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PubMed2005

Methodological approaches to the study of metabolism across individual tissues in man.

PURPOSE OF REVIEW: This article is intended to briefly overview available methodological approaches for the study of regional metabolism in man in vivo, and to summarize recent advances in this field of research. RECENT FINDINGS: Several methods have been developed and currently allow for the qualitative and quantitative assessment of energy interconversions and substrate fluxes across individual tissues of man, including the measurement of arteriovenous concentration differences, microdialysis, and nuclear magnetic resonance spectroscopy of carbon, hydrogen, and phosphorus isotopes. Each method alone has been used rather extensively to examine certain aspects of organ and tissue metabolism under a variety of experimental conditions, and has contributed novel information in this regard. The most exciting development appears to be the combined use of more than one investigational technique, across one or more tissues simultaneously. A handful of recent studies have employed complex experimental designs or hybrid methodologies, ultimately demonstrating the potential for a more detailed assessment of metabolism at the local level. SUMMARY: Clearly, advances in the use, performance, and applications of available methods are expected to provide improved and more powerful tools for the metabolic investigation of organs and tissues in humans in vivo.

Blood Flow Velocity↗
PubMed1969

Identification of components of (Na+ plus K+)-adenosine triphosphatase by double isotopic labeling and electrophoresis.

A microsomal adenosine triphosphatase (ATPase) that requires both sodium and potassium ions is thought to be identical with, or an integral part of, the active cation transport system located in cell membranes. Attempts to isolate and purify (Na(+) + K(+))-ATPase have met with limited success because solubilization of microsomal protein causes partial, if not complete, loss of enzymatic activity. We now report the isolation from rat kidney microsomes of proteins which, though enzymatically inactive, could still be identified as components of the (Na(+) + K(+))-ATPase system. Phosphoproteins known to be intermediates in the hydrolysis of ATP by (Na(+) + K(+))-ATPase were prepared by incubating rat kidney microsomes with gamma-labeled ATP(33) in the presence of sodium or with P(32)-orthophosphate in the presence of ouabain. After the P(32)- and P(33)-labeled microsomes had been dissolved in phenol-acetic acid-urea, the resultant solutions were mixed and subjected to polyacrylamide gel electrophoresis. The radioactivity from both phosphorus isotopes was found almost exclusively in one of the resultant 21 protein bands. In contrast, the radioactive protein from DFP(32)-labeled microsomes moved slightly faster than the radioactive protein from microsomes labeled with P(33)-orthophosphate in the presence of ouabain. DFP inhibits (Na(+) + K(+))-ATPase by reacting with a nucleophilic site at or near the active site. These results suggest that while a single protein component of (Na(+) + K(+))-ATPase accepts the terminal phosphate from ATP, the final splitting of this phosphoprotein intermediate may be catalyzed by nucleophilic sites on a second protein.

Adenosine Triphosphatases↗