Reducing Negative Attitudes Toward Immigrants in Russia and Taiwan: Possible Beneficial Effects of Naïve Dialecticism and an Incremental Worldview.

Greater mobility in human societies has resulted in more interactions and contact with immigrants. In the current research, we investigated how viewing the world as flexible, changing, and paradoxical (i.e., naïve dialecticism and an incremental theory) may predict one's authoritarian beliefs and in turn predict one's attitudes toward immigrants. To test the generalizability of our findings, we recruit comparable samples (i.e., college students) from two societies that are largely different (Russia and Taiwan). Great cultural similarities were observed. Naïve dialecticism and an incremental theory appeared as two distinctive constructs. People who were higher on naïve dialecticism and an incremental over entity theory had lower support for authoritarian beliefs (i.e., right-wing authoritarianism and social dominance orientation) and, in turn, had more favorable attitudes toward immigrants. Some cultural differences were also observed. Taiwanese participants' negative attitudes toward immigrants were entirely ideology-based, whereas Russian participants' negative attitudes toward immigrants were partly based on presumably personal experiences. Pan-cultural and culturally specific mechanisms in predicting attitudes toward immigrants were further discussed and explored.

Catch muscle of bivalve molluscs contains myosin- and twitchin-associated protein kinase phosphorylating myorod.

We have shown previously that myorod, a molluscan thick filament protein of unknown function, is phosphorylated by vertebrate smooth myosin light chain kinase (MLCK) in N-terminal unique region. The aim of the present study was to clarify whether such phosphorylation may occur in molluscan muscles. We detected three kinases endogenous to molluscan catch muscle, namely, to the complex of surface thick filament proteins that consists of twitchin, myosin, and myorod. The first kinase was a protein kinase A because it was inhibited by a specific inhibitor; the second one was associated with twitchin and phosphorylated myorod at its N-terminal unique region independently of Ca(2+); and the third kinase was bound to myosin and phosphorylated myorod as well as myosin in the C-terminal part of both proteins. The myosin-associated kinase was inhibited by micromolar concentration of calcium ions. This enzyme could be separated from myosin by chromatography, whereas the kinase associated with twitchin could not be separated from twitchin. Since twitchin has a MLCK-like domain, it is possible that this domain was responsible for myorod phosphorylation. Phosphorylation of myorod within the twitchin-myosin-myorod complex increased the actin-activated Mg(2+)-ATPase activity of myosin. Taken together, these results indicate that phosphorylation of myorod by kinases associated with key proteins of catch contraction may contribute to the functional activity of myorod in molluscan smooth muscle.

Phosphorylation of myorod (catchin) by kinases tightly associated to molluscan and vertebrate smooth muscle myosins.

Myorod, also known as catchin, a newly discovered component of molluscan smooth muscle thick filaments, is an alternative product of the myosin heavy chain gene. It contains a C-terminal rod part that is identical to that part of myosin and a unique N-terminal domain that is very small relative to the myosin head domain. The role of myorod in contraction or relaxation of this muscle type is unknown. In the present study we demonstrated that myorod was phosphorylated not only by a kinase endogenous to molluscan myosin and twitchin but also to vertebrate smooth muscle myosin light chain kinase (MLCK). The rates and maximal levels of phosphorylation were up to threefold higher than those observed by protein kinase A with clear optima at the physiological salt concentrations. Using a mild digestion with chymotrypsin we isolated an 11 kDa phosphopeptide and showed that the phosphorylation site was located at the N-terminal domain of myorod at Thr 141 position. The sequence around this site exhibited a high degree of similarity to that expected for the substrate recognition site of MLCK. The phosphorylation rates strongly depended on the ionic conditions indicating that this site could be readily sterically blocked during myorod polymerization. Another component of the thick filaments involved in regulation of the catch state, twitchin, was phosphorylated by MLCK and exhibited endogenous myorod kinase and MLCK activities. A possible role of these phosphorylation reactions in the regulation of molluscan smooth muscles is discussed.