Literature DB >> 13712446

Biochemical study of cellular antigen-antibody reaction in tissue culture. I. Activation and release of a protease.

H HAYASHI, A TOKUDA, K UDAKA.   

Abstract

The correlation between morphological and biochemical changes produced by the antigen-antibody reaction was studied in cultures of tissue monocytes taken from sensitized animals. The cells were grown under conditions which allowed collection of samples from the culture fluid as well as microscopic observation. Introduction of the antigen into the culture medium causes rapid release of a protease characterized by its susceptibility to sulfhydryl block and its optimum pH in the neutral range. Protease activation occurs simultaneously with morphological changes in the cytoplasm of the cultured cells. Delayed changes affecting the mitochondria and Golgi bodies appear after the peak of the proteolytic reaction and may be secondary to it. The gradual inactivation of the protease observed in the course of the antigen-antibody reaction will be discussed in a separate paper.

Entities:  

Keywords:  ANTIEMETICS/therapy; PROTEASES/metabolism; TISSUE CULTURE/metabolism

Mesh:

Substances:

Year:  1960        PMID: 13712446      PMCID: PMC2137228          DOI: 10.1084/jem.112.2.237

Source DB:  PubMed          Journal:  J Exp Med        ISSN: 0022-1007            Impact factor:   14.307


  12 in total

1.  Enzymatic mechanisms in allergy.

Authors:  G UNGAR; H HAYASHI
Journal:  Ann Allergy       Date:  1958 Sep-Oct

2.  Specificity of cathepsin C.

Authors:  N IZUMIYA; J S FRUTON
Journal:  J Biol Chem       Date:  1956-01       Impact factor: 5.157

3.  The action of anti-Ehrlich ascites tumor antibody.

Authors:  M H FLAX
Journal:  Cancer Res       Date:  1956-09       Impact factor: 12.701

4.  Studies on beef spleen cathepsin C.

Authors:  J S FRUTON; M J MYCEK
Journal:  Arch Biochem Biophys       Date:  1956-11       Impact factor: 4.013

5.  Proteolytic activity in organ extracts after anaphylactic shock; with special regard to the action of thiols.

Authors:  G HERBERTS
Journal:  Acta Soc Med Ups       Date:  1955-12-31

6.  Effect of antigen and organic bases on intracellular histamine in guinea-pig lung.

Authors:  J L MONGAR; H O SCHILD
Journal:  J Physiol       Date:  1956-01-27       Impact factor: 5.182

7.  Action of fibrinolysin (plasmin) on proteins.

Authors:  E H KAPLAN
Journal:  Proc Soc Exp Biol Med       Date:  1954-01

8.  The presence of antibody in macrophage extracts.

Authors:  K F GIRARD; E G MURRAY
Journal:  Can J Biochem Physiol       Date:  1954-01

9.  Studies on a proteolytic enzyme system of the blood. I. Inhibition of fibrinolysin.

Authors:  J H LEWIS; J H FERGUSON
Journal:  J Clin Invest       Date:  1950-04       Impact factor: 14.808

10.  Proteolytic enzymes; further studies on protein, polypeptide, and other inhibitors of serum proteinase, leucoproteinase, trypsin, and papain.

Authors:  D GROB
Journal:  J Gen Physiol       Date:  1949-11       Impact factor: 4.086

View more
  14 in total

1.  ENDOGENEOUS PERMEABILITY FACTORS AND THEIR INHIBITORS AFFECTING VASCULAR PERMEABILITY IN CUTANEOUS ARTHUS REACTIONS AND THERMAL INJURY.

Authors:  H HAYASHI; M YOSHINAGA; M KOONO; H MIYOSHI; M MATSUMURA
Journal:  Br J Exp Pathol       Date:  1964-08

Review 2.  [ACTH AND CORTICOID TREATMENT OF NEUROLOGIC DISEASES].

Authors:  H BAMMER
Journal:  Dtsch Z Nervenheilkd       Date:  1963-07-10

3.  THE ROLE OF SH AND S-S GROUPS AND OXYGEN IN THE ANAPHYLACTIC REACTION OF CHOPPED GUINEA-PIG LUNG.

Authors:  K A EDMAN; J L MONGAR; H O SCHILD
Journal:  J Physiol       Date:  1964-01       Impact factor: 5.182

Review 4.  [ENZYMATIC PROCESSES IN THE PATHOGENESIS OF ALLERGIC REACTIONS].

Authors:  W RAAB; E KAISER
Journal:  Klin Wochenschr       Date:  1965-04-01

5.  Biochemical and morphological studies of radiation injury in tissue culture: a comparison with cellular injury in antigen-antibody reactions.

Authors:  H HAYASHI; A TOKUDA; T ONO; Y TAKABA
Journal:  Br J Exp Pathol       Date:  1963-02

6.  Higher susceptibility to thiol compounds of a protease in healing sites of Arthus-type inflammation and its biological significance.

Authors:  H HAYASHI; K UDAKA; M KOONO; M YOSHIMURA
Journal:  Br J Exp Pathol       Date:  1962-12

7.  Proteolytic mechanism in recurrence of Arthus-type inflammation by thiol compounds.

Authors:  H MAYASHI; H MIYOSHI; R NITTA; K UDAKA
Journal:  Br J Exp Pathol       Date:  1962-10

8.  The natural mediator for PMN emigration in inflammation. 3. In vitro production of a chemotactic factor by inflammatory SH-dependent protease from serum immunoglobulin G.

Authors:  M Yoshinaga; S Yamamoto; S Maeda; H Hayashi
Journal:  Immunology       Date:  1971-05       Impact factor: 7.397

9.  The natural mediator for PMN emigration in inflammation. I. Purification and characterization of leucoegresin from Arthus skin site.

Authors:  M Yoshinaga; K Yoshida; A Tashiro; H Hayashi
Journal:  Immunology       Date:  1971-08       Impact factor: 7.397

10.  Influence of proteolysis inhibitors on the formation of the anaemization factor released following interaction of hypersensitive lymph node cells with antigen in vitro.

Authors:  J Pekárek; J Svejcar; J Krejci; J Johanovský
Journal:  Folia Microbiol (Praha)       Date:  1969       Impact factor: 2.099

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