α-macroglobulin-like plasma inactivator for Vibrio vulnificus metalloprotease

Shin-ichi Miyoshi, Sumio Shinoda

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

The metalloprotease produced by Vibrio vulnificus (VVP) is known to be quickly inactivated by plasma proteins which belong to the class of α-macroglobulins in vitro at a molar ratio of 1 : 1. But the in vivo potential of the inactivators has not been studied. Macroal-bumin (MA), a member of α-macroglobulins in Guinea pig plasma, was found to inactivate WP by means of physical entrapment in vitro. In vivo actions of VVP, permeability-enhancing and hemorrhagic actions, were greatly augmented by simultaneous injection of the antibody against MA, which had no effect on in vitro proteolytic action toward azocasein. The interstitial-tissue space in the normal Guinea pig skin contains a negligible amount of MA. However, sufficient MA was present in the extravascular fluid collected after the intradermal injection of VVP. Besides, in the extravascular fluid, VVP formed a complex with MA and no inactivator other than MA was found. These results indicate that plasma MA leaked from the vascular system owing to the permeability-enhancing and hemorrhagic actions of VVP, resulting in inactivation of VVP in situ.

Original languageEnglish
Pages (from-to)548-552
Number of pages5
JournalJournal of Biochemistry
Volume110
Issue number4
Publication statusPublished - Oct 1991

Fingerprint

Vibrio vulnificus
Macroglobulins
Metalloproteases
Plasma
Plasmas
Guinea pig
Fluids
Permeability
Guinea Pigs
Blood Proteins
Intradermal Injections
Injection
Skin
Tissue
Antibodies
Fluid
Blood Vessels
Antibody
Proteins
Injections

ASJC Scopus subject areas

  • Statistics, Probability and Uncertainty
  • Applied Mathematics
  • Physiology (medical)
  • Radiology Nuclear Medicine and imaging
  • Molecular Biology
  • Biochemistry

Cite this

α-macroglobulin-like plasma inactivator for Vibrio vulnificus metalloprotease. / Miyoshi, Shin-ichi; Shinoda, Sumio.

In: Journal of Biochemistry, Vol. 110, No. 4, 10.1991, p. 548-552.

Research output: Contribution to journalArticle

@article{151528aedc944ac7a054ebae13584016,
title = "α-macroglobulin-like plasma inactivator for Vibrio vulnificus metalloprotease",
abstract = "The metalloprotease produced by Vibrio vulnificus (VVP) is known to be quickly inactivated by plasma proteins which belong to the class of α-macroglobulins in vitro at a molar ratio of 1 : 1. But the in vivo potential of the inactivators has not been studied. Macroal-bumin (MA), a member of α-macroglobulins in Guinea pig plasma, was found to inactivate WP by means of physical entrapment in vitro. In vivo actions of VVP, permeability-enhancing and hemorrhagic actions, were greatly augmented by simultaneous injection of the antibody against MA, which had no effect on in vitro proteolytic action toward azocasein. The interstitial-tissue space in the normal Guinea pig skin contains a negligible amount of MA. However, sufficient MA was present in the extravascular fluid collected after the intradermal injection of VVP. Besides, in the extravascular fluid, VVP formed a complex with MA and no inactivator other than MA was found. These results indicate that plasma MA leaked from the vascular system owing to the permeability-enhancing and hemorrhagic actions of VVP, resulting in inactivation of VVP in situ.",
author = "Shin-ichi Miyoshi and Sumio Shinoda",
year = "1991",
month = "10",
language = "English",
volume = "110",
pages = "548--552",
journal = "Journal of Biochemistry",
issn = "0021-924X",
publisher = "Oxford University Press",
number = "4",

}

TY - JOUR

T1 - α-macroglobulin-like plasma inactivator for Vibrio vulnificus metalloprotease

AU - Miyoshi, Shin-ichi

AU - Shinoda, Sumio

PY - 1991/10

Y1 - 1991/10

N2 - The metalloprotease produced by Vibrio vulnificus (VVP) is known to be quickly inactivated by plasma proteins which belong to the class of α-macroglobulins in vitro at a molar ratio of 1 : 1. But the in vivo potential of the inactivators has not been studied. Macroal-bumin (MA), a member of α-macroglobulins in Guinea pig plasma, was found to inactivate WP by means of physical entrapment in vitro. In vivo actions of VVP, permeability-enhancing and hemorrhagic actions, were greatly augmented by simultaneous injection of the antibody against MA, which had no effect on in vitro proteolytic action toward azocasein. The interstitial-tissue space in the normal Guinea pig skin contains a negligible amount of MA. However, sufficient MA was present in the extravascular fluid collected after the intradermal injection of VVP. Besides, in the extravascular fluid, VVP formed a complex with MA and no inactivator other than MA was found. These results indicate that plasma MA leaked from the vascular system owing to the permeability-enhancing and hemorrhagic actions of VVP, resulting in inactivation of VVP in situ.

AB - The metalloprotease produced by Vibrio vulnificus (VVP) is known to be quickly inactivated by plasma proteins which belong to the class of α-macroglobulins in vitro at a molar ratio of 1 : 1. But the in vivo potential of the inactivators has not been studied. Macroal-bumin (MA), a member of α-macroglobulins in Guinea pig plasma, was found to inactivate WP by means of physical entrapment in vitro. In vivo actions of VVP, permeability-enhancing and hemorrhagic actions, were greatly augmented by simultaneous injection of the antibody against MA, which had no effect on in vitro proteolytic action toward azocasein. The interstitial-tissue space in the normal Guinea pig skin contains a negligible amount of MA. However, sufficient MA was present in the extravascular fluid collected after the intradermal injection of VVP. Besides, in the extravascular fluid, VVP formed a complex with MA and no inactivator other than MA was found. These results indicate that plasma MA leaked from the vascular system owing to the permeability-enhancing and hemorrhagic actions of VVP, resulting in inactivation of VVP in situ.

UR - http://www.scopus.com/inward/record.url?scp=0026062621&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026062621&partnerID=8YFLogxK

M3 - Article

C2 - 1723411

AN - SCOPUS:0026062621

VL - 110

SP - 548

EP - 552

JO - Journal of Biochemistry

JF - Journal of Biochemistry

SN - 0021-924X

IS - 4

ER -