Vascular smooth muscle contractile properties in the turtle Pseudemys scripta elegans

1. Turtle aortic rings were characterized by high frequency spontaneous contractile activity and variable responsiveness to constrictor agents.2. The tissue response was remarkably insensitive to temperature at a range of 37°–15°C.3. The contractile response was effectively blocked by the calcium channel antagonist nifedipine and was substantially dependent on extracellular calcium concentrations.4. Lowering the sodium concentration of the bath medium resulted in a strong, transient contraction followed by reduced responsiveness to norepinephrine and the absence of spontaneous activity.5. Disruption of the vessel endothelium resulted in enhanced and reduced responsiveness to norepinephrine (NE) and acetylcholine (ACh), respectively.6. The results indicate that the regulation of contractile function in turtle vascular smooth muscle differs in several respects from that of mammalian tissue, perhaps, reflecting the adaptation of the vasculature to low pressure and ectothermic conditions.     

The retinopetal system in the turtle Pseudemys scripta elegans

Injections of 125I wheat-germ agglutinin or horseradish peroxidase into the eyes of turtles labeled retrogradely cells in a mesencephalic reticular area lying between the trochlear and the isthmic nuclei. Their number was small and they were found predominantly contralateral to the injected eye. These reticular neurons were not labeled following control injections into the orbital cavity and therefore are considered to project to the retina similar to correspondingly located neurons in some other vertebrates.     

Morphology and histochemistry of the ambiens muscle of the red-eared turtle (Pseudemys scripta)

Six fiber types have been described in the ambiens muscle of red-eared turtles. These include one slow oxidative type, two fast oxidative types, two fast oxidative and glycolytic types, and one fast glycolytic type. Fiber types are non-randomly distributed throughout cross sections of the muscle. There is a decreasing gradient of oxidative staining and an increasing gradient of glycolytic staining along an axis from the superficial to deep regions of the muscle. The slow oxidative fibers are predominantly located within one or two fascicles of the superficial surface of the muscle. The fast glycolytic fibers are predominant in deep fascicles. In contrast to previous reports of histochemically monotypic intrafusal fibers in turtle muscle, ambiens muscle spindles have been observed containing one to eleven intrafusal fibers, including two fiber types. Fiber diameter and area are consistently smaller than observed in most extrafusal fibers. Spindles are predominantly located in superficial and cranial fascicles of the ambiens muscle and are located in regions characterized by extrafusal fibers with high oxidative activity.     

Antioxidant systems and anoxia tolerance in a freshwater turtle Trachemys scripta elegans

In the search for MBP phosphorylating activities in Dictyostelium discoideum, we have found a proteolysis-activated protein kinase. This activity which is distributed between the soluble and the particulate fractions of the cell, uses MBP and histone as substrate and has a molecular mass of 140 kDa as detected in an in situ' assay.This protein kinase has several features shared by the protein kinase C family, such as substrate specificity and sensitivity to proteolysis, but its molecular mass is much larger than that described for the known protein kinase C isoforms.To better characterize this activity we have studied its sensitivity to several protein kinase C inhibitors and activators. This protein kinase is activated neither by phorbol ester nor by phosphatidylserine or Ca²⁺. The activity is inhibited by staurosporine and PKC pseudosubstrate, but is not affected by the specific protein kinase C inhibitor bisindolylmaleimide.These data lead us to propose that proteolytically activated Dictyostelium protein kinase belongs to the recently described protein kinase C-related family.