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While certain cases showed a discrepancy in fucosylated haptoglobin concentrations between the lectin-antibody ELISA and conventional lectin blotting, this novel type of lectin-antibody ELISA might be useful for a tumor marker for PC.

Mirabegron was well tolerated in real-world Japanese patients with overactive bladder and coexisting cardiovascular disease. No unexpected cardiovascular safety concerns were observed.

Abstract. α2-Heremans-Schmid glycoprotein (human fetuin) is one of numerous serum proteins produced in the liver. Recently, the biological functions of fetuin, such as calcification and insulin resistance, have been clarified. However, these effects appear to be indirect, occurring through binding to other molecules. When equal amounts of fetuin in sera were treated with chymotrypsin, resistance to the protease treatment was observed in patients with pancreatic cancer, but not in normal volunteers. To investigate the molecular mechanism behind this resistance, gel-filtration chromatography was performed. The results revealed that high molecular types of fetuin showed a resistance to protease treatment. When fetuin was purified from sera of patients with pancreatic cancer and normal volunteers, certain types of proteins, including haptoglobin (which binds to fetuin derived from pancreatic cancer patients), were identified using mass spectrometry. Furthermore, the oligosaccharide structures of fetuin analyzed with lectin microarray differed between pancreatic cancer patients and normal volunteers. This macro/micro heterogeneity of fetuin might contribute to pancreatic cancer resistance to chymotrypsin treatment. Introductionα2-Heremans-Schmid glycoprotein (aHSG, human fetuin) is one of the plasma proteins that occur in high concentrations during fetal life and gradually decrease towards adulthood.However, fetuin remains abundant in adult serum, and is mostly produced in the liver (1,2). Previous studies have demonstrated that fetuin isolated from cohn's fraction Vi of human plasma is a two-chain molecule consisting of an A-chain of 282 amino acid residues and a B-chain of 27 residues (3,4). it is thought that the circulating form of fetuin in serum is a two-chain protein with a heavy chain of 321 residues, which indicates the A chain with the connecting peptide, and a light chain of 27 residues, which indicates the B chain (5). Jahnen dechent W et al reported that chymotrypsin cleaved the critical Leu-Leu bond flanking the NH 2 -terminal portion of the connecting peptide region, and that this proteolysis was accelerated in sera of patients with sepsis (6).Fetuin is a glycoprotein with both N-and O-linked carbohydrate side chains whose structures vary in several biological aspects (7,8). Fetuin occurs in large amounts in blood and cerebrospinal fluid, accumulates to high concentrations in calcified bone, and is involved in the regulation of mineral concentration (9). Since fetuin belongs to one of the negative acute-phase proteins, levels of fetuin in serum are decreased in individuals with infections, malignancies, malnutrition and liver and renal diseases at the end stage (10-13). Its high affinity for bone mineral and ability to prevent the precipitation of basic calcium phosphates from supersaturated solutions suggest that fetuin is a potent systemic inhibitor of soft tissue calcification (14-17). As there is a similarity in anion acid structures between fetuin and TGF-β receptor, fetuin acts as an antagonist o...

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