Cleavage of Myelin Basic Protein by Neutral Protease Activity of Human White Matter and Myelin

Berlet, Hans H.; Ilzenhöfer, Heike; Schulz, Günther

doi:10.1111/j.1471-4159.1984.tb12781.x

Cited by 24 publications

(17 citation statements)

References 32 publications

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“…When CNS myelin is partially or completely ablated, damaged axons in the vicinity are capable of extensive neurite outgrowth (Dyer et al, 1998;Keirstead et al, 1995Keirstead et al, , 1998Keirstead et al, , 1999. Several lines of evidence suggest that myelin has endogenous protease activity with the potential to degrade myelin proteins (Berlet et al, 1984;Chantry et al, 1989;Sato et al, 1982). An in vitro biochemical assay showed that neuropsin degraded myelin basic protein (He et al, 2001).…”

Section: Discussionmentioning

confidence: 96%

“…Within unlesioned spinal cord white matter, a subpopulation of mature oligodendrocytes and oligodendrocyte progenitors expressed protease M/neurosin. These cells may function in normal homeostasis such as turnover of the myelin sheath (Berlet et al, 1984). After injury to the spinal cord, some of the protease M/neurosin-expressing cells also expressed neuropsin and most of the cells expressing neuropsin were CNPase-positive oligodendrocytes.…”

Section: Discussionmentioning

confidence: 97%

“…Less attention has been paid to oligodendroglial serine proteases (Tomizawa et al, 1999). Oligodendrocytes extend their processes to myelinate axons in the CNS and display protease activity, which might contribute to the turnover of the myelin sheath (Berlet et al, 1984). Neuropsin is a kalliklein-like serine protease whose mRNA is constitutively expressed specifically in the neurons of the limbic system of the adult mouse brain (Chen et al, 1995;Shiosaka and Yoshida, 2000;Yoshida and Shiosaka, 1999).…”

Section: Introductionmentioning

confidence: 99%

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Differential expression of neuropsin and protease M/neurosin in oligodendrocytes after injury to the spinal cord

Terayama

Bandô

Takahashi

et al. 2004

Glia

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Neuropsin and protease M/neurosin are serine proteases expressed by neurons and glial cells, and serve a variety of functions in the central nervous system (CNS). The current study demonstrates changes in the expression of these proteases following hemisection of the mouse spinal cord. Within unlesioned spinal cord, neuropsin mRNA expression was occasionally observed in the gray but not white matter, while the level of protease M/neurosin mRNA was higher in the white matter. After injury to the spinal cord, neuropsin mRNA expression was induced in the white matter in the area immediately adjacent to the lesion, peaking at 4 days post-injury and disappearing by 14 days. Enhanced expression of protease M/neurosin mRNA was observed throughout the white and gray matter surrounding the lesion, peaking at 4 days and persisting for 14 days. Neuropsin mRNA was expressed predominantly by CNPase-positive oligodendrocytes. Furthermore, most of these cells were also associated with immunoreactivity for protease M/neurosin protein. Within unlesioned spinal cord, most protease M/neurosin mRNA-expressing cells were CNPase-positive oligodendrocytes, and a substantial fraction of these cells also showed immunoreactivity for NG2, a marker for oligodendrocyte progenitors. After injury, protease M/neurosin mRNA expression within NG2-positive cells was significantly decreased, while the constitutive expression in CNPase-positive oligodendrocytes appeared to be preserved. These findings suggest that each subpopulation of oligodendrocytes based on the expression of neuropsin and protease M/neurosin has different roles in the response of the spinal cord to injury as well as in normal homeostasis.

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

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Differential expression of neuropsin and protease M/neurosin in oligodendrocytes after injury to the spinal cord

Terayama

Bandô

Takahashi

et al. 2004

Glia

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“…It has been suggested that oligodendrocytes and myelin have endogenous protease activity with the potential to degrade myelin proteins (Sato et al, 1982;Berlet et al, 1984;Chantry et al, 1989;Scarisbrick et al, 2002;Terayama et al, 2005b). The in vitro biochemical assay showed that neuropsin is capable of degrading MBP (He et al, 2001).…”

Section: Discussionmentioning

confidence: 99%

“…Since oligodendrocytes have protease activity which might contribute to the pathology after SCI (Berlet et al, 1984), the identification and characterization of key enzymatic players may suggest new therapeutic targets to reduce further damage and promote remyelination. Kallikreins are serine proteases that comprise a recently -6 -identified large and closely related 15-member family in humans.…”

Section: Introductionmentioning

confidence: 99%

Neuropsin promotes oligodendrocyte death, demyelination and axonal degeneration after spinal cord injury

et al. 2007

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Abbreviations: SCI, spinal cord injury; DIG, digoxigenin; APC, adenomatus polyposis coli; MBP, myelin basic protein; TUNEL, TdT-mediated dUTP-fluorescein nick end labeling -3 - AbstractPrevious studies indicated that the expression of neuropsin, a serine protease, is induced in mature oligodendrocytes after injury to the central nervous system (CNS). The pathophysiology of spinal cord injury (SCI) involves primary and secondary mechanisms, the latter contributing further to permanent losses of function. To explore the role of neuropsin after SCI, histochemical and behavioral analyses were performed in wild-type (WT) and neuropsin-deficient (neuropsin -/-) mice using a crush injury model, a well-characterized and consistently reproducible model of SCI. In situ hybridization revealed that neuropsin mRNA expression was induced in the spinal cord white matter from WT mice after crush SCI, peaking at day 4. Neuropsin -/-mice showed attenuated demyelination, oligodendrocyte death, and axonal damage after SCI.Although axonal degeneration in the corticospinal tract was obvious caudal to the lesion site in both strains of mice after SCI, the number of surviving nerve fibers caudal to the lesion was significantly larger in neuropsin -/-mice than WT mice. Behavioral analysis revealed that the recovery at days 10-42 was significantly improved in neuropsin -/-mice compared to WT mice in spite of the severe initial hindlimb impairments due to SCI in both strains. These observations suggest that neuropsin is involved in the secondary phase of the pathogenesis of SCI mediated by demyelination, oligodendrocyte death, and axonal degeneration.-4 -

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2006

Dial. Transplant.

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We have analyzed surfactant protein B (SP‐B) and its encoding gene (SFTPB, MIM 178640) in 40 unrelated pediatric patients with unexplained respiratory distress (URD). There was high consanguinity (eight kindreds) and an underlying autosomal recessive trait could be inferred in most cases, with overall high sex ratio (32/17) suggesting proband's gender to impact on penetrance. The clinical/biological presentations fitted into three major nosologic frameworks. I: SP‐B deficiency (nine probands), complete or incomplete, with homozygous/compoundly heterozygous mutations identified (six probands), including one from the population isolate of Réunion Island (496delG). In addition, there was a consanguineous kindred in which incomplete deficiency was unambiguously unlinked to SFTPB. II: pulmonary alveolar proteinosis (PAP, 19 probands), with typical storage of PAS‐positive material within the alveoli with foamy macrophages and variable interstitial reaction, which was diagnosed in most patients from Réunion Island. In contrast to previously published findings, mutation and/or segregation analyses excluded SFTPB as a disease locus, although slight metabolic derangement related to SP‐B and/or mild SFTPB changes could somehow contribute to disease. III: URD without evidence for SP‐B deficiency or PAP (12 probands), equally unlinked to SFTPB, although a single patient had a possibly causal, maternally‐derived, heterozygous genetic change (G4521A). The population frequency of five known and four novel SNPs was studied, providing as many potential markers for pulmonary disease related to SFTPB. Overall, URD was found to be heterogeneous, both phenotypically and genetically, even in population isolates where a founder effect might have been expected. When disease loci are identified, patient genotyping will be crucial as a diagnostic aid, for devising proper treatment, and as a basis for genetic counseling. © 2003 Wiley‐Liss, Inc.

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Cleavage of Myelin Basic Protein by Neutral Protease Activity of Human White Matter and Myelin

Cited by 24 publications

References 32 publications

Differential expression of neuropsin and protease M/neurosin in oligodendrocytes after injury to the spinal cord

Differential expression of neuropsin and protease M/neurosin in oligodendrocytes after injury to the spinal cord

Neuropsin promotes oligodendrocyte death, demyelination and axonal degeneration after spinal cord injury

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