neurilemmoma/protease

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Calpain-dependent proteolysis of NF2 protein: involvement in schwannomas and meningiomas.

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The neurofibromatosis type 2 (NF2) protein, known as merlin or schwannomin, is a tumor suppressor, and the NF2 gene has been found to be mutated in the majority of schwannomas and meningiomas, including both sporadically occurring and familial NF2 cases. Although the development of these tumors

The involvement of calpain-dependent proteolysis of the tumor suppressor NF2 (merlin) in schwannomas and meningiomas.

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Neurofibromatosis type 2 (NF2) protein, also known as merlin or schwannomin, is a tumor suppressor, and NF2 is mutated in most schwannomas and meningiomas. Although these tumors are dependent on NF2, some lack detectable NF2 mutations, which indicates that alternative mechanisms exist for

Immunohistochemical localization of lysosomal cathepsin D in schwannomas.

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The immunohistochemical localization of cathepsin D (CD) was demonstrated for the first time in 54 schwannomas (32 intra- and 22 extracranial; 47 benign and 7 malignant) and 5 normal nerve fibers. Granular or vesicular CD-reactive structures were observed in all normal Schwann cells. All tumors

Schwannoma cell-derived inhibitor of the neurite-promoting activity of laminin.

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During the purification of laminin-proteoglycan complexes from rat RN22 Schwannoma cell-conditioned medium, a laminin-rich fraction was obtained which lacked neurite-promoting activity. Since laminin from several sources is known to have potent neurite-promoting activity, this result suggested that

Neurite-promoting factor in conditioned medium from RN22 Schwannoma cultures: bioassay, fractionation, and properties.

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On polyornithine (PORN) substrata dissociated 8-day chick embryo ciliary ganglionic neurons will survive if the culture medium is supplemented with Ciliary neuronotrophic Factor. However, neuritic growth will not occur unless the substratum is derivatized with a PORN-bindable Neurite Promoting

Characterization of the protease activity that cleaves the extracellular domain of beta-dystroglycan.

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Dystroglycan (DG) complex, composed of alphaDG and betaDG, provides a link between the extracellular matrix (ECM) and cortical cytoskeleton. Although the proteolytic processing of betaDG was reported in various physiological and pathological conditions, its exact mechanism remains unknown. In this

Genesis and biology of vestibular schwannomas.

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This review chapter is a synthesis of the recent literature about pathogenesis of schwannomas with emphasis on vestibular schwannomas (VSs). The cornerstone of cellular transformation and proliferation of Schwann cells toward schwannomas has been attributed to the nonexpression of normal

MMP-14 (MT1-MMP) Is a Biomarker of Surgical Outcome and a Potential Mediator of Hearing Loss in Patients With Vestibular Schwannomas

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Improved biomarkers are needed for vestibular schwannoma (VS), the most common tumor of the cerebellopontine angle, as existing clinical biomarkers have poor predictive value. Factors such as tumor size or growth rate do not shed light on the pathophysiology of associated sensorineural hearing loss

Immunohistochemical demonstration of bikunin, a light chain of inter-alpha-trypsin inhibitor, in human brain tumors.

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The presence and localization of bikunin (HI-30, or acid-stable protease inhibitor), a light chain of inter-alpha-trypsin inhibitor, was examined in 30 brain tumors employing immunohistochemical methods. The brain tumors involved 13 kinds of histological diagnosis. Bikunin immunoreactivity was

Nuclear localization of catalytically active MMP-2 in endothelial cells and neurons.

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From microscopic organelles and sub-cellular domains to the level of whole tissues, organs, and body parts, living organisms must continuously maintain and renovate structural components. Matrix metalloproteinases (MMPs) comprise a family of over two dozen Zn-dependent endopeptidases thought to be

Stromelysin generates a fibronectin fragment that inhibits Schwann cell proliferation.

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Our previous report (Muir, D., S. Varon, and M. Manthorpe. 1990. J. Cell Biol. 109:2663-2672) described the isolation and partial characterization of a 55-kD antiproliferative protein found in Schwann cell (SC) and schwannoma cell line-conditioned media and we concluded that SC proliferation is

Construction of a mutated pro-nerve growth factor resistant to degradation and suitable for biophysical and cellular utilization.

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Precursor of nerve growth factor (proNGF) has been found to be proapoptotic in several cell types and mediates its effects by binding to p75 neurotrophin receptor (p75NTR) and sortilin. The proNGF molecule is processed by proteases at three dibasic sites found in the pro domain to form mature NGF

Thrombin and protein C pathway in peripheral nerve Schwann cells.

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Thrombin and activated protein C (aPC) bound to the endothelial protein C receptor (EPCR) both activate protease-activated receptor 1 (PAR1) generating either harmful or protective signaling respectively. In the present study we examined the localization of PAR-1 and EPCR and thrombin activity in

Tight association of loss of merlin expression with loss of heterozygosity at chromosome 22q in sporadic meningiomas.

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Mutations of NF2, the gene for neurofibromatosis 2, are detected in 20-30% of sporadic meningiomas, and almost all mutations lead to loss of merlin expression. However, loss of heterozygosity (LOH) at chromosome 22q is found at a much higher frequency, up to 50-70%, and the possibility of another

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