Hostname: page-component-669899f699-tzmfd Total loading time: 0 Render date: 2025-04-25T07:25:31.676Z Has data issue: false hasContentIssue false
  • English
  • Français

Differential expression and secretion of α1-acid glycoprotein in bovine milk

Published online by Cambridge University Press:  09 July 2007

Fabrizio Ceciliani ,
Vanessa Pocacqua ,
Cristina Lecchi ,
Riccardo Fortin ,
Raffaella Rebucci ,
Giancarlo Avallone ,
Valerio Bronzo ,
Federica Cheli  and
Paola Sartorelli
Fabrizio Ceciliani*
Affiliation:
Dipartimento di Patologia Animale, Igiene e Sanità Pubblica Veterinaria, Via Celoria 10, 20133 Milan
Vanessa Pocacqua
Affiliation:
Dipartimento di Patologia Animale, Igiene e Sanità Pubblica Veterinaria, Via Celoria 10, 20133 Milan
Cristina Lecchi
Affiliation:
Dipartimento di Patologia Animale, Igiene e Sanità Pubblica Veterinaria, Via Celoria 10, 20133 Milan
Riccardo Fortin
Affiliation:
Dipartimento di Scienze Cliniche Veterinarie, Via Celoria 10, 20133 Milan
Raffaella Rebucci
Affiliation:
Dipartimento di Scienze e Tecnologie Veterinarie per la Sicurezza Alimentare, Via Celoria 10, 20133 Milan
Giancarlo Avallone
Affiliation:
Dipartimento di Patologia Animale, Igiene e Sanità Pubblica Veterinaria, Via Celoria 10, 20133 Milan
Valerio Bronzo
Affiliation:
Dipartimento di Patologia Animale, Igiene e Sanità Pubblica Veterinaria, Via Celoria 10, 20133 Milan
Federica Cheli
Affiliation:
Dipartimento di Scienze e Tecnologie Veterinarie per la Sicurezza Alimentare, Via Celoria 10, 20133 Milan
Paola Sartorelli
Affiliation:
Dipartimento di Patologia Animale, Igiene e Sanità Pubblica Veterinaria, Via Celoria 10, 20133 Milan
*
*For correspondence; e-mail: fabrizio.ceciliani@unimi.it
Get access Rights & Permissions [Opens in a new window]

Abstract

α1-Acid glycoprotein (AGP) is a lipocalin that is produced mainly by the liver and secreted into plasma in response to infections and injuries. In this study, we evaluated AGP isoforms that can be detected in bovine milk. We found that milk-AGP content is made up of at least two isoform groups, a low MW group (44 kDa) that is produced in the mammary gland (MG-AGP), and a higher MW group (55–70 kDa), that is produced by somatic cells (SC-AGP). Identical SC-AGP isoforms can be found both in milk and blood PMN cells. Analysis of the mammary tissue cDNA showed that the sequence of the MG-AGP isoform is identical to that of plasma AGP. Each group contains several proteins with different MWs and different isoelectric points, as shown by 2D-electrophoresis. The glycosylation patterns of these isoforms were analysed by means of specific lectin binding, to evaluate the degree of sialylation, fucosylation and branching. The MG-AGP glycan pattern was identical to plasma AGP produced by the liver. Several differences were detected, however, between plasma and SC-AGP isoforms, the most evident being the strong degree of fucosylation and the elevated number of di-antennary glycans in SC-AGP. Immunohistochemistry showed that AGP is found in all tissues that make up the mammary gland, but that it is most likely produced for the main part by the alveoli.

Keywords

α1-acid glycoproteinacute phase reactionglycosylationudder defense
Type
Research Article
Information
Journal of Dairy Research , Volume 74 , Issue 3 , August 2007 , pp. 374 - 380
Copyright
Copyright © Proprietors of Journal of Dairy Research 2007

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

Article purchase

Temporarily unavailable

References

Ceciliani, F, Grossi, C, Giordano, A, Pocacqua, V & Paltrinieri, S 2004 Decreased sialylation of the acute phase protein alpha1-acid glycoprotein in feline infectious peritonitis (FIP). Veterinary Immunology and Immunopathology 99 229–236CrossRefGoogle ScholarPubMed
Ceciliani, F, Pocacqua, V, Provasi, E, Comunian, C, Bertolini, A, Bronzo, V, Moroni, P & Sartorelli, P 2005 Identification of the bovin α1-Acid Glycoprotein in colostrum and milk. Veterinary Research 36 735–746CrossRefGoogle ScholarPubMed
Ceciliani, F, Pocacqua, V, Miranda-Ribera, A, Bronzo, V, Lecchi, C & Sartorelli, P 2007 a1-acid glycoprotein modulates apoptosis in bovine monocytes. Veterinary Immunology and Immunopathology 116 145–152CrossRefGoogle Scholar
Dosogne, H, Vangroenweghe, F, Barrio, B, Rainard, P & Burvenich, C 2001 Decreased number and bactericidal activity against Staphylococcus aureus of the resident cells in milk of dairy cows during early lactation. Journal of Dairy Research 68 539–549CrossRefGoogle ScholarPubMed
Fournier, T, Bouach, N, Delafosse, C, Crestani, B & Aubier, M 1999 Inducible expression of the α1-Acid glycoprotein gene by alveolar macrophages: prostaglandine E2 and cyclin AMP act as positive stimuli. Journal of Immunology 163 1883–2890Google Scholar
Gorg, A, Postel, W & Gunther, S 1988 The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 9 531–546CrossRefGoogle ScholarPubMed
Hochepied, T, Berger, FG, Baumann, H & Libert, C 2003 α1-Acid glycoprotein: an acute phase protein with inflammatory and immunomodulatory properties. Cytokine and Growth Factors Reviews 54 25–34CrossRefGoogle Scholar
Logdberg, L & Wester, L 2000 Immunocalins: a lipocalin subfamily that modulates immune and inflammatory responses. Biochimica and Biophysica Acta 1482 284–297CrossRefGoogle ScholarPubMed
McDonald, TL, Larson, MA, Mack, DR & Weber, A 2001 Elevated extrahepatic expression and secretion of mammary-associated serum amyloid A3 (M-SAA3) into colostrum. Veterinary Immunology and Immunopathology 82 201–211Google Scholar
Mehrzad, J, Dosogne, H, Meyer, E, Heyneman, R & Burvenich, C 2001 Respiratory burst activity of blood and milk neutrophils in dairy cows during different stages of lactation. Journal of Dairy Research 68(3) 399–415CrossRefGoogle ScholarPubMed
Nakano, M, Kakehi, K, Tsai, M & Lee, YC 2004 Detailed structural features of glycan chains derived from a1-acid glycoproteins of several different animals: the presence of hypersialylated, O-acetylated sialic acids but not disialyle residues. Glycobiology 14 431–441CrossRefGoogle Scholar
Petersen, HH, Nielsen, JP & Heegard, PM 2004 Application of acute phase protein measurement in veterinary clinical chemistry. Veterinary Research 35 163–187CrossRefGoogle ScholarPubMed
Poland, DC, Vallejo, JJ, Niessen, HW, Nijmeyer, R, Calafat, J, Porse, T, Van Het Hof, B & Van Dijk, W 2005 Activated human PMN synthesize and release a strongly fucosylated glycoform of a1-acid glycoprotein which is transiently deposted in human myocardial infarction. Journal of Leukocyte Biology 77 1–8Google Scholar
Rainard, P & Riollet, C 2006 Innate immunity of the bovine mammary gland. Veterinary Research 37 369–400CrossRefGoogle ScholarPubMed
Sorensson, J, Matejka, GL, Ohlson, M & Haraldsson, B 1999 Human endothelial cells produce orosomucoid, an important component of the capillary barrier. American Journal of Physiology 276 530–534Google ScholarPubMed
Tamura, K, Yatsu, T, Itoh, H & Motoi, Y 1989 Isolation, characterization and quantitative measurement of serum a1-acid glycoprotein in cattle. Nippon Juigaku Zasshi 51 987–994CrossRefGoogle Scholar
Theilgaard-Monch, K, Jacobsen, LC, Rasmussen, T, Niemann, CU, Udby, L, Borup, R, Gharib, M, Arkwright, PD, Gombart, AF, Calafat, J, Porse, BT & Borregaard, N 2005 Highly glycosylated α1-acid glycoprotein is synthesized in myelocytes, stored in secondary granules, and released by activated neutrophils. Journal of Leukocyte Biology 78(2) 462–470CrossRefGoogle ScholarPubMed
Tilg, H, Vannier, E, Vachino, G, Dinarello, C & Mier, JJW 1993 Anti-inflammatory properties of hepatic acute phase proteins: preferential induction of interleukin 1 (IL-1) receptor antagonist over IL-1 beta synthesis by human periferal blood mononuclear cells. Journal of Experimental Medicine 178 1629–1636CrossRefGoogle Scholar
Van Molle, W, Libert, C, Fiers, W & Brouckaert, P 1997 Alpha 1-acid glycoprotein and alpha 1-antitrypsin inhibit TNF-induced but not anti-Fas-induced apoptosis of hepatocytes in mice. Journal of Immunology 159 3555–3564CrossRefGoogle Scholar
Williams, JP, Weiser, MR, Pechet, TT, Kobzik, L, Moore, FD & Hechtman, HB 1997 alpha 1-Acid glycoprotein reduces local and remote injuries after intestinal ischemia in the rat. American Journal of Physiology 273(5Pt1) G1031–1035Google ScholarPubMed
Zavizion, B, Van Duffelen, M, Schaeffer, W & Politis, I 1996 Establishment and characterization of a bovine mammary epithelial cell line with unique properties. In vitro Cellular Development and Biology 32 138–148CrossRefGoogle ScholarPubMed
Supplementary material: PDF

Ceciliani Supplementary Material

Figure.pdf

Download Ceciliani Supplementary Material(PDF)
PDF 16.6 KB