Calmodulin in rat enterocyte: an immunogold electron-microscope study.

Immunogold labeling of ultrathin sections of the epithelium of rat small intestine has been used to obtain insights into the ultrastructural localization and possible function of calmodulin in the enterocyte. Calmodulin is found mainly overlying the periphery of the microvillous core, in agreement with the location of the 110-kDa calmodulin complex. Extremely small amounts of calmodulin can be detected along the interdigitating basolateral membrane. This immunogold electron-microscope study suggests that calmodulin plays an important role in regulating the mechanochemical activity of myosin I but not in processes associated with the basolateral membrane of rat enterocyte.

Calmodulin during development and metamorphosis in urodelan amphibians.

Calmodulin isolated and purified to homogeneity from young larvae is very similar to that obtained from adult Pleurodeles waltlii and these proteins are almost identical to previously described vertebrate calmodulins. During P. waltlii development, an increase in total individual calmodulin content is observed after the heart beating stage. In dorsal axial muscle, calmodulin level which is very high at the beginning of larval life (premetamorphosis) decreases strikingly in the first part of prometamorphosis. Such an evolution is observed in Ambystoma mexicanum too. Then, a significant increase occurs during metamorphosis. In contrast, calmodulin level in P. waltlii cardiac ventricular muscle increases continuously from hatching to the end of metamorphic climax. Thyroxine treatment which promotes precocious metamorphosis in P. waltlii and experimental metamorphosis in neotenic A. mexicanum, induces a rapid and significant increase in muscle calmodulin concentration.

Annexins in rat enterocyte and hepatocyte: an immunogold electron-microscope study.

In the present study, immunogold labeling of ultrathin sections of rat small intestine and liver has been used to obtain insights into the ultrastructural localization and possible functions of annexins. In enterocytes, annexins II, IV, and VI are found at the periphery of the core of each microvillus and of the rootlets, but are absent from the interrootlet space. Annexins II, IV, and VI are also observed close to the interdigitated plasma membrane. In hepatocytes, only annexin VI is found to be concentrated within the microvilli in the bile canaliculi, on the inner face of the sinusoidal cell surface, particularly in the space of Disse, and all along the plasma membrane. Annexin VI is also detected in mitochondria of enterocytes and hepatocytes. These localizations are in agreement with the concept of a close calcium-dependent association of annexins with membranes and cytoskeletal proteins, particularly with actin. Moreover, they support the hypothesis of an involvement of annexins in exocytotic and endocytotic processes, which take place in epithelial cells.

The expression of the 35- and 67-kDa calcimedins is dependent on thyroid hormone.

We have investigated the expression of the 35- and 67-kDa calcimedins and calmodulin during fetal and neonatal periods and in adulthood in rat liver, muscle, and brain. The 35- and 67-kDa calcimedin expression in liver and muscle increased during the perinatal period and correlated with the thyroid status of the developing rat. In fact, animals treated with thyroxine demonstrated a precocious appearance of the 35- and 67-kDa calcimedin in liver and muscle. Animals treated with methylthiouracil, an inhibitor of T4 and T3 synthesis, strongly suppressed the synthesis of the calcimedins in these tissues. Neither treatment influenced the levels of either the 35- and 67-kDa calcimedins in brain. In contrast, each tissue examined produced a unique pattern of calmodulin expression during development. None of the tissue calmodulin concentrations changed during hyper- or hypothyroid states. Collectively, these data support the concept that the intracellular calcium signal possesses multiple, independent molecular pathways of mediation. In addition, the variety of these pathways is influenced by hormonal preconditioning in that the cellular response to elevated cytosolic calcium is dependent upon the thyroid status of a tissue.