Disease-related variations of the glycosylation of haptoglobin in the dog
(1998) In Journal of Comparative Pathology 119(3). p.227-238- Abstract
- Haptoglobin phenotypes have been shown in human medicine to be related to the prevalence of various diseases. Furthermore, abnormal glycosylation of haptoglobin has been reported as a consequence of liver disease, cancer and immunological disorders in man. To our knowledge, similar findings have not, so far, been reported in canine disease. The present paper describes a method for investigation of canine haptoglobin phenotypes and of microheterogeneity caused by altered glycosylation. The method consisted of isoelectric focusing (IEF) of dog serum, followed by immunoblotting. The results indicated the existence of only one canine haptoglobin phenotype with a characteristic microheterogeneity pattern in healthy dogs. Changes in this pattern... (More)
- Haptoglobin phenotypes have been shown in human medicine to be related to the prevalence of various diseases. Furthermore, abnormal glycosylation of haptoglobin has been reported as a consequence of liver disease, cancer and immunological disorders in man. To our knowledge, similar findings have not, so far, been reported in canine disease. The present paper describes a method for investigation of canine haptoglobin phenotypes and of microheterogeneity caused by altered glycosylation. The method consisted of isoelectric focusing (IEF) of dog serum, followed by immunoblotting. The results indicated the existence of only one canine haptoglobin phenotype with a characteristic microheterogeneity pattern in healthy dogs. Changes in this pattern were found in serum from dogs with liver disease, predominantly chronic progressive hepatitis, and with different kinds of anaemia. Pretreatment of serum with neuraminidase or glycopeptidase F (PNGase F) resulted in identical IEF patterns of haptoglobin from healthy and diseased dogs. Moreover, a fucose-specific lectin was capable of binding to some of the abnormal haptoglobin fractions, mainly those found in association with anaemia. The changes described were interpreted as alterations of the carbohydrate content, with or without fucosylation, of some haptoglobin fractions. (Less)
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https://lup.lub.lu.se/record/1113311
- author
- Andersson, M ; Stenström, Martin LU ; Vatne, M ; Sevelius, E and Jonsson, L
- organization
- publishing date
- 1998
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Comparative Pathology
- volume
- 119
- issue
- 3
- pages
- 227 - 238
- publisher
- Elsevier
- external identifiers
-
- pmid:9807725
- scopus:0031728896
- ISSN
- 1532-3129
- language
- English
- LU publication?
- yes
- id
- d7a9de57-0332-41df-867f-00829f36a6d0 (old id 1113311)
- date added to LUP
- 2016-04-01 12:36:21
- date last changed
- 2022-04-21 17:44:09
@article{d7a9de57-0332-41df-867f-00829f36a6d0,
abstract = {{Haptoglobin phenotypes have been shown in human medicine to be related to the prevalence of various diseases. Furthermore, abnormal glycosylation of haptoglobin has been reported as a consequence of liver disease, cancer and immunological disorders in man. To our knowledge, similar findings have not, so far, been reported in canine disease. The present paper describes a method for investigation of canine haptoglobin phenotypes and of microheterogeneity caused by altered glycosylation. The method consisted of isoelectric focusing (IEF) of dog serum, followed by immunoblotting. The results indicated the existence of only one canine haptoglobin phenotype with a characteristic microheterogeneity pattern in healthy dogs. Changes in this pattern were found in serum from dogs with liver disease, predominantly chronic progressive hepatitis, and with different kinds of anaemia. Pretreatment of serum with neuraminidase or glycopeptidase F (PNGase F) resulted in identical IEF patterns of haptoglobin from healthy and diseased dogs. Moreover, a fucose-specific lectin was capable of binding to some of the abnormal haptoglobin fractions, mainly those found in association with anaemia. The changes described were interpreted as alterations of the carbohydrate content, with or without fucosylation, of some haptoglobin fractions.}},
author = {{Andersson, M and Stenström, Martin and Vatne, M and Sevelius, E and Jonsson, L}},
issn = {{1532-3129}},
language = {{eng}},
number = {{3}},
pages = {{227--238}},
publisher = {{Elsevier}},
series = {{Journal of Comparative Pathology}},
title = {{Disease-related variations of the glycosylation of haptoglobin in the dog}},
volume = {{119}},
year = {{1998}},
}