In this study, we show that miR-34a not only inhibits INHBB in a direct way but also may result in the down-regulation of INHBB in regenerating liver. More importantly, we proved that knockdown of INHBB via a siRNA system could strongly repress rat Salvianolic-acid-C hepatocyte proliferation. In activin family, activin A has been shown to decelerate hepatocyte growth in LR. Interestingly, in our findings, activin B seemed to play an opposite role in cell proliferation with an opposite mRNA expression pattern after PHx. There have been a few reports comparing the biological potency of activin A and activin B. For example, stimulation of DNA synthesis by EGF could be inhibited by activin A, but not by activin B. It has been reported that activin A and activin B had opposite effects on Ca2+ signaling in islet cells, with activin A increasing, but activin B decreasing. Therefore, it is conceivable that the overall effect of activins during LR may result from the balance between the expression of INHBB and INHBA subunit genes. Apart from INHBB, we also confirmed Met as another target of miR-34a in the regenerating livers. It has been reported that an increase in Met, together with its ligand HGF, could lead to impaired liver regeneration. In accordance with previous study, our investigation suggests that miR-34a-mediated inhibition of Met may also contribute to the suppression of hepatocyte proliferation during LR. In conclusion, miR-34a is strongly induced in the late phase of LR after PHx. Elevated miR-34a greatly suppressed hepatocyte proliferation by targeting INHBB and Met. Our data also provided a tantalizing hint that miR-34a might be a ��stop�� signal in regenerating hepatocytes. When the immune system is compromised, or when the normal microbiota are disrupted, debilitating and often recurring mucosal diseases can result, uses adhesins, hypha AT-56 formation, phenotypic switching and production of extracellular hydrolytic enzymes to interact with its human host. Among C. albicans adhesins is the Als family, encoded by eight distinct genetic loci. Als proteins have a similar structure, including an N-terminal secretory signal sequence, followed by an NT domain of approximately 320 amino acids, a T domain of approximately 104 amino acids, a TR domain of head-to-tail copies of a Ser/Thr-rich repeated sequence, and a Ser/Thr-rich C domain of variable size and sequence. Mature Als molecules are large glycoproteins that are linked to b-1,6 glucan in the C. albicans cell wall. For example, the estimated sizes for mature Als1 and Als3 are 600 and 440 kDa, respectively. Because of its proposed similarity to functional domains of other adhesion proteins, the Als NT domain is often studied in the absence of the remainder of the mature molecule. X-ray crystallography and NMR were used to solve the structure of the Als9-2 and Als1 respectively.