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T C Chen

Publications and source records attributed to T C Chen.

At least 235 records · Page 13Linked to original sources
PubMed1984

Difference between 1-84 parathyroid hormone and the 1-34 fragment on renal tubular calcium transport in the dog.

Acute clearance studies were performed in chronically thyroparathyroidectomized dogs to determine similarities and differences between the effects of 1-34 and 1-84 parathyroid hormone (PTH) on urinary calcium excretion. In a small (physiological) dose, 1-84 PTH caused no mean change in percentage calcium excretion, while the 1-34 fragment was frankly calciuric. At this dose, the two hormone preparations were equally phosphaturic. Fragments of PTH in the range 25-84 did not alter calcium or phosphate transport. We conclude that the entire molecule is required in order for the distal nephron effect of the hormone to enhance net calcium transport in the kidney to become manifest.

Adenylyl Cyclases↗
PubMed1983

Parathyroid hormone: effects of the 3-34 fragment in vivo and vitro.

The biologically active fragment ofparathyroid hormone, consisting of residues 1-34, and its in vitro antagonist, fragment 3-34, were administered separately or in combination to chronically thyroparathyroidectomized dogs. These fragments were also studied in vitro with dog renal cortical membranes. Fragment 3-34 inhibited the stimulation of adenylate cyclase by fragment 1-34 in vitro, but had no agonist or antagonistic effects on renal phosphate transport in vivo.

Adenylyl Cyclases↗
PubMed1982

Occupational exposure in the academic sector of the R.O.C.

This paper deals with occupational exposure in the academic sector of the Republic of China during the past two decades. The Tsing-Hua film badges were used for personnel monitoring. The radiation sources available in the research institutes and universities are listed and illustrated. The number, sex, age and per capita dose equivalent for the radiation workers in the past 21 yr are analyzed. The radioisotope production rate and the dose equivalent received by the workers are compared, and the results indicate that radiation protection has been greatly improved during last decade.

Academies and Institutes↗
PubMed1982

Participation of the renin system in treatment-resistant hypertension as measured by acute blockade of the angiotensin converting enzyme.

The acute blood pressure response to the angiotensin converting enzyme inhibitor, captopril, was used to measure participation of the renin-angiotensin system in treatment-resistant hypertension. By 2 h after a single 25-mg oral captopril dose in patients still receiving a diuretic-vasodilator-beta-blocker combination, systolic and diastolic blood pressures had fallen significantly; the decrease in diastolic pressure correlated with the control (immediately pre-captopril) plasma renin activity (r = 0.64, p less than 0.001). Apart from its possible contribution to the underlying hypertension, this captopril-identified renin component may have reflected diuretic and vasodilator-induced renin stimulation that could not adequately be prevented by the renin-lowering properties of the beta-blocker. Captopril, and perhaps other specific antirenin drugs, therefore, may be valuable adjuncts to treatment in patients with hypertension refractory to conventional therapy.

Adult↗
PubMed1982

Potentiation by calcium of the proximal tubular transport effects of parathyroid hormone.

Previous studies from this laboratory have demonstrated that a low ('physiological') dose of parathyroid hormone (PTH) effects a phosphaturia in chronically thyroparathyroidectomized (TPTX), hypocalcemic dogs, similar in magnitude to that seen in normal intact animals, without altering proximal tubular reabsorption. In addition, cyclic AMP did not increase following this amount of PTH, despite the phosphaturia. Since calcium is an important modulator of transport events, we studied the effects of restoring serum calcium (Ca) to normal before administering a physiological dose of PTH (0.3-0.5 U/kg). In hypocalcemic dogs given only physiological amounts of PTH, percentage phosphate excretion (%EPO4) rose from 3.81 +/- 1.48 to 18.29 +/- 5.69% (p less than 0.025) without any alteration in proximal tubular function. Ca infusion alone likewise did not change %EPO4 or proximal tubular transport. However, calcium-infused dogs given a physiological dose of PTH showed a reduction in proximal tubular fractional phosphate reabsorption from 0.73 +/- 0.04 to 0.63 +/- 0.04 (p less than 0.005), as well as an increase in %EPO4 (from 5.64 +/- 1.69 to 15.86 +/- 2.82%, p less than 0.001), without any increase in urinary or tissue cyclic AMP. We conclude that the elevation of the serum Ca to normal restores the ability of PTH in physiological amounts to alter proximal tubular PO4 transport. The data also suggest that this action of PTH is mediated by Ca, rather than by the adenylate cyclase system.

Absorption↗
PubMed1981

Inhibition of the renal tubular effects of parathyroid hormone on phosphate transport by prostaglandin E2.

The infusion of PGE2 into TPTX dogs abolishes the phosphaturic action of PTH in vivo. This effect occurs only if PGE2 infusion precedes the administration of PTH. The infusion of PGE2 in vivo induces a state of refractoriness of PTH-sensitive adenylate cyclase in renal middle medulla from TPTX dogs in vitro. These results suggest that PGE2 inhibits the biological effects of PTH, in part by altering the events related to PTH activation of renal adenylate cyclase. These effects of PGE2, a local mediator, suggest that the renal tubular cell may modulate its responses to multiple and antagonistic stimuli by altering local renal prostaglandins.

Adenylyl Cyclases↗
PubMed1980

Effects of di-isopropylfluorophosphate and isopropanol on the measurement of plasma renin activity.

Since the protease inhibitor, di-isopropylfluorophosphate (DFP), inhibits the cryoactivation of inactive renin, its addition to stored plasma should prevent unintended renin activation and thereby minimize this source of inaccuracy in the assay of plasma renin activity. However, we have found that 6 mmol/l DFP in stored frozen plasma actually reduced plasma renin activity from 4.89 +/- 0.13 (S.D.) to 2.48 +/- 0.17 ng . ml-1 . h-1 (p < 0.001). This effect did not occur if DFP was added immediately before assay, suggesting that the decreased renin activity reflected an action of DFP on components of the renin system during storage rather than any interference with the assay method itself. The organic solvent isopropanol, which is required to dilute the DFP, appeared responsible for this phenomenon, for when the isopropanol alone, in concentrations of 20 and 40 microliter/ml, was added to stored frozen plasma it decreased plasma renin activity from 3.6 +/- 0.3 to 2.2 +/- 0.1 and 0.6 +/- 0.1 ng . ml-1 . h-1, respectively (p < 0.001 in each case). Correspondingly, plasma renin substrate concentrations were decreased to 71% and 6% of control, indicating that the renin activity reductions produced by isopropanol were due to its denaturation of substrate. Moreover, addition of exogenous sheep renin substrate (1400 ng/ml) immediately before assay restored plasma renin activity to control. Thus, although DFP effectively prevents inadvertent renin activation in stored frozen plasma, it would seem important that subsequent assays for plasma renin activity be performed in the presence of added exogenous substrate.

1-Propanol↗
PubMed1980

Magnetic resonance studies of apolipoprotein C-I nitroxide labeled or [13C]methyl enriched at methionine-38.

One of the three proposed lipid-binding regions of the human apolipoprotein C-I (apo-C-I) is an amphipathic helix which extends from residue 33 to residue 53 and includes a single methionine at sequence position 38. The involvement of the sequence around methionine-38 in phospholipid binding has been evaluated with paramagnetic and nuclear reported groups attached to the thiomethyl moiety. This moiety has been spin-labeled with N-(2,2,6,6-tetramethylpiperidinyl-1-oxy)bromoacetamide or 13C enriched with 13CH3I. As determined from its EPR spectrum, the nitroxide at Met-38 of apoC-I had a rotational correlation time (tau C) of 0.22 ns. When dimyristoylphosphatidylcholine (DMPC) was bound to the spin-labeled apoprotein, tau c increased to 0.35 ns, indicating decreased motion for the methionyl side chain. The line width (nu 1/2) and spin--lattice relaxation time (T1) for the thiomethyl resonance of 13C-enriched apoC-I in 10 mM phosphate buffer was 6.0 Hz and 320 ms, respectively. When the protein solution was made 1.6 M in Gdn-HCl, these values changed to 2.6 Hz and 970 ms, respectively. Upon addition of DMPC multilamellar liposomes to [13C]apoC-I in 1.6 M Gdn-HCl, the line width increased to 4.7 Hz and the T1 decreased to 380 ms. These results strongly suggest that methionine-38 of apoC-I resides in a region of the apoprotein which undergoes significant secondary and/or tertiary structural change upon disaggregation/unfolding in Gdn-HCl and upon interaction with phospholipid.

Apolipoprotein C-I↗