Conclusion
Changes in concentrations of O2Hb, HHb and tHb, induced by small and slow O2 changes, measured by NIRS over the neonatal brain, are inversely correlated to the measured changes in the oxidation state of CytO2. For small O2 changes the methodology CytO2 measurement needs to be improved.
Keywords
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
6. References
D.W. Lubbers, in: Oxygen Supply: Theoretical and Practical Aspects of Supply and Microcirculation in Tissue, edited by M. Kessler, et al. (University Park, Baltimore,1973), 151–155.
H. Beinert, R.W. Shaw, R.E. Hansen, and C.R. Hartzell, Studies on the origin of the near infrared (800–900 nm) absorption of cytochrome c oxidase. Biochim. Biophys. Acta. 458–470 (1980).
H.F. Bienfait, J.M. Jacobs, and E.C. Slater, Mitochondrial oxygen affinity as a function of redox and phosphate potentials, Biochim. Biophys. Acta. 376, 446–57 (1975).
F.F. Jobsis, Oxidative metabolism at low pO2, Fed. Proc. 31, 1404–13 (1972).
N.B. Hampson, E.M. Camporesi, B.W. Stolp, R.E. Moon, J.A. Griebel, and C.A. Piantadosi, Cerebral oxygen availability by NIR spectroscopy during transient hypoxia in humans, J. Appl. Physiol. 69, 907–13 (1990).
A.D. Edwards, G.C. Brown, M. Cope, D.T. Delpy, and E.O. Reynolds, Quantification of concentration changes in neonatal human cerebral oxidized cytochrome oxidase. J. Appl. Physiol. 71, 1907–13 (1991).
L. Skov and G. Greisen, Apparent cerebral cytochrome aa3 reduction during cardiopulmonary bypass in hypoxaemic children with congenital heart disease, Physiol. Meas. 15, 447–57 (1994).
M. Wolf, P. Evans, and H.U. Bucher, The Measurement of Absolute Cerebral Haemoglobin Concentration in Adults and Neonates, Adv. Exp. Med. Biol. 428, 219–227 (1997).
S. Wray, M. Cope, D.T. Delpy, J.S. Wyatt, and E.O. Reynolds, Characterization of the near infrared absorption spectra of cytochrome aa3 and haemoglobin for the non-invasive monitoring of cerebral oxygenation. Biochim Biophys Acta. 933, 184–92 (1988).
M. Brunori, E. Antonini, and M.T. Wilson, In: Metal Ions in Biological Systems XXIII, edited by H. Siegel (Marcel Dekker, New York) 187–228.
S.J. Matcher, C.E. Elwell, C.E. Cooper, M. Cope, and D.T. Delpy, Performance comparison of several published tissue near-infrared spectroscopy algorithms, Anal. Biochem. 227, 54–68 (1995).
C.E. Cooper and R. Springett, Measurement of cytochrome oxidase and mitochondrial energetics by near-infrared spectroscopy, Philos. Trans. R. Soc. Lond. B. Biol. Sci. 352, 669–676 (1997).
M. Ferrari, D.F. Hanley, D.A. Wilson, and R.J. Traystman, Redox changes in cat brain cytochrome-c oxidase after blood-fluorocarbon exchange. Am. J. Physiol. 258, H1706–13 (1990).
A.L. Sylvia and C.A. Piantadosi, O2 dependence of in vivo brain cytochrome redox responses and energy metabolism in blood less rats, J. Cereb. Blood. Flow. Metab. 8, 163–172 (1988).
M. Ferrari, M.A. R.J. Traystman, and D.F. Hanley, Cat brain cytochrome-c oxidase redox changes induced by hypoxia after blood-fluorocarbon exchange transfusion, Am. J. Physiol. 269, H417–24 (1995).
R. Stingele, B. Wagner, R.J. Traystman, and D.F. Hanley, Reduction of cytochrome-c oxidase copper precedes failing cerebral O2 utilization in fluorcarbon-perfused cats, Am. J. Physiol. 271, H579–87 (1996).
A.J. du Plessis, J. Newburger, H. Naruse, M. Tsuji, A. Walsh, G. Walter, D. Wypij, and J.J. Volpe, Cerebral oxygen supply and utilization during infant cardiac surgery, Ann. Neurol. 37, 488–97 (1995).
M. Tsuji, H. Naruse, J. Volpe, and D. Holtzman, Reduction of cytochrome aa3 measured by near-infrared spectroscopy predicts cerebral energy loss in hypoxic piglets, Pediatr. Res. 37, 253–9 (1995).
Y. Hoshi, O. Hazeki, Y. Kakihana, and M. Tamura, Redox behavior of cytochrome oxidase in the rat brain measured by near-infrared spectroscopy, J. Appl. Physiol. 83, 1842–8 (1997).
C.E. Cooper, S.J. Matcher, J.S. Wyatt, M. Cope, E.M. Nemoto, and D.T. Delpy, Near-infrared sepctroscopy of the brain: relevance to cytochrome oxidase bioenergetics. Biochem. Soc. Trans. 22, 974–980 (1994).
B. Chance, Metabolic heterogeneities in rapidly metabolizing tissues, L. Appl. Cardiol. 4, 207–221 (1989).
C. Cooper, M. Sharpe, C. Elwell, R. Springett, J. Penrice, L. Tyszczuk, P. Amess, J. Wyatt, V. Quaresima, and D. Delpy, The cytochrome oxidase redox state in vivo, Adv. Exp. Med. Biol. 428, 449–56 (1997).
J.M. Cimadevilla, L.M. Garcia Moreno, M.C. Zahonero, and J.L. Arias, Glial and neuronal cell numbers and cytochrome oxidase activity in CA1 and CA3 during postnatal development and aging of the rat, Mech. Ageing. Dev. 99, 49–60 (1997).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2006 Springer Science+Business Media, Inc.
About this paper
Cite this paper
Wolf, M., Keel, M., Dietz, V., von Siebenthal, K., Bucher, HU., Baenziger, O. (2006). Do Slow and Small Oxygen Changes Affect the Cerebral Cytochrome Oxidase Redox State Measured by Near-Infrared Spectroscopy?. In: Cicco, G., Bruley, D.F., Ferrari, M., Harrison, D.K. (eds) Oxygen Transport to Tissue XXVII. Advances in Experimental Medicine and Biology, vol 578. Springer, Boston, MA . https://doi.org/10.1007/0-387-29540-2_39
Download citation
DOI: https://doi.org/10.1007/0-387-29540-2_39
Publisher Name: Springer, Boston, MA
Print ISBN: 978-0-387-29543-5
Online ISBN: 978-0-387-29540-4
eBook Packages: Physics and AstronomyPhysics and Astronomy (R0)