Journal of Immunological Methods, 119 (1989) 65-73 65
Elsevier
JIM05135
Local tissue injury induced by glucose oxidase conjugated
with anti-collagen antibody
Vladimir R. Muzykantov, Mikhail M. Peclo and Olga Yu. Printseva
Institute of Experimental Cardiology of the U.S.S.R. CardiologyResearch Center (IEC UCRC),
Academy of Medical Sciences, Moscow, U.S.S.R.
(Received17 May 1988,revisedreceived 3 October1988, accepted28 November1988)
The conjugation of glucose oxidase with anti-collagen antibody using periodate oxidation of the enzyme
carbohydrate moiety is described. After conjugation, the antibody retained its antigen-binding capacity
and the enzyme retained hydrogen peroxide-generating activity. Intradermal administration of the immune
conjugate into rats induced local tissue injury at doses 10-100/~g. Pronounced damage (local hyperemia
and edema) occurred 24 h after injection and necrosis developed 1 week later. The enzyme was tightly
bound to the fibrillar components of the extracellular matrix and retained its activity in vivo for a
prolonged period of time. In contrast, non-immune IgG-conjugated glucose oxidase was removed rapidly
from the site of injection and did not induce tissue damage. Pure native anti-collagen antibody was
retained at the site of injection for 8 days, but caused no tissue injury. These results suggest that active
glucose oxidase conjugated with antibodies to tissue antigen can be accumulated and retained in the
tissues. At the site of accumulation local 'proinflammatory' damage develops even in the absence of the
halide-peroxidase system. Similar conjugates could be potential agents for local modulation of inflamma-
tion.
Key words: Hydrogen peroxide; Drug targeting;Inflammation; Tissuedamage; Immunotoxin
Introduction
Hydrogen peroxide released by activated
phagocytes produces a direct cytotoxic effect
(Nathan et al., 1979; Badwey and Karnovsky,
1980), degrades extracellular matrix (Weiss et al.,
Correspondence to: V.R. Muzykantov, U.S.S.R. Cardiology
Research Center, 3rd Cherepkovskaya Str. 15A, Moscow
121552, U.S.S.R.
Abbreviations: PBS,phosphate-buffered saline;BSA, bovine
serum albumin; GARGG, goat antibody against rabbit im-
munoglobulins; HRPO, horseradish peroxidase; DAB, di-
aminobenzidine; HAP, hydroxylapatite; PEG, polyethylene
glycol; BAM,biologicalactivitymodifier; SMCC, succinimi-
dyl-4-( N-maleimidomethyl)cyclohexane-l-carboxylate; SPDP,
succinimidyl-3-(pyridyl-dithio)propionate.
1985, 1986), modulates plasma proteases and in-
duces chemoattractant activity (Shingu and
Nobunaga, 1984). In vivo and in vitro studies have
demonstrated both protective 'anti-inflammatory'
properties of the HEOE-destroying enzyme catalase
(Nathan et al., 1979; Fliegel et al., 1984) and
damaging 'proinflammatory' properties of the
H2OE-generating enzymes glucose oxidase and
xanthine oxidase (Johnson et al., 1981). It has
been suggested that catalase and its PEG or lipo-
somal derivatives protect host cells at inflamma-
tory or ischemic sites against injury induced by
hydrogen peroxide (Fliegel et al., 1984; Freeman
et al., 1985). To achieve a prolonged local effect
the targeting of protective substances has been
proposed (Muzykantov et al., 1987; Sakharov et
al., 1987). It is obvious, however, that in certain
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