Myosin II regulation during C. elegans embryonic elongation: LET-502/ROCK, MRCK-1 and PAK-1, three kinases with different roles.

Myosin II plays a central role in epithelial morphogenesis; however, its role has mainly been examined in processes involving a single cell type. Here we analyze the structure, spatial requirement and regulation of myosin II during C. elegans embryonic elongation, a process that involves distinct epidermal cells and muscles.

The RhoGAP RGA-2 and LET-502/ROCK achieve a balance of actomyosin-dependent forces in C. elegans epidermis to control morphogenesis.

Embryonic morphogenesis involves the coordinate behaviour of multiple cells and requires the accurate balance of forces acting within different cells through the application of appropriate brakes and throttles. In C. elegans, embryonic elongation is driven by Rho-binding kinase (ROCK) and actomyosin contraction in the epidermis.

Quantitative determination of the binding of epsilon-aminocaproic acid to native plasminogen.

The binding of epsilon-amino[14C]caproic acid (6-aminohexanoic acid, EACA) to native human plasminogen was determined using the ultrafiltration technique of Paulus (Paulus, H. (1969) Anal. Biochem.

Heterogeneity of bovine snout epidermal prekeratin.

The prekeratin of the snout of cows was extracted with 0-1 mol/l citric acid-sodium citrate buffer, pH 2-6. The results of equilibrium ultracentrifugation analyses of this prekeratin strongly suggest that this protein is not homogeneous. This conclusion is in accordance with the observations of two other investigators whose data infer that there is no major homogeneous keratin precursor in cow's lip or snout epidermis.

Properties of the major component of a peptic digest of rabbit antibody.

The molecular weight of the active, major component isolated from a peptic digest of rabbit antibody was found to be 106,000. After treatment with a disulfide-splitting reagent, the molecular weight was 56,000, and the products migrated as a single peak in the ultracentrifuge. he univalent fragments thus formed can be partially recombined by passage through IR-120 cation-exchange resin at room temperature or by treatment with a difunctional organic mercurial.