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L. Lögdberg, Lena Wester (2000)
Immunocalins: a lipocalin subfamily that modulates immune and inflammatory responses.Biochimica et biophysica acta, 1482 1-2
Y. Kim, A. Varki (1997)
Perspectives on the significance of altered glycosylation of glycoproteins in cancerGlycoconjugate Journal, 14
T. Fournier, Najet Medjoubi-N, D. Porquet (2000)
Alpha-1-acid glycoprotein.Biochimica et biophysica acta, 1482 1-2
S. Hsu, L. Raine, H. Fanger (1981)
Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: a comparison between ABC and unlabeled antibody (PAP) procedures.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 29
Julian Williams, M. Weiser, T. Pechet, L. Kobzik, F. Moore, H. Hechtman (1997)
α1-Acid glycoprotein reduces local and remote injuries after intestinal ischemia in the rat.American journal of physiology. Gastrointestinal and liver physiology, 273 5
L. Rabehi, F. Ferrière, L. Saffar, L. Gattegno (1995)
alpha 1-Acid glycoprotein binds human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein via N-linked glycans.Glycoconjugate journal, 12 1
N. Waly, Timothy Gruffydd-Jones, Christopher Stokes, Michael Day (2001)
The distribution of leucocyte subsets in the small intestine of healthy cats.Journal of comparative pathology, 124 2-3
M. Costello, B. Fiedel, H. Gewurz (1979)
Inhibition of platelet aggregation by native and desialised alpha-1 acid glycoproteinNature, 281
A. Mackiewicz, K. Mackiewicz (1995)
Glycoforms of serum α1-acid glycoprotein as markers of inflammation and cancerGlycoconjugate Journal, 12
(1997)
Serum protein and the dysproteinemias
D. Biou, C. Bauvy, H. N'Guyen, P. Codogno, G. Durand, M. Aubery (1991)
Alterations of the glycan moiety of human αl-acid glycoprotein in late-term pregnancyClinica Chimica Acta, 204
S. Shiyan, N. Bovin (1997)
Carbohydrate composition and immunomodulatory activity of different glycoforms of α1-acid glycoproteinGlycoconjugate Journal, 14
G. Cattoretti, S. Pileri, C. Parravicini, M. Becker, S. Poggi, C. Bifulco, G. Key, L. D'Amato, E. Sabattini, E. Feudale, Fred Reynolds, J. Gerdes, F. Rilke (1993)
Antigen unmasking on formalin‐fixed, paraffin‐embedded tissue sectionsThe Journal of Pathology, 171
T. Hochepied, F. Berger, H. Baumann, C. Libert (2003)
Alpha(1)-acid glycoprotein: an acute phase protein with inflammatory and immunomodulating properties.Cytokine & growth factor reviews, 14 1
P. Bories, J. Féger, N. Benbernou, J. Rouzeau, J. Agneray, G. Durand (1990)
Prevalence of tri- and tetraantennary glycans of humanα1-acid glycoprotein in release of macrophage inhibitor of interleukin-1 activityInflammation, 14
K. Selting, Gregory Ogilvie, S. Lana, M. Fettman, K. Mitchener, R. Hansen, K. Richardson, J. Walton, M. Scherk (2000)
Serum Alpha 1-Acid Glycoprotein Concentrations in Healthy and Tumor-Bearing CatsJournal of Veterinary Internal Medicine, 14
D. Biou, C. Bauvy, H. N'Guyen, P. Codogno, G. Durand, M. Aubery (1991)
Alterations of the glycan moiety of human alpha 1-acid glycoprotein in late-term pregnancy.Clinica chimica acta; international journal of clinical chemistry, 204 1-3
M. Vasson, Monique Roch-Arveiller, Rémy Couderc, Jean Baguet, Denis Raichvarg (1994)
Effects of alpha-1 acid glycoprotein on human polymorphonuclear neutrophils: influence of glycan microheterogeneity.Clinica chimica acta; international journal of clinical chemistry, 224 1
J. Kaneko (1963)
Clinical biochemistry of domestic animals
F. Ceciliani, A. Giordano, V. Spagnolo (2002)
The systemic reaction during inflammation: the acute-phase proteins.Protein and peptide letters, 9 3
A. Mackiewicz, K. Mackiewicz (1995)
Glycoforms of serum alpha 1-acid glycoprotein as markers of inflammation and cancer.Glycoconjugate journal, 12 3
S. Duthie, P. Eckersall, D. Addie, C. Lawrence, O. Jarrett (1997)
Value of α1-acid glycoprotein in the diagnosis of feline infectious peritonitisVeterinary Record, 141
U. Laemmli (1970)
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 227
(1995)
An overview of feline enteric coronavirus and feline infectious peritonitis virus infection
A. Giordano, V. Spagnolo, A. Colombo, S. Paltrinieri (2003)
Changes in some acute phase protein and immunoglobulin concentrations in cats affected by feline infectious peritonitis or exposed to feline coronavirus infectionVeterinary Journal (London, England : 1997), 167
α1-Acid glycoprotein (AGP) is an acute-phase protein (APP) that modulates immune responses, probably – at least in humans – owing to the modification of its glycosylation pattern. On this perspective, feline AGP can be a useful comparative model, as it has different concentrations in cats susceptible or resistant to some disease. As a preliminary approach to the study of feline AGP (fAGP) we have purified this protein from feline serum by HPLC using human AGP (hAGP) as a model. Immunoblotting with a polyclonal antibody against fAGP and with a monoclonal antibody against hAGP was performed on serum from healthy cats, from cats exposed to feline coronavirus (FCoV) infection and from cats with purulent inflammations, such as feline infectious peritonitis (FIP), feline immunodeficiency virus (FIV) and feline leukemia virus (FeLV). Immunohistochemistry on tissues from healthy cats and from cats with different diseases (FIP, FIV, FeLV, locally extensive inflammation) was also performed with the same antibodies. Both hAGP and fAGP have been purified to homogenity as determined by SDS-PAGE. fAGP did not react with the anti-hAGP antibody which, in contrast, detected in feline serum a low MW protein that we called fAGP-related protein (fAGPrP). This protein was underexpressed in cats with FeLV and FIP. Both fAGP and fAGPrP were immunohistochemically detected in plasma and hepatocytes with a stronger intensity in cats with FIP and some inflammatory conditions. Moreover, fAGPrP was detected in the cytoplasm of tissue cells, most likely identifiable with plasma cells. These cells were rarely detectable in cats with FIV and FeLV, and numerous in cats with FIP and with locally extensive inflammation. In conclusion, purified fAGP has physicochemical characteristics similar to those of hAGP, but does not cross-react with anti-hAGP antibodies. In contrast, the anti-hAGP detected an AGP-related protein whose blood concentration and tissue distribution was not related to that of fAGP. Moreover, both fAGP and fAGPrP were differently expressed in cats with pathologic conditions compared to controls. Further study of these proteins by analysing their structural characteristics is required.
Comparative Clinical Pathology – Springer Journals
Published: Jan 1, 2003
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