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Biosynthesis of protease nexin-I

Howard, E W ; Knauer, D J

The Journal of biological chemistry, 1986-10, Vol.261 (30), p.14184-14190 [Periódico revisado por pares]

Bethesda, MD: Elsevier Inc

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  • Título:
    Biosynthesis of protease nexin-I
  • Autor: Howard, E W ; Knauer, D J
  • Assuntos: Amyloid beta-Protein Precursor ; Analytical, structural and metabolic biochemistry ; Antibodies ; Biological and medical sciences ; Carrier Proteins - biosynthesis ; Cell Line ; Electrophoresis, Polyacrylamide Gel ; Enzymes and enzyme inhibitors ; Fibroblasts - enzymology ; Fundamental and applied biological sciences. Psychology ; Glycoside Hydrolases - metabolism ; Humans ; Hydrolases ; Mannose - metabolism ; Protease Nexins ; Receptors, Cell Surface
  • É parte de: The Journal of biological chemistry, 1986-10, Vol.261 (30), p.14184-14190
  • Notas: ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
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  • Descrição: Protease nexin-I (PN-I) is representative of a newly described class of serine protease inhibitors secreted by human fibroblasts, the protease nexins. Protease nexins form covalent complexes with their target proteases, subsequently binding to cells via specific receptors. PN-I preferentially binds thrombin, urokinase, trypsin, and plasmin, and its binding to thrombin is accelerated by heparin. We have previously described the production of a polyclonal antibody against PN-I which is able to block the binding of PN-I X proteinase complexes to cells and will immunoprecipitate metabolically labeled PN-I. Anti-PN-I was used to investigate the biosynthesis and regulation of PN-I in human fibroblasts. Unlabeled PN-I could compete for the binding of metabolically labeled PN-I to anti-PN-I, as shown by the elimination of the 43-kDa band representing PN-I on sodium dodecyl sulfate-polyacrylamide gel electrophoresis autoradiographs. Excision of this 43-kDa band from gels, followed by amino-terminal sequencing, showed a homogeneous protein that is homologous with that described by Scott et al. (Scott, R. W., Bergman, B. L., Bajpai, A., Hersh, R. T., Rodriguez, H., Jones, B. N., Barreda, C., Watts, S., and Baker, J. B. (1985) J. Biol. Chem. 260, 7029-7034). An analysis of the biosynthesis of the PN-I revealed that a lower Mr precursor exists intracellularly. This apparent rough endoplasmic reticulum form appears as a doublet on sodium dodecyl sulfate gels, as does mature PN-I. The PN-I precursor was also sensitive to endoglycosidase H, suggesting that it contains N-linked carbohydrates of the high mannose form. Mature PN-I is not sensitive to endoglycosidase H, but does contain 3 kDa of N-linked carbohydrate. PN-I appears to be constitutively secreted by fibroblasts. PN-I levels in conditioned media reach a steady state within 48 h, although PN-I synthesis maintains a constant rate. This steady state is due to the continuous uptake of PN-I from medium, presumably through a specific receptor.
  • Editor: Bethesda, MD: Elsevier Inc
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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