A glia-derived neurite promoting factor with protease inhibitory activity belongs to the protease nexins

Gioor, Sergio; Odink, Karel; Guenther, Joachim; Nick, Hanspeter; Monard, Denis

doi:10.1016/0092-8674(86)90511-8

Cited by 294 publications

(147 citation statements)

References 23 publications

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“…In separate studies, a rat glioma-derived 43 kDa protein, which had been identified on the basis of its activity in promoting neurite outgrowth in mouse neuroblastoma cells, was shown to be the rat equivalent of human PN-I (Gloor et al, 1986;Sommer et al, 1987). More recently, PN-I has been identified in human platelets, smooth and striated muscle, rat brain astrocytes, regenerating rat peripheral nerve and rat olfactory system (Rosenblatt et al, 1987;Reinhard et al, 1988;Gronke et al, 1989;Meier et al, 1989;Festoff et al, 1990); in the latter two cases, PN-I probably originates primarily from the non-neuronal component of the tissues.…”

Section: Resultsmentioning

confidence: 99%

“…Using radiolabelled uPA, we have detected high levels of a uPA ligand in extracts of adult mouse and rat seminal vesicles. We have identified this ligand as protease nexin I (PN-I), a serpin released by human fibroblasts (Baker et al, 1980) and identical to glia-derived nexin (GDN) (Gloor et al, 1986;Sommer et al, 1987;McGrogan et al, 1988), first detected as a factor promoting neurite outgrowth in vitro (Guenther et al, 1985) that is found in different structures of the nervous system (Reinhard et al, 1988;Meier et al, 1989). PN-I reacts with and inhibits thrombin, uPA, tissuetype PA (tPA), trypsin and plasmin (Baker et al, 1980;Eaton and Baker, 1983;Guenther et al, 1985;Stone et al, 1987).…”

Section: Introductionmentioning

confidence: 99%

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Protease-nexin I as an androgen-dependent secretory product of the murine seminal vesicle.

et al. 1993

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A search for inhibitors of urokinase-type plasminogen activator (uPA) in the male and female murine genital tracts revealed high levels of a uPA ligand in the seminal vesicle. This ligand is functionally, biochemically and immunologically indistinguishable from protease-nexin I (PN-I), a serpin ligand of thrombin and uPA previously detected only in mesenchymal cells and astrocytes. A survey of murine tissues indicates that PN-I mRNA is most abundant in seminal vesicles, where it represents 0.2-0.4% of the mRNAs. PN-I is synthesized in the epithelium of the seminal vesicle, as determined by in situ hybridization, and is secreted in the lumen of the gland. PN-I levels are much lower in immature animals, and strongly decreased upon castration. Testosterone treatment of castrated males rapidly restores PN-I mRNA levels, indicating that PN-I gene expression is under androgen control.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Protease-nexin I as an androgen-dependent secretory product of the murine seminal vesicle.

et al. 1993

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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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“…It can degrade basement membrane components (Liotta et al, 1981) and can activate type IV procollagenase (Paranjpe et al, 1980;O'Grady et al, 1981). uPA can by itself degrade fibronectin (Gold et al, 1989). Inhibition of uPA using anti-urokinase antibodies has shown the importance of uPA in tumour invasion (Ossowski & Reich, 1983).…”

mentioning

confidence: 99%

Relationship between cathepsin D, urokinase, and plasminogen activator inhibitors in malignant vs benign breast tumours

Foucre

Bouchet²,

Hacène³

et al. 1991

Br J Cancer

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Summary The concentrations of cathepsin D (Cath D), urokinase (uPA) and two plasminogen activator inhibitors (PAI-I and PAI-2) were analysed in the cytosols of 130 human mammary tumours (43 benign tumours and 87 primary and unilateral breast carcinomas). uPA, PAI-i and PAI-2 levels were measured by antigenic immunoassays and Cath D by immunoradiometric assay. The median levels of the four parameters were significantly higher in the malignant tumours than in the benign ones. Cath D and uPA increases were 4-fold and 5-fold respectively. PAI-I and PAI-2 increases were much more important, 74-fold and 29-fold respectively. In malignant tumours, median levels of Cath D and uPA did not vary according to classical prognostic factors (histologic grade, presence or absence of axillary lymph nodes, steroid receptors, UICC stage, tumour size, age, and menopausal status). However, PAI-I decreased in ER+ and PR+ tumours and PAI-2 increased in menopausal women's tumours. When Cath D, uPA, PAI-I and PAI-2 levels in malignant tumours were compared, positive correlations were found for all combinations. The implication of plasminogen activator inhibitors in the phenomenon was surprising and merits further investigation using tools other than global antigen measurements in tumours.

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A glia-derived neurite promoting factor with protease inhibitory activity belongs to the protease nexins

Cited by 294 publications

References 23 publications

Protease-nexin I as an androgen-dependent secretory product of the murine seminal vesicle.

Protease-nexin I as an androgen-dependent secretory product of the murine seminal vesicle.

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

Relationship between cathepsin D, urokinase, and plasminogen activator inhibitors in malignant vs benign breast tumours

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