Responses of pink shrimp Farfantepenaeus brasiliensis (Latreille, 1817) (Penaeoidea) to physico-chemical parameters in a marine protected area: changes in abundance and distribution after 20 years

ABSTRACT

This study analysed the influence of temperature, salinity and sediment texture on the distribution of pink shrimp juveniles (Farfantepenaeus brasiliensis) over a 20-year period. The shrimps were sampled monthly in Fortaleza Bay, north coast of São Paulo, Brazil, in November 1988–October 1989 (period 1) and then 20 years later in November 2008–October 2009 (period 2). In period 1 we captured 80 juveniles whereas in period 2 we captured 226. The abundance and distribution of F. brasiliensis seemed to be modulated by temperature and sediment texture, along with the fishing activity. The management strategies established between the samplings might have been responsible for the higher abundance of juveniles seen during period 2. The strategies included the limitation of fishing effort, regulation of fishing equipment and the establishment of environmental protection areas and temporary fishing ban.     

Glucose transporter recycling in response to insulin is facilitated by myosin Myo1c

Insulin stimulates glucose uptake in muscle and adipocytes by signalling the translocation of GLUT4 glucose transporters from intracellular membranes to the cell surface. The translocation of GLUT4 may involve signalling pathways that are both independent of and dependent on phosphatidylinositol-3-OH kinase (PI(3)K). This translocation also requires the actin cytoskeleton, and the rapid movement of GLUT4 along linear tracks may be mediated by molecular motors. Here we report that the unconventional myosin Myo1c is present in GLUT4-containing vesicles purified from 3T3-L1 adipocytes. Myo1c, which contains a motor domain, three IQ motifs and a carboxy-terminal cargo domain, is highly expressed in primary and cultured adipocytes. Insulin enhances the localization of Myo1c with GLUT4 in cortical tubulovesicular structures associated with actin filaments, and this colocalization is insensitive to wortmannin. Insulin-stimulated translocation of GLUT4 to the adipocyte plasma membrane is augmented by the expression of wild-type Myo1c and inhibited by a dominant-negative cargo domain of Myo1c. A decrease in the expression of endogenous Myo1c mediated by small interfering RNAs inhibits insulin-stimulated uptake of 2-deoxyglucose. Thus, myosin Myo1c functions in a PI(3)K-independent insulin signalling pathway that controls the movement of intracellular GLUT4-containing vesicles to the plasma membrane.