The acute-phase protein serum amyloid A3 is expressed in the bovine mammary gland and plays a role in host defence

References

• Akerstedt M, Persson Waller K, Sternesjö A. (2007). Haptoglobin and serum amyloid A in relation to the somatic cell count in quarter, cow composite and bulk tank milk samples. J Dairy Res 74:198–203.
   PubMed Web of Science ®Google Scholar
• Akerstedt M, Persson Waller K, Bach Larsen L, Forsbäck L, Sternesjö A. (2008). Relationship between haptoglobin and serum amyloid A in milk and milk quality. Int Dairy J 18:669–674.
   Google Scholar
• Bing Z, Reddy SA, Ren Y, Qin J, Liao WS. (1999). Purification and characterization of the serum amyloid A3 enhancer factor. J Biol Chem 274:24649–24656.
   PubMedGoogle Scholar
• Bradford MM. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72:248–254.
   PubMed Web of Science ®Google Scholar
• Burvenich C, Paape MJ, Hill AW, Guidry AJ, Miller RH, Heyneman R, Kremer WD Brand A. (1994). Role of the neutrophil leucocyte in the local and systemic reactions during experimentally induced E. coli mastitis in cows immediately after calving. Vet Q 16:45–50.
   PubMed Web of Science ®Google Scholar
• Capuco AV, Bright SA, Pankey JW, Wood DL, Miller RH, Bitman J. (1992). Increased susceptibility to intramammary infection following removal of teat canal keratin. J Dairy Sci 75:2126–2130.
   PubMed Web of Science ®Google Scholar
• Casl MT, Coen D, Simic D. (1996). Serum amyloid A protein in the prediction of postburn complications and fatal outcome in patients with severe burns. Eur J Clin Chem Clin Biochem 34:31–35.
   Google Scholar
• Casl MT, Surina B, Glojnaric-Spasic I, Pape E, Jagarinec N, Kranjcevic S. (1995). Serum amyloid A protein in patients with acute myocardial infarction. Ann Clin Biochem 32:196–200.
   Google Scholar
• Chomczynski P. (1993). A reagent for the single-step simultaneous isolation of RNA, DNA and proteins from cell and tissue samples. Biotechniques 15:532–534, 536–537.
   PubMed Web of Science ®Google Scholar
• Church GM, Gilbert W. (1984). Genomic sequencing. Proc Natl Acad Sci U S A 81:1991–1995.
   PubMed Web of Science ®Google Scholar
• Eckersall PD. (1999). The Acute Phase Response In Animals. Japanese Society of Veterinary Clinical Pathology. Tokyo; p. 10–21.
   Google Scholar
• Eckersall PD. (2004). The time is right for acute phase protein assays. Vet J 168:3–5.
   Google Scholar
• Eckersall PD, Young FJ, McComb C, Hogarth CJ, Safi S, Weber A, McDonald T, Nolan AM, Fitzpatrick JL. (2001). Acute phase proteins in serum and milk from dairy cows with clinical mastitis. Vet Rec 148:35–41.
   PubMed Web of Science ®Google Scholar
• Eckersall PD, Young FJ, Nolan AM, Knight CH, McComb C, Waterston MM, Hogarth CJ, Scott EM, Fitzpatrick JL. (2006). Acute phase proteins in bovine milk in an experimental model of Staphylococcus aureus subclinical mastitis. J Dairy Sci 89:1488–1501.
   Google Scholar
• Goldammer T, Zerbe H, Molenaar A, Schuberth HJ, Brunner RM, Kata SR, Seyfert HM. (2004). Mastitis increases mammary mRNA abundance of beta-defensin 5, toll-like-receptor 2 (TLR2), and TLR4 but not TLR9 in cattle. Clin Diagn Lab Immunol 11:174–185.
   PubMedGoogle Scholar
• Goodman RE, Schanbacher FL. (1991). Bovine lactoferrin mRNA: sequence, analysis, and expression in the mammary gland. Biochem Biophys Res Commun 180:75–84.
   PubMed Web of Science ®Google Scholar
• Grönlund U, Hultén C, Eckersall PD, Hogarth C, Persson Waller K. (2003). Haptoglobin and serum amyloid A in milk and serum during acute and chronic experimentally induced Staphylococcus aureus mastitis. J Dairy Res70(4):379–386.
   Google Scholar
• Gruys E, Toussaint M, Upragarin N, van Ederen A, Adewuyi S, Candiani D, Nguyen T, Sabeckiene J.(2005a). Acute-phase reactants, challenge in the near future. 5th International Colloquium on Animal Acute Phase Proteins, Dublin.
   Google Scholar
• Gruys E, Toussaint MJM, Upragarin N, van Ederen AM, Adewuyi AA, Candiani D, Nguyen TKA, Sabeckiene J.(2005b). Acute phase reactants, challenge in the near future of animal production and veterinary medicine. J Zhejiang Univ. Sci 6B:941–947.
   Google Scholar
• Hari-Dass R, Shah C, Meyer DJ, Raynes JG. (2005). Serum amyloid A protein binds to outer membrane protein A of Gram-negative bacteria. J Biol Chem 280:18562–18567.
   PubMed Web of Science ®Google Scholar
• Hartmann A, Eide TC, Fauchald P, Bentdal O, Herbert J, Gallimore JR, Pepys MB. (1997). Serum amyloid A protein is a clinically useful indicator of acute renal allograft rejection. Nephrol Dial Transplant 12:161–166.
   PubMedGoogle Scholar
• Hirakura Y, Carreras I, Sipe JD, Kagan BL. (2002). Channel formation by serum amyloid A: a potential mechanism for amyloid pathogenesis and host defense. Amyloid 9:13–23.
   PubMed Web of Science ®Google Scholar
• Hiss S, Mielenz M, Bruckmaier RM, Sauerwein H. (2004). Haptoglobin concentrations in blood and milk after endotoxin challenge and quantification of mammary Hp mRNA expression. J Dairy Sci 87:3778–3784.
   PubMed Web of Science ®Google Scholar
• Hooper LV, Stappenbeck TS, Hong CV, Gordon JI. (2003). Angiogenins: a new class of microbicidal proteins involved in innate immunity. Nature Immunology 4:269–273.
   PubMed Web of Science ®Google Scholar
• Hubank M, Schatz DG. (1994). Identifying differences in mRNA expression by representational difference analysis of cDNA. Nucleic Acids Res 22:5640–5648.
   PubMed Web of Science ®Google Scholar
• Jensen LE, Whitehead AS. (1998). Regulation of serum amyloid A protein expression during the acute-phase response. Biochem J 334:489–503.
   PubMed Web of Science ®Google Scholar
• Kho YJ, Cho KK, Kim SC, Kim SH, Chung MI, Baik MG, Choi YJ. (2000). Rapid communication: cloning of bovine serum amyloid A3 cDNA. J Anim Sci 78:2756–2757.
   Google Scholar
• Larson MA, Weber A, Weber AT, McDonald TL. (2005). Differential expression and secretion of bovine serum amyloid A3 (SAA3) by mammary epithelial cells stimulated with prolactin or lipopolysaccharide. Vet Immunol Immunopathol 107:255–264.
   PubMedGoogle Scholar
• Larson MA, Wei SH, Weber A, Mack DR, McDonald TL. (2003a). Human serum amyloid A3 peptide enhances intestinal MUC3 expression and inhibits EPEC adherence. Biochem Biophys Res Commun 300:531–540.
   PubMedGoogle Scholar
• Larson MA, Wei SH, Weber A, Weber AT, McDonald TL. (2003b). Induction of human mammary-associated serum amyloid A3 expression by prolactin or lipopolysaccharide. Biochem Biophys Res Commun 301:1030–1037.
   PubMed Web of Science ®Google Scholar
• Liuzzo G, Biasucci LM, Gallimore JR, Grillo RL, Rebuzzi AG, Pepys MB, Maseri A. (1994). The prognostic value of C-reactive protein and serum amyloid a protein in severe unstable angina. N Engl J Med 331:417–424.
   PubMed Web of Science ®Google Scholar
• Mack DR, McDonald TL, Larson MA, Wei S, Weber A. (2003). The conserved TFLK motif of mammary-associated serum amyloid A3 is responsible for up-regulation of intestinal MUC3 mucin expression in vitro. Pediatr Res 53:137–142.
   PubMedGoogle Scholar
• McDonald TL, Larson MA, Mack DR, Weber A. (2001). Elevated extrahepatic expression and secretion of mammary-associated serum amyloid A 3 (M-SAA3) into colostrum. Vet Immunol Immunopathol 83:203–211.
   PubMed Web of Science ®Google Scholar
• Molenaar A, Rajan G, Stelwagen K, Grigor M, Davis S. (1999). A serum amyloid protein homologue is expressed by the mammary gland. In Research Seminar of the Waikato Academic division of the University of Auckland, Byrant Education Centre, Waikato Hospital, New Zealand.
   Google Scholar
• Molenaar A, Rajan G, Stelwagen K, Grigor M, Davis S. (2000). A serum amyloid protein homologue is expressed by the mammary gland. N Z Med J 10:85.
   Google Scholar
• Molenaar A, Rajan G, Pearson M, Miles M, Petrova R, Davis S, Stelwagen K. (2002). A serum amyloid protein homologue is expressed by the mammary gland in a similar pattern to lactoferrin. In the Third European Colloquium on Acute Phase Proteins, Food Safety & Acute Phase Proteins.
   Google Scholar
• Molenaar AJ, Davis SR, Jack LJW, Wilkins RJ. (1995). Expression of the butyrophilin gene, a milk fat globule membrane protein, is associated with the expression of the alpha 1casein gene. Histochem J 27:388–394.
   Google Scholar
• Molenaar AJ, Davis SR, Wilkins RJ. (1992). Expression of alpha-lactalbumin, alpha-S1-casein, and lactoferrin genes is heterogeneous in sheep and cattle mammary tissue. J Histochem Cytochem 40:611–618.
   PubMed Web of Science ®Google Scholar
• Molenaar AJ, Kuys YM, Davis SR, Wilkins RJ, Mead PE, Tweedie JW. (1996). Elevation of lactoferrin gene expression in developing, ductal, resting, and regressing parenchymal epithelium of the ruminant mammary gland. J Dairy Sci 79:1198–1208.
   PubMedGoogle Scholar
• Nguyen TKA, Stockhofe N, Toussaint MJM, Vivanco V, Gruys E, Niewold TA. (2003). Serum amyloid A in acute phase response of cows with mastitis experimentally induced by streptococcus uberis. Fourth European Colloquium on acute phase proteins, Segovia, Spain; Abstract 23, p. 76.
   Google Scholar
• Nielsen BH, Jacobsen S, Andersen PH, Niewold TA, Heegaard PMH. (2004). Acute phase protein concentrations in serum and milk from healthy cows, cows with clinical mastitis and cows with extramammary inflammatory conditions. Vet Rec 154:361–365.
   Google Scholar
• Oliver SP, Mitchell BA. (1983). Susceptibility of bovine mammary gland to infections during the dry period. J Dairy Sci 66:1162–1166.
   PubMed Web of Science ®Google Scholar
• O’Mahony MC, Healy AM, Harte D, Walshe KG, Torgerson PR, Doherty ML. (2006). Milk amyloid A: correlation with cellular indices of mammary inflammation in cows with normal and raised serum amyloid A. Res Vet Sci 80:155–161.
   Google Scholar
• Pepys MB, Baltz ML. (1983). Acute phase proteins with special reference to C-reactive protein and related proteins (pentaxins) and serum amyloid A protein. Adv Immunol 34:141–212.
   PubMed Web of Science ®Google Scholar
• Petersen HH, Gardner IA, Rossitto P, Larsen HD, Heegaard PMH. (2005). Accuracy of milk amyloid A (MAA) concentration and somatic cell count for diagnosing bovine mastitis. 5th International Colloquium on Animal Acute Phase Proteins. Dublin.
   Google Scholar
• Rainard P, Riollet C. (2006). Innate immunity of the bovine mammary gland. Vet Res 37:369–400.
   PubMed Web of Science ®Google Scholar
• Rentrop M, Knapp B, Winter H, Schweizer J. (1986). Aminoalkylsilane-treated glass slides as support for in situ hybridization of keratin cDNAs to frozen tissue sections under varying fixation and pretreatment conditions. Histochem J 18:271–276.
   PubMedGoogle Scholar
• Rienhoff Jr HY, Huang JH, Li X Liao WSL. (1990). Molecular and cellular biology of serum amyloid A. Mol Biol Med 7:287–298.
   PubMedGoogle Scholar
• Riggs MG, McLachlan A. (1986). A simplified screening procedure for large numbers of plasmid mini-preparations. Biotechniques 4:310–313.
   Google Scholar
• Salonen M, Hirvonen J, Pyörälä S, Sankari S, Sandholm M. (1996). Quantitative determination of bovine serum haptoglobin in experimentally induced Escherichia coli mastitis. Res Vet Sci 60:88–91.
   Google Scholar
• Sambrook J, Fritsch EF, Maniatis T. (1989). Molecular Cloning: A Laboratory Manual. Second Edition. Cold Spring Harbour Laboratory Press, USA.
   Google Scholar
• Schultz DR, Arnold PI. (1990). Properties of four acute phase proteins: C-reactive protein, serum amyloid A protein, α-1-acid glycoprotein, and fibrinogen. Semin Arthritis Rheum 20:129–147.
   PubMed Web of Science ®Google Scholar
• Sellar GC, Whitehead AS. (1993). The acute phase response and major acute phase proteins in early host defence. J Biomed Sci 4:1–9.
   Google Scholar
• Shah C, Hari-Dass R, Raynes JG. (2006). Serum amyloid A is an innate immune opsonin for Gram-negative bacteria. Blood 108:1751–1757.
   PubMed Web of Science ®Google Scholar
• Shamay A, Homans R, Fuerman Y, Levin I, Barash H, Silanikove N, Mabjeesh SJ. (2005). Expression of albumin in nonhepatic tissues and its synthesis by the bovine mammary gland. J Dairy Sci 88:569–576.
   PubMedGoogle Scholar
• Shin K, Yamauchi K, Teraguchi S, Hayasawa H, Tomita M, Otsuka Y, Yamazaki S. (1998). Antibacterial activity of bovine lactoferrin and its peptides against enterohaemorrhagic Escherichia coli O157:H7. Lett Appl Microbiol 26:407–411.
   PubMed Web of Science ®Google Scholar
• Singh K, Dobson J, Phyn CVC, Davis SR, Farr VC, Molenaar AJ, Stelwagen K. (2005). Milk accumulation decreases expression of genes involved in cell–extracellular matrix communication and is associated with induction of apoptosis in the bovine mammary gland. Livestock Prod Sci 98:67–78.
   Google Scholar
• Swanson K, Gorodetsky S, Good L, Davis S, Musgrave D, Stelwagen K, Farr V, Molenaar A. (2004). Expression of a beta-defensin mRNA, lingual antimicrobial peptide, in bovine mammary epithelial tissue is induced by mastitis. Infect Immun 72:7311–7314.
   PubMed Web of Science ®Google Scholar
• Tartoff KD, Hobbs CA. (1987). Improved media for growing plasmid and cosmid clones. Focus Bethesda Res Lab 9:12.
   Google Scholar
• Thielen MA, Mielenz M, Hiss S, Zerbe H, Petzl W, Schuberth HJ, Seyfert HM, Sauerwein H. (2007). Short communication: cellular localization of haptoglobin mRNA in the experimentally infected bovine mammary gland. J Dairy Sci 90:1215–1219.
   PubMed Web of Science ®Google Scholar
• Thuring RW, Sanders JP, Borst P. (1975). A freeze-squeeze method for recovering long DNA from agarose gels. Anal Biochem 66:213–220.
   PubMed Web of Science ®Google Scholar
• Uhlar CM, Whitehead AS. (1999). Serum amyloid A, the major vertebrate acute-phase reactant. Eur J Biochem 265:501–523.
   PubMedGoogle Scholar
• Urieli-Shoval S, Cohen,P, Eisenberg S, Matzner Y. (1998). Widespread expression of serum amyloid A in histologically normal human tissues. Predominant localization to the epithelium. J Histochem Cytochem 46:1377–1384.
   PubMed Web of Science ®Google Scholar
• Wang L, Lashuel HA, Walz T, Colon W. (2002). Murine apolipoprotein serum amyloid A in solution forms a hexamer containing a central channel. Proc Natl Acad Sci U S A 99:15947–15952.
   PubMed Web of Science ®Google Scholar
• Wang L, Lashuel HA, Colon W. (2005). From hexamer to amyloid:marginal stability of apolipoprotein SAA2.2 leads to in vitro fibril formation at physiological temperature. Amyloid 12:139–148.
   PubMed Web of Science ®Google Scholar
• Wang L, Colon W. (2007). Effect of zinc, copper, and calcium on the structure and stability of serum amyloid A. Biochemistry 46:5562–5569.
   Google Scholar
• Weber A, Weber AT, McDonald TL, Larson MA. (2006). Staphylococcus aureus lipotechoic acid induces differential expression of bovine serum amyloid A3 (SAA3) by mammary epithelial cells: implications for early diagnosis of mastitis. Vet Immunol Immunopath 109:79–83.
   PubMedGoogle Scholar
• Wellnitz O, Kerr DE. (2004). Cryopreserved bovine mammary cells to model epithelial response to infection. Vet Immunol Immunopathol 101:191–202.
   PubMed Web of Science ®Google Scholar
• Whicher JT, Chambers RE, Higginson J, Nashef L, Higgins PG. (1985). Acute phase response of serum amyloid A protein and C reactive protein to the common cold and influenza. J Clin Pathol 38:312–316.
   PubMed Web of Science ®Google Scholar
• Wilkins MR, Gasteiger E, Bairoch A, Sanchez JC, Williams KL, Appel RD Hochstrasser DF. (1999). Protein identification and analysis tools in the ExPASy server. Method Mol Biol (Clifton, NJ) 112:531–552.
   PubMedGoogle Scholar
• Winter P, Miny M, Baumgartner W. (2005). Interpretation of SAA concentrations in milk from dairy ewes and goats. 5th International Colloquium on Animal Acute Phase Proteins Dublin
   Google Scholar
• Winter P, Miny M, Fuchs K, Baumgartner W. (2006). The potential of measuring serum amyloid A in individual ewe milk and in farm bulk milk for monitoring udder health on sheep dairy farms. Res Vet Sci 81:321–326.
   PubMed Web of Science ®Google Scholar
• Yamada T, Kluve-Beckerman B, Liepnieks JJ, Benson MD. (1994). Fibril formation from recombinant human serum amyloid A. Biochim Biophys Acta. Mol Basis Dis 1226:323–329.
   PubMed Web of Science ®Google Scholar
• Yamauchi K, Tomita M, Giehl TJ, Ellison RT 3rd. (1993). Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect Immun 61:719–728.
   PubMed Web of Science ®Google Scholar
• Yang W, Molenaar A, Kurts-Ebert B, Seyfert HM. (2006). NF-kappaB factors are essential, but not the switch, for pathogen-related induction of the bovine beta-defensin 5-encoding gene in mammary epithelial cells. Mol Immunol 43:210–225.
   Google Scholar
• Zagorski MG, Yang J, Shao H, Ma K, Zeng H, Hong A. (1999). Methodological and chemical factors affecting amyloid B peptide amyloidogenicity. Method Enzymol 309:189–204.
   Google Scholar