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C Terner

Publications and source records attributed to C Terner.

At least 19 recordsLinked to original sources

E-health, phase two: the imperative to integrate process automation with communication automation for large clinical reference laboratories.

The initial efforts of e-health have fallen far short of expectations. They were buoyed by the hype and excitement of the Internet craze but limited by their lack of understanding of important market and environmental factors. E-health now recognizes that legacy systems and processes are important, that there is a technology adoption process that needs to be followed, and that demonstrable value drives adoption. Initial e-health transaction solutions have targeted mostly low-cost problems. These solutions invariably are difficult to integrate into existing systems, typically requiring manual interfacing to supported processes. This limitation in particular makes them unworkable for large volume providers. To meet the needs of these providers, e-health companies must rethink their approaches, appropriately applying technology to seamlessly integrate all steps into existing business functions. E-automation is a transaction technology that automates steps, integration of steps, and information communication demands, resulting in comprehensive automation of entire business functions. We applied e-automation to create a billing management solution for clinical reference laboratories. Large volume, onerous regulations, small margins, and only indirect access to patients challenge large laboratories' billing departments. Couple these problems with outmoded, largely manual systems and it becomes apparent why most laboratory billing departments are in crisis. Our approach has been to focus on the most significant and costly problems in billing: errors, compliance, and system maintenance and management. The core of the design relies on conditional processing, a "universal" communications interface, and ASP technologies. The result is comprehensive automation of all routine processes, driving out errors and costs. Additionally, compliance management and billing system support and management costs are dramatically reduced. The implications of e-automated processes can extend beyond the specific transaction problems they are designed to solve. The ready access and communication of process details required by e-automation can apply to many other business functions.

Accounts Payable and Receivable↗

Cyclic adenosine 3',5'-monophosphate-phosphodiesterases in epididymis and prostate of castrate and of aged rats.

The activities of the low-Km and high-Km forms of cyclic AMP phosphodiesterase (PDE) were determined in extracts prepared from epididymis and prostate taken from adult (10-12 months) and from aged (32-35 months) rats. The maximum velocity V of low-Km PDE in the epididymis of normal adult rats (approx. 300 pmoles/min per mg protein) was increased after castration by 80%, whereas V of the high-Km form remained unchanged, suggesting that only the low-Km PDE is subject to regulation by the animals' endocrine status. In the epididymis of aged rats V of low-Km PDE was unchanged, whereas V of high-Km PDE (approx. 3000 pmoles/min per mg protein) was decreased by 40%; in the prostate of aged rats V of both low-Km (approx. 225 pmoles/min per mg protein), and of high-Km PDE (approx. 1500 pmoles/min per mg protein) were decreased by 50-60%. The absence of interdependence of the two forms of the enzyme in their response to changes in environmental conditions in each organ suggests different mechanisms of control of their activities and adds validity to the reported age-related decline of low-Km-PDE activity in prostate.

3',5'-Cyclic-AMP Phosphodiesterases↗

Control of low Km cyclic adenosine 3',5'-monophosphate-phosphodiesterase in prostate and heart of adult and aged rats.

The activity of low Km cAMP-phosphodiesterase (PDE) was determined in extracts of prostate and heart of adult (10-12 months old) and aged (32-35 months old) Sprague-Dawley rats; the enzyme's response to endogenous inhibitors extracted from the two organs was analyzed by kinetic studies. Different mechanisms of inhibition, non-competitive in prostate and competitive in heart extracts, indicate organ-specificity of the inhibitor. The decreased PDE activity in organ extracts of aged rats and its continued sensitivity to the endogenous inhibitor suggest an age-associated impairment of the tissues' ability to terminate cAMP-mediated signals.

3',5'-Cyclic-AMP Phosphodiesterases↗

Endogenous inhibitors of cyclic adenosine 3',5'-monophosphate-phosphodiesterase in rat epididymis.

Stabilization of cyclic adenosine 3',5'-monophosphate (cAMP)-phosphodiesterase (PDE) in 50% glycerol made possible the removal of endogenous inhibitors from tissue extracts by dialysis and the storage of the extracts at -20 degrees C without loss of PDE activity. Dialysates of heat-inactivated epididymal extracts were fractionated by liquid chromatography, and 4 fractions-F2, F5, F7, and F12-were found to contain endogenous inhibitors of PDE. The masses of the fractions required to inhibit low-Km PDE activity by ca. 50% in 430-microliter incubation mixtures were F2, 89 micrograms; F5, 23 micrograms; F7, 275 micrograms; and F12, 1.2 mg. The mechanisms of inhibition of low-Km PDE by the endogenous inhibitors were investigated by kinetic analysis of enzyme-inhibitor interaction. F2 and F12 inhibited PDE competitively; F5 and F7 decreased both apparent Km and Vmax, suggesting an uncompetitive mechanism of inhibition. The high potency of F5 in low concentration suggests that it may be a physiological modulator of low-Km cAMP-PDE activity.

3',5'-Cyclic-AMP Phosphodiesterases↗

Androgen control of an inhibitory modulator of phosphodiesterase in rat epididymis and prostate.

When rats were injected with the progestin ethynodiol diacetate in doses that suppressed spermatogenesis and the growth of accessory sex glands, the level of phosphodiesterase in epididymal and prostate tissues increased 5- to 10-fold. This increase was prevented by concurrent administration of testosterone propionate. A similar increase in phosphodiesterase activity was observed in the epididymides and prostates of castrated animals, with reversal by treatment with androgen. In immature rats approaching puberty, the phosphodiesterase activity in epididymis and prostate increased while the blood testosterone level remained low; as the testosterone level rose with the onset of puberty, the phosphodiesterase activity decreased. Incubation of enzymically active extracts of accessory tissues from castrated rats with heat-treated extracts of the corresponding normal tissues resulted in strong inhibition of the initially high phosphodiesterase activity. The addition of heat-treated extracts of accessory glands from castrated rats to enzymically active extracts of the corresponding tissues from normal rats resulted in a marked elevation of their phosphodiesterase activities. Of the two heat-stable modulators, the inhibitor factor was dialyzable. The dependence of this factor on testosterone suggests a mechanism of action by which the steroid hormone, by inducing the production in its target tissues of an inhibitory modulator of phosphodiesterase, controls the maintenance of functional levels of cAMP.

3',5'-Cyclic-AMP Phosphodiesterases↗

Changes in lipase and phosphatase activities of rat spermatozoa in transit from the caput to the cauda epididymidis.

Rat spermatozoa from the cauda epididymidis, freed from their cytoplasmic droplets and acrosomes, were found to have a lower lipid content and to incorporate [14C]glucose into their glycerides and glycerophosphatides at a lower rate than spermatozoa from the caput epididymidis. Against the background of the activities of some glycolytic enzymes which remained constant the activity of alkaline phosphatase decreased in spermatozoa migrating through the epididymis, whereas the activity of monoglyceride lipase increased. The corresponding enzyme activities of non-flagellate germ cells of the testis were measured for comparison. The triglyceride lipase of non-flagellate germ cells and of spermatozoa from both caput and cauda epididymidis was activated by cyclic 3':5'-AMP.

Acid Phosphatase↗