end labeling-positive cells counted in the thalamus was found to be significantly decreased by chronic treatment of L-NAME or SMT, whereas neither the neuronal accumulation of ceroid-lipofuscin nor the microglial phagocytic activity was affected by these treatments. Moreover, the chronic treatment Of L-NAME or SMT completely suppressed hemorrhage-necrotic changes in the small intestine of CD-/- mice, resulting in normal growth of the body weight of the mice. These results suggest that NO production via iNOS activity in microglia. and peripheral macrophages contributes to secondary tissue damages such as neuronal apoptosis and intestinal necrosis, respectively."],["dc.identifier.isi","000171154000014"],["dc.identifier.pmid","11567042"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18301"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Soc Neuroscience"],["dc.relation.issn","0270-6474"],["dc.title","Involvement of nitric oxide released from microglia-macrophages in pathological changes of cathepsin D-deficient mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","146"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Molecular and Cellular Neuroscience"],["dc.bibliographiccitation.lastpage","161"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Koike, M."],["dc.contributor.author","Shibata, M."],["dc.contributor.author","Ohsawa, Y."],["dc.contributor.author","Nakanishi, H."],["dc.contributor.author","Koga, T."],["dc.contributor.author","Kametaka, S."],["dc.contributor.author","Waguri, S."],["dc.contributor.author","Momoi, T."],["dc.contributor.author","Kominami, E."],["dc.contributor.author","Peters, C."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Saftig, P."],["dc.contributor.author","Uchiyama, Y."],["dc.date.accessioned","2018-11-07T10:41:25Z"],["dc.date.available","2018-11-07T10:41:25Z"],["dc.date.issued","2003"],["dc.description.abstract","To understand the mechanisms of retinal atrophy in cathepsin D-deficient mice, the postnatal development of their retinae was analyzed. TUNEL-positive cells appeared abundantly in the outer nuclear layer (ONL) and slightly in the inner nuclear layer (INL). Nitric oxide synthase (NOS) was induced in microglial cells which invaded retinal layers and phagocytosed dead cell debris, while NOS inhibitors prevented cell death in the INL but not in the ONL. Caspases 9 and 3 were activated only in the ONL after P15. Moreover, no atrophic change was detected in the retina of mice deficient in cathepsin B or L. These results suggest that cathepsin D is essential for the metabolic maintenance of retinal photoreceptor cells and that its deficiency induces apoptosis of the cells, while the loss of INL neurons is mediated by NO from microglial cells. (C) 2003 Elsevier Science (USA). All rights reserved."],["dc.identifier.doi","10.1016/S1044-7431(03)00035-6"],["dc.identifier.isi","000182046400002"],["dc.identifier.pmid","12676526"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/46527"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Inc Elsevier Science"],["dc.relation.issn","1044-7431"],["dc.title","Involvement of two different cell death pathways in retinal atrophy of cathepsin D-deficient mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Tepel, C."],["dc.contributor.author","Deussing, J. M."],["dc.contributor.author","Reinheckel, T."],["dc.contributor.author","Saftig, P."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Peters, C."],["dc.contributor.author","Herzog, V."],["dc.contributor.author","Brix, K."],["dc.date.accessioned","2018-11-07T10:49:47Z"],["dc.date.available","2018-11-07T10:49:47Z"],["dc.date.issued","2000"],["dc.format.extent","323A"],["dc.identifier.isi","000165525901683"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/48510"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Cell Biology"],["dc.publisher.place","Bethesda"],["dc.relation.issn","1059-1524"],["dc.title","Cathepsin-deficient mice show aberrations in thyroid morphology and physiology"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4816"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","4822"],["dc.bibliographiccitation.volume","277"],["dc.contributor.author","Nishioku, T."],["dc.contributor.author","Hashimoto, Koichi"],["dc.contributor.author","Yamashita, K."],["dc.contributor.author","Liou, S. Y."],["dc.contributor.author","Kagamiishi, Y."],["dc.contributor.author","Maegawa, H."],["dc.contributor.author","Katsube, N."],["dc.contributor.author","Peters, C."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Saftig, P."],["dc.contributor.author","Katunuma, N."],["dc.contributor.author","Yamamoto, K."],["dc.contributor.author","Nakanishi, H."],["dc.date.accessioned","2018-11-07T10:31:55Z"],["dc.date.available","2018-11-07T10:31:55Z"],["dc.date.issued","2002"],["dc.description.abstract","We have attempted to elucidate an involvement of cathepsin E (CE) in major histocompatibility complex class II-mediated antigen presentation by microglia. In primary cultured murine microglia, CE was localized mainly in early endosomes and its expression level was markedly increased upon stimulation with interferon-gamma. Pepstatin A, a specific inhibitor of aspartic proteases, significantly inhibited interleukin-2 production from an OVA-(266-281)-specific T helper cell hybridomas upon stimulation with native OVA presented by interferon-gamma-treated microglia. However, pepstatin A failed to inhibit the presentation of OVA-(266-281) peptide. The possible involvement of CE in the processing of native OVA into antigenic peptide was further substantiated by that digested fragments of native OVA by CE could be recognized by OVA-specific Th cells. Cathepsin D also degraded native OVA into antigenic peptide, whereas microglia prepared from cathepsin D-deficient mice retained an ability for antigen presentation. On the other hand, the requirement for cysteine proteases such as cathepsins S and B in the processing of invariant chain (Ii) was confirmed by immunoblot analyses in the presence of their specific inhibitors. In conclusion, CE is required for the generation of an antigenic epitope from OVA but not for the processing of Ii in microglia."],["dc.identifier.doi","10.1074/jbc.M108382200"],["dc.identifier.isi","000173962900036"],["dc.identifier.pmid","11719510"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/44223"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","0021-9258"],["dc.title","Involvement of cathepsin E in exogenous antigen processing in primary cultured murine microglia"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","6898"],["dc.bibliographiccitation.issue","18"],["dc.bibliographiccitation.journal","Journal of Neuroscience"],["dc.bibliographiccitation.lastpage","6906"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Koike, M."],["dc.contributor.author","Nakanishi, H."],["dc.contributor.author","Saftig, P."],["dc.contributor.author","Ezaki, J."],["dc.contributor.author","Isahara, K."],["dc.contributor.author","Ohsawa, Y."],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.contributor.author","Watanabe, T."],["dc.contributor.author","Waguri, S."],["dc.contributor.author","Kametaka, S."],["dc.contributor.author","Shibata, M."],["dc.contributor.author","Yamamoto, K."],["dc.contributor.author","Kominami, E."],["dc.contributor.author","Peters, C."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Uchiyama, Y."],["dc.date.accessioned","2018-11-07T10:10:58Z"],["dc.date.available","2018-11-07T10:10:58Z"],["dc.date.issued","2000"],["dc.description.abstract","Cathepsin D-deficient (CD-/-) mice have been shown to manifest seizures and become blind near the terminal stage [approximately postnatal day (P) 26]. We therefore examined the morphological, immunocytochemical, and biochemical features of CNS tissues of these mice. By electron microscopy, autophagosome/ autolysosome-like bodies containing part of the cytoplasm, granular osmiophilic deposits, and fingerprint profiles were demonstrated in the neuronal perikarya of CD-/- mouse brains after P20. Autophagosomes and granular osmiophilic deposits were detected in neurons at P0 but were few in number, whereas they increased in the neuronal perikarya within days after birth. Some large-sized neurons having autophagosome/ autolysosome-like bodies in the perikarya appeared in the CNS tissues, especially in the thalamic region and the cerebral cortex, at P17. These lysosomal bodies occupied the perikarya of almost all neurons in CD-/- mouse brains obtained from P23 until the terminal stage. Because these neurons exhibited autofluorescence, it was considered that ceroid lipofuscin may accumulate in lysosomal structures of CD-/- neurons. Subunit c of mitochondrial ATP synthase was found to accumulate in the lysosomes of neurons, although the activity of tripeptidyl peptidase-I significantly increased in the brain. Moreover, neurons near the terminal stage were often shrunken and possessed irregular nuclei through which small dense chromatin masses were scattered. These results suggest that the CNS neurons in CD-/- mice show a new form of lysosomal accumulation disease with a phenotype resembling neuronal ceroid lipofuscinosis."],["dc.identifier.isi","000089379000020"],["dc.identifier.pmid","10995834"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39956"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Soc Neuroscience"],["dc.relation.issn","0270-6474"],["dc.title","Cathepsin D deficiency induces lysosomal storage with ceroid lipofuscin in mouse CNS neurons"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","680"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Neurochemistry"],["dc.bibliographiccitation.lastpage","690"],["dc.bibliographiccitation.volume","94"],["dc.contributor.author","Shimizu, T."],["dc.contributor.author","Hayashi, Y."],["dc.contributor.author","Yamasaki, R."],["dc.contributor.author","Yamada, J."],["dc.contributor.author","Zhang, J."],["dc.contributor.author","Ukai, K."],["dc.contributor.author","Koike, M."],["dc.contributor.author","Mine, K."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Peters, C."],["dc.contributor.author","Saftig, P."],["dc.contributor.author","Fukuda, T."],["dc.contributor.author","Uchiyama, Y."],["dc.contributor.author","Nakanishi, H."],["dc.date.accessioned","2018-11-07T11:02:10Z"],["dc.date.available","2018-11-07T11:02:10Z"],["dc.date.issued","2005"],["dc.description.abstract","Although of clinical importance, little is known about the mechanism of seizure in neuronal ceroid lipofuscinosis (NCL). In the present study, we have attempted to elucidate the mechanism underlying the seizure of cathepsin D-deficient (CD-/-) mice that show a novel type of lysosomal storage disease with a phenotype resembling late infantile NCL. In hippocampal slices prepared from CD-/- mice at post-natal day (P)24, spontaneous burst discharges were recorded from CA3 pyramidal cells. At P24, the mean amplitude of IPSPs after stimulation of the mossy fibres was significantly smaller than that of wild-type mice, which was substantiated by the decreased level of gamma-aminobutyric acid (GABA) contents in the hippocampus measured by high-performance liquid chromatography (HPLC). At this stage, activated microglia were found to accumulate in the pyramidal cell layer of the hippocampal CA3 subfield of CD-/- mice. However, there was no significant change in the numerical density of GABAergic interneurons in the CA3 subfield of CD-/- mice at P24, estimated by counting the number of glutamate decarboxylase (GAD) 67-immunoreactive somata. In the hippocampus and the cortex of CD-/- mice at P24, some GABAergic interneurons displayed extremely high somatic granular immunoreactivites for GAD67, suggesting the lysosomal accumulation of GAD67. GAD67 levels in axon terminals abutting on to perisomatic regions of hippocampal CA3 pyramidal cells was not significantly changed in CD-/- mice even at P24, whereas the total protein levels of GAD67 in both the hippocampus and the cortex of CD-/- mice after P24 were significantly decreased as a result of degradation. Furthermore, the recombinant human GAD65/67 was rapidly digested by the lysosomal fraction prepared from the whole brain of wild-type and CD-/- mice. These observations strongly suggest that the reduction of GABA contents, presumably because of lysosomal degradation of GAD67 and lysosomal accumulation of its degraded forms, are responsible for the dysfunction of GABAergic interneurons in the hippocampal CA3 subfield of CD-/- mice."],["dc.identifier.doi","10.1111/j.1471-4159.2005.03250.x"],["dc.identifier.isi","000230963100012"],["dc.identifier.pmid","15992379"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/51315"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","0022-3042"],["dc.title","Proteolytic degradation of glutamate decarboxylase mediates disinhibition of hippocampal CA3 pyramidal cells in cathepsin D-deficient mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2075"],["dc.bibliographiccitation.issue","13"],["dc.bibliographiccitation.journal","The FASEB Journal"],["dc.bibliographiccitation.lastpage","2086"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Roth, W."],["dc.contributor.author","Deussing, J. M."],["dc.contributor.author","Botchkarev, V. A."],["dc.contributor.author","Pauly-Evers, M."],["dc.contributor.author","Saftig, P."],["dc.contributor.author","Hafner, A."],["dc.contributor.author","Schmidt, P."],["dc.contributor.author","Schmahl, Wolfgang"],["dc.contributor.author","Scherer, J."],["dc.contributor.author","Anton-Lamprecht, I."],["dc.contributor.author","von Figura, K."],["dc.contributor.author","Paus, R."],["dc.contributor.author","Peters, C."],["dc.date.accessioned","2018-11-07T09:31:02Z"],["dc.date.available","2018-11-07T09:31:02Z"],["dc.date.issued","2000"],["dc.description.abstract","Lysosomal cysteine proteinases of the papain family are involved in lysosomal bulk proteolysis, major histocompatibility complex class II mediated antigen presentation, prohormone processing, and extracellular matrix remodeling. Cathepsin L (CTSL) is a ubiquitously expressed major representative of the papain-like family of cysteine proteinases. To investigate CTSL in vivo functions, the gene was inactivated by gene targeting in embryonic stem cells. CTSL-deficient mice develop periodic hair loss and epidermal hyperplasia, acanthosis, and hyperkeratosis. The hair loss is due to alterations of hair follicle morphogenesis and cycling, dilatation of hair follicle canals, and disturbed club hair formation. Hyperproliferation of hair follicle epithelial cells and basal epidermal keratinocytes-both of ectodermal origin-are the primary characteristics underlying the mutant phenotype. Pathological inflammatory responses have been excluded as a putative cause of the skin and hair disorder. The phenotype of CTSL-deficient mice is reminiscent of the spontaneous mouse mutant furless (fs). Analyses of the cfsl gene of fs mice revealed a G149R mutation inactivating the proteinase activity. CTSL is the first lysosomal proteinase shown to be essential for epidermal homeostasis id regular hair follicle morphogenesis and cycling."],["dc.identifier.doi","10.1096/fj.99-0970com"],["dc.identifier.isi","000089634400027"],["dc.identifier.pmid","11023992"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31448"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Federation Amer Soc Exp Biol"],["dc.relation.issn","0892-6638"],["dc.title","Cathepsin L deficiency as molecular defect of furless: hyperproliferation of keratinocytes and pertubation of hair follicle cycling"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]