486
C.H.J. Lamers
Lamers
&
De
Haas
(1985)
showed
that
the
bacterial
antigen
Aeromonas
hydrophila, after initial rapid phag0cytosis by ellipsoids, became located
in
MMCs
from
the
time antibody was detectable in the circulation (Î_day 7—14 at
20°C;
Lamers,
The antigen first was located
exclusively
extracellu—
lar1y,
bound
to
the outer surface of
cells
or
to
reticular
fibres°
Lateron,
when all antigen became concentrated in MMCs, it was
found
both
intraand
extra—cellularly°
Moreover
the
presence of
lg could be demonstrated simul—
taneously (Lamers, 1985)…
These
data
suggest
a
dual
function
for
MMCs;
scavenger,
in
case
of
inert material and intracellular
located antigen, and
immunoregulatory, in case of surface bound antigen in presence of immunoglobu—
lin°
The antigen processing in both head— and trunk kidney involves, in first
instance
solitary
phagocytic
cells
and
reticulo—endothelial
cells.
Subsequently
MMCs
become
involved in an identical way as
observed in Spleen
(Lamers & De Haas,
As MMCs
become involved in antigen binding only after onset of the
anti—
body
response,
and
regarding
their
long—term
involvement in this process
(longer than 1 year;
Lamers
& De Haas,
1985),
this
process
resembles
the
trapping
of antigen in germinal centres in lymphoid organs of mammals°
There
it
is
thought to be involved in development of immunological memory (Klaus
et
1980)°
Although it has been shown that immunecomplexes are involved in
induction of
immunological memory in carp (Secombes & Resink, 1984), the
process
of antigen—trapping in carp and its relation to memory awaits further in—
vestigation°
The possible involvement of the complement factor C3 and the
Fc
fragment
of
lg in the binding of antigen to (melano—)macrophages is not documented in
DÆÂUNOGLOBULIN
Several reviewshave appeared on the structure and function of teleost im—
munoglobulin (lg)( Marchalonis, 1977;
Dorson, 1981;
Ellis, 1982).
In common
carp lg is found in most of the tissue fluids as blood, bile
and
mucus
skin
and
intestine (see
table
1).
In immunoelectrophoreses carp lg migrates as a
B globulin (Ambrosius, 1966) and it comprises about 6% of the total serum protein,
which
in carp
ranges
from 30—40 mg/ml (Hilge, 1980;
personal observation).
lg of cyprinids has only one heavy chain
isotype,
which
corresponds
With
the
mammalian
U chain.
Serum lgM is found exclusively in a tetrameric
form (Shelton & Smith, 1970), nevertheless a joining polypeptide (J—chain)
is
lacking.
During
the
immune
response
no
shift from high to low molecular
weight lg takes placeNo data are available on extra light—chain classes
in
carp,
as
has
been demonstrated for channel catfish (lctalurus punctatus) (L0bb
et
al., 1984), nor on structural adaptations of the secretory lg, like
a
se—
cretory
component.
The
physicochemical
properties of cyprinid lg slightly
varies
between species, eug.
Vilain et al.
(1984) reported that the
molecu—
1ar
weight
Of
18 heavy—chains of tench (Tinca tinca), carp and goldfish are
67:5>
76-0 and 79 kilodalton (KD) respectively, whereas the light chains
were
quite
uniform,
namely
about 26 KD.
Some properties of carp lg are given in
table 2.
_
CËrP lg has been demonstrated to be effective in a variety of processeS,
including agglutination, complement fixation and activation, precipitation,
etc.
Dorson, 1981).
On
the
contrary,
only
few
cretions îseîîîïeanân
lts
aCtlv1ty,
its
functional significance in se“
mucus
or
in
relation to hypersensitivity reactions;
e.gresults
of
Hines
&
Spira (1974) showed that parasital colonization on carp
skin was
SP€Cifically inhibited following immunization,
which
is
suggeStive
for
the
Pï0teCtive
role of
skin mucus antibody.
lmmediate hypersensitivity
reactions occur in cyprinid fish (Goven et al., 1980), although
no
data
are
available on the cells and mechanisms involved, and the function of lg in Us
C.H.J. Lamers
Lamers
&
De
Haas
(1985)
showed
that
the
bacterial
antigen
Aeromonas
hydrophila, after initial rapid phag0cytosis by ellipsoids, became located
in
MMCs
from
the
time antibody was detectable in the circulation (Î_day 7—14 at
20°C;
Lamers,
The antigen first was located
exclusively
extracellu—
lar1y,
bound
to
the outer surface of
cells
or
to
reticular
fibres°
Lateron,
when all antigen became concentrated in MMCs, it was
found
both
intraand
extra—cellularly°
Moreover
the
presence of
lg could be demonstrated simul—
taneously (Lamers, 1985)…
These
data
suggest
a
dual
function
for
MMCs;
scavenger,
in
case
of
inert material and intracellular
located antigen, and
immunoregulatory, in case of surface bound antigen in presence of immunoglobu—
lin°
The antigen processing in both head— and trunk kidney involves, in first
instance
solitary
phagocytic
cells
and
reticulo—endothelial
cells.
Subsequently
MMCs
become
involved in an identical way as
observed in Spleen
(Lamers & De Haas,
As MMCs
become involved in antigen binding only after onset of the
anti—
body
response,
and
regarding
their
long—term
involvement in this process
(longer than 1 year;
Lamers
& De Haas,
1985),
this
process
resembles
the
trapping
of antigen in germinal centres in lymphoid organs of mammals°
There
it
is
thought to be involved in development of immunological memory (Klaus
et
1980)°
Although it has been shown that immunecomplexes are involved in
induction of
immunological memory in carp (Secombes & Resink, 1984), the
process
of antigen—trapping in carp and its relation to memory awaits further in—
vestigation°
The possible involvement of the complement factor C3 and the
Fc
fragment
of
lg in the binding of antigen to (melano—)macrophages is not documented in
DÆÂUNOGLOBULIN
Several reviewshave appeared on the structure and function of teleost im—
munoglobulin (lg)( Marchalonis, 1977;
Dorson, 1981;
Ellis, 1982).
In common
carp lg is found in most of the tissue fluids as blood, bile
and
mucus
skin
and
intestine (see
table
1).
In immunoelectrophoreses carp lg migrates as a
B globulin (Ambrosius, 1966) and it comprises about 6% of the total serum protein,
which
in carp
ranges
from 30—40 mg/ml (Hilge, 1980;
personal observation).
lg of cyprinids has only one heavy chain
isotype,
which
corresponds
With
the
mammalian
U chain.
Serum lgM is found exclusively in a tetrameric
form (Shelton & Smith, 1970), nevertheless a joining polypeptide (J—chain)
is
lacking.
During
the
immune
response
no
shift from high to low molecular
weight lg takes placeNo data are available on extra light—chain classes
in
carp,
as
has
been demonstrated for channel catfish (lctalurus punctatus) (L0bb
et
al., 1984), nor on structural adaptations of the secretory lg, like
a
se—
cretory
component.
The
physicochemical
properties of cyprinid lg slightly
varies
between species, eug.
Vilain et al.
(1984) reported that the
molecu—
1ar
weight
Of
18 heavy—chains of tench (Tinca tinca), carp and goldfish are
67:5>
76-0 and 79 kilodalton (KD) respectively, whereas the light chains
were
quite
uniform,
namely
about 26 KD.
Some properties of carp lg are given in
table 2.
_
CËrP lg has been demonstrated to be effective in a variety of processeS,
including agglutination, complement fixation and activation, precipitation,
etc.
Dorson, 1981).
On
the
contrary,
only
few
cretions îseîîîïeanân
lts
aCtlv1ty,
its
functional significance in se“
mucus
or
in
relation to hypersensitivity reactions;
e.gresults
of
Hines
&
Spira (1974) showed that parasital colonization on carp
skin was
SP€Cifically inhibited following immunization,
which
is
suggeStive
for
the
Pï0teCtive
role of
skin mucus antibody.
lmmediate hypersensitivity
reactions occur in cyprinid fish (Goven et al., 1980), although
no
data
are
available on the cells and mechanisms involved, and the function of lg in Us