Nerve growth factor: a protease that can activate plasminogen.

Orenstein, Neil S.; Dvorak, Harold F.; Blanchard, Muriel H.; Young, Michael

doi:10.1073/pnas.75.11.5497

Cited by 50 publications

(34 citation statements)

References 21 publications

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“…(iv) Activated NGF has a highly restricted spectrum of proteolytic activity toward certain Na-substituted arginine and lysine esters (ref. 10; see also ref. 11).…”

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confidence: 99%

“…(v) NGF has also been found to hydrolyze certain naturally occurring substrates. For example, it can activate plasminogen with concomitant lysis of a fibrin clot by plasmin (10), and, within the classical pathway of complement activation, it can also specifically substitute for component Cl and only Cl (12).II Moreover, this Cl-like activity of mouse NGF may be inhibited by the Cl inactivator protein of human serum (12). (vi) Finally, topical application of NGF to superficial skin wounds in mice significantly accelerates the rate of wound contraction-and this activity depends on proteolytic activity of the growth factor (14).…”

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confidence: 99%

“…1 1 also reveals a maximum in leukocyte migration activity at a NGF concentration of 0.4 ,g/ml (3.4 nM), followed by a decrease in activity at higher concentrations. All NGF preparations used in this study were electrophoretically, ultracentrifugally, and chromatographically homogeneous (1,10,12). Nonetheless, to minimize further the possibility that a contaminant might be responsible for the results shown in Fig.…”

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confidence: 99%

“…NGF-zymogen was prepared from adult male mouse submandibular glands as described (1). All preparations were shown to be electrophoretically homogeneous by polyacrylamide gel staining and by radioimmunoassay procedures (1,10). Hanks' balanced salt solution was obtained from GIBCO.…”

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confidence: 99%

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Nerve growth factor: stimulation of polymorphonuclear leukocyte chemotaxis in vitro.

Gee¹,

Boyle²,

Munger³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

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Topical application of mouse nerve growth factor (NGF) to superficial skin wounds of mice has previously been shown to accelerate the rate of wound contraction. Results of the present study reveal that NGF in the presence of plasma is also chemotactic for human polymorphonuclear leukocytes in vitro, and the concentration of NGF required for this effect is similar to that which stimulates ganglionic neurite outgrowth. This property does not arise from liberation of the C5a fragment of complement, nor does it require the known enzymic activity of NGF. (NGF inactivated with diisopropyl fluorophosphate is equally active.) We conclude that NGF can display biological effects on cells of nonneural origin and function, and this feature might play a role in the early inflammatory response to injury.Present evidence indicates that the predominant form of male mouse submandibular gland nerve growth factor (NGF; purified and characterized as in ref . 1) MATERIALS AND METHODS Reagents. NGF-zymogen was prepared from adult male mouse submandibular glands as described (1). All preparations were shown to be electrophoretically homogeneous by polyacrylamide gel staining and by radioimmunoassay procedures (1, 10). Hanks' balanced salt solution was obtained from GIBCO. NGF concentrations were measured spectrophotometrically (7) and by radioimmunoassay (1,15). No-(p-Tosyl)-L-arginine methyl ester (TAME) and diisopropyl fluorophosphate (iPr2P-F) were obtained from Sigma, and [ H]iPr2P-F was from New England Nuclear.Heparinized freshly drawn human blood was used to prepare plasma and cells. CS-deficient human plasma was a gift from John Leddy (University of Rochester). Human polymorphonuclear leukocyte-enriched suspensions were prepared by differential sedimentation of blood with 5% (wt/vol) dextran. The cell pellet was washed twice with Hanks' solution (without Ca2" and Mg2+) and erythrocytes were lysed hypotonically. The leukocyte pellet was washed twice and suspended in Hanks' solution containing Ca2' and Mg2+. Microscopic examination revealed that these preparations contained >90% polymorphonuclear cells.Chemotaxis Measurements. Chemotactic assays used multiwell microchemotaxis chambers (Neuro Probe, Cabin John, MD) and a 5-I~m-pore-size polyvinylpyrollidone-free polycarbonate membrane (Nuclepore). Forty-five microliters of cell suspension (2.2 X 106 cells per ml) was placed in the top chamAbbreviations: NGF, male mouse submandibular gland nerve growth factor; TAME, NV-(p-tosyl)L-arginine methyl ester; iPr2P-F, diisopropyl fluorophosphate; DIP-NGF, NGF inactivated with iPr2P-F. ¶ To whom reprint requests should be addressed. IITerminology for the complement system is that recommended in ref.13. 7215The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.

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“…(iv) Activated NGF has a highly restricted spectrum of proteolytic activity toward certain Na-substituted arginine and lysine esters (ref. 10; see also ref. 11).…”

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Nerve growth factor: stimulation of polymorphonuclear leukocyte chemotaxis in vitro.

Gee¹,

Boyle²,

Munger³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

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“…various combinations of RNA and protein and show a most interesting differential pattern of cytolocation in oogenesis (20), development (35), and differentiation (21). As for the alleged identity of the HSPs and prosomal proteins (3,43) dealt with in this paper, the significance of the protease activity of prosomes, which recalls that of factors as various as mammalian growth factors (34) and the Gro E factor of Escherichia coli (8), for example, will need extensive and careful investigation (in progress).…”

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Prosomes and heat shock complexes in Drosophila melanogaster cells.

de¹,

Rollet²,

de³

et al. 1989

Mol. Cell. Biol.

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Prosomes and heat shock protein (HSP) complexes isolated from the cytoplasm of Drosophila cells in culture were biochemically and immunologically characterized. The two complexes were found to separate on sucrose gradients, allowing the analysis of their protein constituents by two-dimensional polyacrylamide gel electrophoresis and by reaction with anti-HSP sera and prosome-specific monoclonal antibodies. All of the prosomal proteins were found to be clearly distinct from the HSP; none of the prosomal proteins was synthesized de novo in heat shock. However, an antiprosome (anti-p27K) monoclonal antibody (mouse anti-duck) recognizing the Drosophila p29K prosomal protein allowed immunoprecipitation from a heat-shocked postmitochondrial supernatant of the crude HSP complex, including the low-and the high-molecular-weight components, in particular the 70 x 103-molecular weight HSP. The highly purified small 16S HSP complex still contained this preexistent p29K prosomal protein, which thus also seems to be a metabolically stable constituent of the HSP complex. The significance of this structural and possibly functional relationship between prosomes and HSP, involving the highly ubiquitous and evolutionarily conserved prosomal protein p27/29K, remains to be elucidated.The heat shock response of most eucaryotic cells involves a strong increase in the synthesis of a small set of evolutionarily conserved proteins known as the heat shock proteins (HSPs). A similar response is induced by a wide variety of other stress agents (for reviews, see references 6, 31, and 41). In eucaryotic cells, HSPs have also been shown to be induced by ethanol (29), by arsenite (53), in recovery from anoxia (38, 39), by cadmium (12), and by hydrogen peroxide (13). The predominant inducible HSPs can generally be classified into three major groups based on their molecular sizes of 80 to 90, 65 to 75, and 20 to 30 kilodaltons (kDa). The last group (referred to as the low-molecular-weight HSPs) is especially well characterized in Drosoplila cells.It has been postulated that these proteins play an important role during embryonic development (7), hormonal induction in Drosophilia melanogaster (23), and normal cell growth (56) and that HSPs have a protective effect (50). However, their precise cellular function remains obscure (41, 55; see also Discussion).The small HSPs were shown to exist as a complex in the cytoplasm, forming a characteristic band in density gradients including protein and RNA (2-4). Some of the HSPs were thought to be primarily associated with the nucleus during the heat shock (24). More recent data of Bonner and collaborators (27) indicate, however, that the HSPs are associated with the intermediate filaments of the cytoplasm and that upon heat shock, these cytoskeletal elements collapse onto the nuclear membrane. Therefore, it seems that the small HSPs exist essentially in the cytoplasm and not in the nucleus, as assumed previously on the basis of the fact that after heavy stress, they co-isolate with the nuclei. The most heter...

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Cathepsin D: The Lysosomal Aspartic Proteinase

Barrett¹

1980

Ciba Foundation Symposium 75 ‐ Protein Degradation in Health and Disease

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Nerve growth factor: a protease that can activate plasminogen.

Cited by 50 publications

References 21 publications

Nerve growth factor: stimulation of polymorphonuclear leukocyte chemotaxis in vitro.

Nerve growth factor: stimulation of polymorphonuclear leukocyte chemotaxis in vitro.

Prosomes and heat shock complexes in Drosophila melanogaster cells.

Cathepsin D: The Lysosomal Aspartic Proteinase

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