Nutrient Composition and Flavor Profile of Crucian Carp Soup Utilizing Fish Residues through Comminution and Pressure-Conduction Treatment.

In conventional fish soup processing, valuable aquatic resources like fish skins, bones, and scales are often squandered. This study was aimed at investigating if comminution combined with pressure-conduction treatment has the potential to enhance the reutilization of cooking residues. The different blending ratios of original soup (OS), made from the initial cooking of fish, and residue soup (RS), produced from processed leftover fish parts, were alternatively investigated to satisfy the new product development. Comminution combined with pressure-conduction treatment significantly increased the nutrient contents of calcium, soluble proteins and total solids in crucian carp soup (p < 0.05). With the increase in RS ratio, the decomposition of inosine monophosphate (IMP) and free amino acids was accelerated, but the accumulation of aromatic compounds was promoted simultaneously. In addition, the Maillard reaction may lead to a reduction in aldehydes, causing a diminution in the characteristic flavor of fish soup, while the formation of 1-octen-3-ol can enhance the earthiness of the fish soup. The electronic tongue test results and the sensory results showed that the blend ratio of OS and RS at 7:3 had a more significant umami and fish aroma (p < 0.05). Under this condition, the mixed soup has better nutritional values and flavor characteristics.

Structural characterization and osteogenic bioactivity of a sulfated polysaccharide from pacific abalone (Haliotis discus hannai Ino).

Bone morphogenic protein-2 (BMP-2) is known to promote osteogenesis. To find novel adjuvants to enhance the activity of BMP-2, the present study investigated the structure BMP-2-induced osteogenic activity of a water-soluble polysaccharide from the gonad of pacific abalone (Haliotis discus hannai Ino) named AGSP. Through analysis of aldobiouronic acids released from AGSP, monosaccharide composition comparison of AGSP and its reduced product, and methylation analysis and NMR analysis of AGSP and its desulfated derivative, the main structure residue of AGSP was determined as →3)-GlcA(1→3)-Gal(1→ with sulfated branches comprised of prevelant Gal and minor Glc, and →4)-ß-GlcA(1→2)-α-Man(1→ residue was also found. AGSP possessed a sulfate content of 12.4% with a relative molecular weight of 6.6kDa. AGSP strengthened alkaline phosphatase activity induced by BMP-2 in a dose dependent manner at 10-200µg/mL with 425% enhancement being observed at 200µg/mL, indicating AGSP could be an adjuvant candidate to enhance osteogenic activity of BMP-2.

Sorafenib inhibits growth and metastasis of hepatocellular carcinoma by blocking STAT3.

AIM: To investigate the inhibitory role and the underlying mechanisms of sorafenib on signal transducer and activator of transcription 3 (STAT3) activity in hepatocellular carcinoma (HCC). METHODS: Human and rat HCC cell lines were treated with sorafenib. Proliferation and STAT3 dephosphorylation were assessed. Potential molecular mechanisms of STAT3 pathway inhibition by sorafenib were evaluated. In vivo antitumor action and STAT3 inhibition were investigated in an immunocompetent orthotopic rat HCC model. RESULTS: Sorafenib decreased STAT3 phosphorylation at the tyrosine and serine residues (Y705 and S727), but did not affect Janus kinase 2 (JAK2) and phospha-tase shatterproof 2 (SHP2), which is associated with growth inhibition in HCC cells. Dephosphorylation of S727 was associated with attenuated extracellular signal-regulated kinase (ERK) phosphorylation, similar to the effects of a mitogen-activated protein kinase (MEK) inhibitor U0126, suggesting that sorafenib induced S727 dephosphorylation by inhibiting MEK/ERK signaling. Meanwhile, sorafenib could also inhibit Akt phosphorylation, and both the phosphatidylinositol-3-kinase (PI3K) inhibitor LY294002 and Akt knockdown resulted in Y705 dephosphorylation, indicating that Y705 dephosphorylation by sorafenib was mediated by inhibiting the PI3K/Akt pathway. Finally, in the rat HCC model, sorafenib significantly inhibited STAT3 activity, reducing tumor growth and metastasis. CONCLUSION: Sorafenib inhibits growth and metastasis of HCC in part by blocking the MEK/ERK/STAT3 and PI3K/Akt/STAT3 signaling pathways, but independent of JAK2 and SHP2 activation.