Purification and biochemical characterization of a fibroblast growth factor-binding protein (FGF-BP) from the lactoferrin fraction of bovine milk

A peptidomic approach to biomarker discovery for bovine mastitis

“…Kawakami et al [36] concluded that FGFBP may be tightly associated with lactoferrin in bovine milk. Plath et al [37] have successfully examined the expression and localization of FGFBP in the bovine mammary gland and it may be important in the local regulation of the bovine mammary gland.…”

Fractionation of bovine whey proteins and characterisation by proteomic techniques

“…Not surprisingly lactoperoxidase, which is a common contaminant of lactoferrin preparations, was also found associated with lactoferrin at higher M r . Highly basic proteins at the next level of magnitude were the ribonucleases PDZ domain containing 6 (secreted protein ribonuclease 4) and angiogenin 1 (spots 11, 12), both of which have been isolated chromatographically from the lactoferrin fraction of bovine milk (Kawakami et al, 2006). Several other proteins of high pI and mid-high M r were identified in spots/regions on the gel where lactoferrin was identified as the major species.…”

Characterization of meFucoidan as a Selective Inhibitor for Secretory Phospholipase A2-IIA and the Phosphorylation of meFucoidan-Binding Proteins by A-Kinase in Vitro

“…14,15) Briefly, these functional basic proteins and synthetic peptides were separately immobilized on a QCM plate in 8 ml of 40 mM Tris-HCl (pH 7.2) at 30°C until an equilibrium was attained. The indicated concentrations of meFucoidan were added to the equilibrated solutions.…”

“…12) On the other hand, we reported recently that (i) two sulfated lipids [sulfatide and cholesterol-3-sulfate (CH-3S), SCS] highly stimulate the phosphorylation of several SCSbinding proteins (SCS-BPs), such as high mobility group protein 1 (HMG1), 13) bovine FGF-binding protein (FGF-BP), 14) and p5 (N-terminal 28 amino acid residues of acidic FGF-BP), 15) by casein kinase 1 (CK1) in vitro; and (ii) the direct binding of SCS to these basic proteins causes them to undergo conformational changes, which presumably facilitate their high phosphorylation by CK1 in vitro. [13][14][15] However, there is no report concerning the effect of meFucoidan on the physiological functions of these SCS-BPs involved in the inflammatory responses.…”

“…12) On the other hand, we reported recently that (i) two sulfated lipids [sulfatide and cholesterol-3-sulfate (CH-3S), SCS] highly stimulate the phosphorylation of several SCSbinding proteins (SCS-BPs), such as high mobility group protein 1 (HMG1), 13) bovine FGF-binding protein (FGF-BP), 14) and p5 (N-terminal 28 amino acid residues of acidic FGF-BP), 15) by casein kinase 1 (CK1) in vitro; and (ii) the direct binding of SCS to these basic proteins causes them to undergo conformational changes, which presumably facilitate their high phosphorylation by CK1 in vitro. [13][14][15] However, there is no report concerning the effect of meFucoidan on the physiological functions of these SCS-BPs involved in the inflammatory responses. Therefore, the present study was carried out to determine (i) the inhibitory effect of meFucoidan, in comparison with two sulfated compounds (heparin and sulfatide), on the activities of sPLA 2 -IIA and pancreatic PLA 2 (pPLA 2 ); (ii) the binding affinity of meFucoidan with four functional basic proteins (sPLA 2 -IIA, bFGF, histone H2B and Hcore 164B) and four synthetic FGF-BP peptides (sp5, GE13, RS6 and RS6 variant) containing potent phosphorylation sites for cAMP-dependent protein kinase (A-kinase); and (iii) the inhibitory effect of meFucoidan on the A-kinase-mediated phosphorylation of these substrate peptides in vitro.…”