dc.contributor.author
Zoellner, Anne
dc.date.accessioned
2018-06-07T22:51:21Z
dc.date.available
2000-12-14T00:00:00.649Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/9726
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-13924
dc.description
Die komplette Dissertation im pdf-Format (704.244 Bytes):
zoell.pdf
dc.description.abstract
The aim of these studies was to obtain more detailed information on the
occurrence and distribution of amyloidosis in captive and wild birds, to
analyse the relationship of amyloidosis to other diseases and influential
factors, and to characterize the avian amyloid protein histochemically and
immunohistochemically.
The studies were performed at the Institute for Zoo and Wildlife Research in
Berlin. Their basis were post-mortem reports and a diversity of organ
specimens embedded in paraffine wax from birds autopsied between 1970 and
1992.
The post-mortem reports on 8456 autopsied birds belonging to 23 avian orders
were analysed in the first part of this study. All records on birds with the
diagnose amyloidosis were evaluated in relation to species, sex, date of
death, accompanying diseases and causes of death.
The object of the second part of this study was to performe a histochemical
and immuno-histochemical characterization of the amyloid protein. For the
histochemical examinations the potassium permanganat reaction (WRIGHT et al.,
1977) was used on 100 selected birds from 13 orders. This method is suitable
for distinguishing the amyloid protein AA from other varieties of amyloid on
the basis of a strongly reduced or lost Congo red binding after exposure to
potassium permanganate. For this distinction, tissue sections pretreated with
potassium permanganat were stained with Congo red and compared with parallel
sections without potassium permanganat exposure. Amyloid was considered
permanganat-sensitive (and identified as amyloid AA protein) if all amyloid
deposits present in the tissue section totally or nearly totally (with more
than 90 % loss) lost their Congo red affinity. The immuno-peroxidase technique
(with diaminobenzidine as the chromogen) was used for immuno-histochemical
characterization of the amyloid protein on 50 selected birds from 13 orders.
As primary antibodies a commercially available monoclonal human anti-AA
antibody and a polyclonal rabbit anti-duck amyloid-A antibody were applied. By
using appropriate controls, all deposits in the tissue sections showing a
light to dark brown colour were identified als amyloid-A positive.
The results of these examinations can be summarized as follows:
1. In partial confirmation of studies performed by other authors the avian orders Anseri-formes, Phoenicopteriformes, Gruiformes and Charadriiformes were shown to be especially prone to amyloidosis. Differences in the incidence of amyloidosis were found also among families, genera and tribes within these orders.
2. According to the results of these studies, the somewhat higher incidence of amyloid occurence in winter and spring, as compared with the summer and autumn months, can not be considered as evidence for a true seasonal variation, as it was claimed by some other authors. In considering the age of the birds, a distinctly higher proportion of young birds with a very low incidence of amyloidosis was generally autopsied in summertime as compared to wintertime. In addition, beginning and course of amyloidosis can not be determined at autopsy due to the chronicity of this disease. Taking into account all these circumstances, a seasonal character of amyloidosis with a peak value in winter and spring can not reliably be demonstrated with certainty.
3. Avian amyloidosis occurred as so-called secondary form associated with chronic diseases or inflammations in the majority of cases. Idiopathic amyloidosis without a recognizable accompanying disease was found in 28,4 % of all cases. According to present knowledge, the two formes can be identified as a reactive amyloidosis which seems to be caused by the same or a similar pathogenetic mechanism.
4. The distribution pattern of the amyloid deposits is consistent with that of the systemic amyloidosis. Amyloid deposits occurred in more than one organ in most cases. Primarily involved were liver, spleen and kidneys.
5. According to the histochemical and immunohistochemical studies the avian amyloid examined belongs to the type AA. That means that the amyloid fibrils are derived from the acute phase protein SAA in all cases.
In conclusion, it can be stated that all cases of amyloidosis in birds
hitherto examined are of the reactive type or type AA.
en
dc.rights.uri
http://www.fu-berlin.de/sites/refubium/rechtliches/Nutzungsbedingungen
dc.subject.ddc
600 Technik, Medizin, angewandte Wissenschaften::630 Landwirtschaft::630 Landwirtschaft und verwandte Bereiche
dc.title
Untersuchungen zur Amyloidose bei Zoo- und Wildvögeln sowie zur Histo- und
Immunhistochemischen Charakterisierung des aviären Amyloidproteins
dc.contributor.firstReferee
Univ.-Prof. Dr. R.R. Hofmann
dc.contributor.furtherReferee
Univ.-Prof. Dr. V. Bergmann
dc.date.accepted
1997-11-28
dc.date.embargoEnd
2001-01-23
dc.identifier.urn
urn:nbn:de:kobv:188-1998001033
dc.title.translated
Studies about amyloidosis in captive and wild birds, with special regard to
the histochemical and immunohistochemical characterization of the avian
amyloid protein
en
refubium.affiliation
Veterinärmedizin
de
refubium.mycore.fudocsId
FUDISS_thesis_000000000015
refubium.mycore.transfer
http://www.diss.fu-berlin.de/1998/103/
refubium.mycore.derivateId
FUDISS_derivate_000000000015
dcterms.accessRights.dnb
free
dcterms.accessRights.openaire
open access