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C J Vincent

Publications and source records attributed to C J Vincent.

7 recordsLinked to original sources

Different red blood cell characteristics in a primitive agnathan (M. glutinosa) and a more recent teleost (O. mykiss) influence their strategies for blood CO2 transport.

This study examines how the different red blood cell (rbc) characteristics in two lower vertebrates, the phylogenetically primitive hagfish and a more recent teleost, the rainbow trout, influence their strategies for blood CO2 transport. Deoxygenation of the blood resulted in a significant increase in rbc CO2 content in hagfish, but there were no significant changes in the CO2 content of plasma or whole blood under these conditions. In contrast, deoxygenation increased the CO2 content of the rbc, plasma and whole blood in the trout. These results demonstrate that the Haldane effect is much less important for CO2 transport in the hagfish as compared to the trout. The relative importance of the rbc and plasma in blood CO2 transport were roughly similar in hagfish and trout and were very different from that previously documented in another primitive vertebrate, the lamprey. In trout, however, the role of the rbc in CO2 carriage was increased upon the addition of the beta-adrenergic agonist isoproterenol (10(-5) M) to the blood. Taken together, these results and those recently collected for lampreys demonstrate that changes in rbc characteristics during vertebrate evolution have probably resulted in several important transitions in the strategy for blood CO2 transport.

Adrenergic beta-Agonists↗

Purification and characterization of recombinant human cyclooxygenase-2.

Recombinant human cyclooxygenase-2 (hCox-2, Prostaglandin G/H synthase-2) has been purified from baculovirus-Sf9 and vaccina virus-Cos-7 cell expression systems. The detergent-solubilized, purified enzyme is heterogeneous in terms of its glycosylation. The vaccinia virus hCox-2 is a mixture of two glycoforms, whereas baculovirus hCox-2 comprises at least four species. The specific cyclooxygenase activities of both enzymes are 43 mumol O2/min/mg with arachidonic acid which is within the range of values reported for ovine Cox-1. The Km values of arachidonic acid for hCox-2 and ovine Cox-1 are 0.9 and 2.7 microM, respectively. Six other C-18 and C-20 fatty acids containing at least one 1,4-cis,cis-pentadiene moiety were also identified as substrates for hCox-2. Linoleic and gamma-linolenic acid were determined by mass spectrometry as being hydroxylated primarily at the C-9 and C-13 positions, whereas linolenic acid was hydroxylated primarily at the C-12 and C-16 positions. hCox-2 binds heme such that maximal activity is observed at a stoichiometry of 1.0 heme per enzyme subunit. The apparent molecular mass of hCox-2, determined by gel filtration chromatography in the presence of 2.0% beta-octylglucoside, is consistent with a dimeric structure. The results of this study indicate that the physical and catalytic properties of recombinant hCox-2 are very similar to that of the extensively studied ovine Cox-1.

Arachidonic Acid↗