Cell-derived proteases and protease inhibitors as regulators of neurite outgrowth

Monard, Denis

doi:10.1016/0166-2236(88)90182-8

Cited by 324 publications

(190 citation statements)

References 26 publications

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“…Once activated, the domain of enzymatic activity can be further modulated by enzymatic inhibitors (see Hecht and Anderson 1992). The effects of the interplay of proteases (e.g., Gurwitz and Cunningham 1988;Dihanich et al 1991) and their inhibitors (Gloor et al 1986;Reinhard et al 1988) have been proposed to play an important role in growth cone motility and in neurite outgrowth (Monard 1988;Suidan et al 1992;Sumi et al 1992). Mutations in the Drosophila Stubble-stubbloid (Sb-sbd) gene, which encodes an apparent transmembrane protein with an extracellular serine protease domain, cause defects in cell shape and changes in the organization of microfilament bundles required for normal imaginal disc and bristle morphogenesis (Appel et al 1993).…”

Section: I(1)myospheroid (Rays)mentioning

confidence: 99%

Masquerade: a novel secreted serine protease-like molecule is required for somatic muscle attachment in the Drosophila embryo.

Murugasu-Oei¹,

Rodrigues²,

Yang³

et al. 1995

Genes Dev.

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Diverse developmental processes, such as neuronal growth cone migration and cell shape changes, are mediated by the interactions of cells with the extracellular matrix. We describe here a secreted molecule encoded by the Drosophila masquerade (mas) gene. Total loss of mas function causes defective muscle attachment. This mutant phenotype suggests that mas normally acts to stabilize cell-matrix interaction and represents a novel functional and limiting component in the adhesion process, mas encodes a 1047-amino-acid preproprotein that is further processed by proteolytic cleavage to generate two polypeptides. The carboxy-terminal polypeptide is highly similar to serine proteases and has an extracellular localization; however, it is unlikely to possess proteolytic activity, because the catalytic site serine has been substituted by a glycine residue. During embryonic development, the mas amino-and carboxy-terminal polypeptides are differentially localized. The mas carboxy-terminal polypeptide accumulates at all somatic muscle attachment sites, which corresponds well with the morphological defect seen in the mas mutants. Our findings demonstrate the involvement of an extracellular component in somatic muscle attachment. We propose that mas acts via its modified serine protease motif, either as a novel adhesion molecule and/or as a competitive antagonist of serine proteases, to stabilize muscle attachment.

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Section: I(1)myospheroid (Rays)mentioning

confidence: 99%

Masquerade: a novel secreted serine protease-like molecule is required for somatic muscle attachment in the Drosophila embryo.

Murugasu-Oei¹,

Rodrigues²,

Yang³

et al. 1995

Genes Dev.

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“…For example, plasminogen activators have been shown to be produced and secreted by neurons and glia and to participate in remodeling events that occur during cell migration (Moonen et al, 1982), neurite outgrowth (Monard, 1988;Pittman and Williams, 1989;Sumi et al, 1992;Sappino et al, 1993), and synaptic plasticity (Monard, 1988;Qian et al, 1993;Sappino et al, 1993). MSP Table 1.…”

Section: Region and Cell-specific Expression Of Msp In The Cnsmentioning

confidence: 99%

“…The activity of serine proteases and their inhibitors has been established to play important roles in the nervous system, including the regulation of neuronal migration during development (Moonen et al, 1982;Seeds et al, 1990), neurite outgrowth (Monard, 1988), synaptic plasticity (Liu et al, 1994a,b), and neuronal degeneration and death (Houenou et al, 1995;Tsirka et al, 1995Tsirka et al, , 1997. These actions may be mediated by the proteolytic cleavage of zymogen precursors and propeptides, the activation of specific cell surface receptors, and /or by the degradation of extracellular matrix proteins (Monard, 1988;Pittman and Williams, 1989;McGuire and Seeds, 1990).…”

mentioning

confidence: 99%

“…Among factors likely to participate in the response of the nervous system to injury, including tissue degeneration, are changes in the constitution of a variety of extracellular matrix components (Sanes, 1983(Sanes, , 1989, growth factors (Barde et al, 1983), and cell proteolytic cascades (Krystosek and Seeds, 1981;Monard, 1988;Seeds et al, 1990). The activity of serine proteases and their inhibitors has been established to play important roles in the nervous system, including the regulation of neuronal migration during development (Moonen et al, 1982;Seeds et al, 1990), neurite outgrowth (Monard, 1988), synaptic plasticity (Liu et al, 1994a,b), and neuronal degeneration and death (Houenou et al, 1995;Tsirka et al, 1995Tsirka et al, , 1997.…”

mentioning

confidence: 99%

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Nervous System-Specific Expression of a Novel Serine Protease: Regulation in the Adult Rat Spinal Cord by Excitotoxic Injury

1997

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A full-length cDNA clone of a previously unidentified serine protease, myelencephalon-specific protease (MSP), has been isolated by using a PCR cloning strategy and has been shown to be expressed in a nervous system and spinal cord-specific pattern. Sequence analysis demonstrated that MSP is most similar in sequence to neuropsin, trypsin, and tissue kallikrein and is predicted to have trypsin-like substrate specificity. MSP mRNA was found to be ϳ10-fold greater in the CNS of the rat and human, as compared with most peripheral tissues, and within the CNS was found to be highest by a factor of four in the medulla oblongata and spinal cord. Levels of mRNA encoding tissue plasminogen activator (tPA) also were elevated in the spinal cord but were more widespread in peripheral tissues as compared with MSP.In the adult rat lumbosacral spinal cord, in situ localization of MSP mRNA demonstrated 2-fold higher levels in the white, as compared with the gray, matter. MSP mRNA expression was shown to increase 3-fold in the white matter and 1.5-fold in the gray laminae at 72 hr after intraperitoneal injection of the AMPA/ kainate glutamate receptor-specific agonist, kainic acid (KA). MSP mRNA remained elevated in the ventral gray matter, including expression associated with the motor neurons of lamina IX, at 7 d after the initial excitotoxic insult. Together, these observations indicate that MSP is in a position to play a fundamental role in normal homeostasis and in the response of the spinal cord to injury.

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“…This secondary phase of injury includes ischemia, inflammation and glutamate excitotoxicity, together with neuronal and glial cell death. These processes are mediated by changes in the constitution of a variety of extracellular matrix components (Sanes, 1983(Sanes, , 1989, growth factors (Mocchetti and Wrathall, 1995), and proteolytic cascades (Krystosek and Seeds, 1981;Monard, 1988;Seeds et al, 1990). Several groups have now demonstrated that oligodendrocyte death and subsequent demyelination are involved in the pathology after SCI (Lu et al, 2000;Blight, 2002;Dong et al, 2003;Park et al, 2004).…”

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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Cell-derived proteases and protease inhibitors as regulators of neurite outgrowth

Cited by 324 publications

References 26 publications

Masquerade: a novel secreted serine protease-like molecule is required for somatic muscle attachment in the Drosophila embryo.

Masquerade: a novel secreted serine protease-like molecule is required for somatic muscle attachment in the Drosophila embryo.

Nervous System-Specific Expression of a Novel Serine Protease: Regulation in the Adult Rat Spinal Cord by Excitotoxic Injury

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

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