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K A Glennemeier

Publications and source records attributed to K A Glennemeier.

3 recordsLinked to original sources

Comparative studies of thyroxine binding proteins in turtle plasma using column chromatography.

Thyroxine (T4) binding proteins in turtle plasma were compared with those of various mammalian and nonmammalian (fish, birds) species using gel filtration chromatography (Bio-Gel). High-affinity T4 binding was observed in all mammals studied, in the chicken, and in one species of turtle, Trachemys scripta. This high affinity T4 binding protein (TBP) appears to be the major component of T4 transport in the turtle; selective removal of this TBP greatly diminished binding activity in T. scripta plasma. In all other nonmammalian species studied (including other turtles), T4 binding appeared to be associated primarily with relatively low affinity components such as albumin. Albumin concentrations in turtle (T. scripta, and Chelydra serpentina) plasmas were examined by measurement of dry weight, protein assay (Bradford), radioimmunoassay, and electrophoretic densitometry. While C. serpentina may have total protein concentrations approaching that of human plasma, albumin content in both turtles was estimated at about 3-4 mg/ml, less than 10% that of human plasma albumin; larger molecular weight components that do not bind T4 comprise a greater proportion of turtle plasma protein. Additionally, purified T. scripta albumin exhibits lower T4 binding than does human albumin; binding to turtle albumin is also reduced by fatty acids. Taken together, these results indicate a lesser role for albumin in plasma T4 binding in T. scripta than in humans, and, thus, a larger role for the T4 binding protein, TBP. Other turtles lacking a TBP may rely wholly on low affinity albumin binding that also has a lower capacity than that in mammals.

Adult↗

Binding affinities of thyroxine-binding proteins in turtle plasma.

Binding affinities (Ka) for thyroxine (T4) by blood plasma and purified plasma proteins from two turtles, the slider (Trachemys scripta) and snapper (Chelydra serpentina), were compared with those of a human using equilibrium dialysis. The purified T4 binding protein (TBP) from T. scripta had a high affinity that was lower by about fivefold than that of human TBG (3.2 x 10(9) vs 1.7 x 10(10) M-1). The affinity of T4 binding by TBP was similar to that determined for whole plasma from this species. T. scripta plasma stripped of TBP by affinity chromatography showed a greatly reduced Ka (2.8 x 10(5) M-1) similar to that of albumin purified from the same species (3.6 x 10(5) M-1), as well as a marked increase in free T4 (9.7%) as compared to whole turtle plasma (0.13%). The T4 binding of snapping turtle plasma (Ka = 5 x 10(5) and free T4 = 2.7%) was similar to that of the TBP-stripped plasma and albumin. Binding affinities for the two turtle and human albumins were similar. Because of low concentrations of albumin in the turtle blood (estimated at ca. 10 mg/ml based on binding), TBP probably accounts for a greater proportion of T4 binding in the slider turtle than does TBG in the human; e.g., when plasma T4 and TBP are elevated in T. scripta, > 98% of bound T4 would be associated with TBP. When both TBP and T4 are depressed (e.g., as in hatchlings), free T4 may actually be higher than in conditions when total T4 is elevated.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

In vivo effects of dexamethasone on the tumor growth of glucocorticoid-sensitive Fu5-derived rat hepatoma cells.

We have previously demonstrated that BDS.1 cells are a minimal deviation rat hepatoma cell line that is hypersensitive to the anti-proliferative effects of glucocorticoids in vitro. When transplanted into athymic mice, exposure to dexamethasone reduced the initial growth rate and increased the latency time before detection of palpable BDS.1-derived tumors but did not affect the maximal growth rate, size and histology of the tumor. After collagenase dissociation, the in vitro growth of BDS.1-derived tumor cells was fully suppressed by dexamethasone. Exposure to insulin prevented the glucocorticoid inhibition of anchorage-independent growth of BDS.1 cell colonies in vitro and may therefore be one of the systemic factors that masks the long term in vivo growth response of glucocorticoids.

Animals↗