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1.
Am J Physiol ; 254(5 Pt 2): F634-41, 1988 May.
Article in English | MEDLINE | ID: mdl-3364574

ABSTRACT

The ontogeny of the renal response to continuous systemic infusion of atrial natriuretic peptide (ANP) was studied in chronically instrumented fetal, newborn, and adult nonpregnant sheep. Plasma immunoreactive ANP (ANPir) concentrations during low (0.025 microgram.kg-1.min-1) and high rate (0.1 microgram.kg-1.min-1) ANP infusion were similar between each group of animals. Decrease in renal blood flow velocity (RBFV) and rise in renal vascular resistance (RVR) were observed in fetal and newborn lambs during ANP infusion. The percent changes in RBFV and RVR were of significantly (P less than 0.05) greater magnitude during high ANP infusion rate in fetuses (-28.5 +/- 8.5 and 93 +/- 6.4%) than in adult sheep (-6.6 +/- 3.2 and -4.4 +/- 4.9%). ANP produced no changes in urine flow (V) in fetuses but increased V significantly in newborn lambs and adult sheep. Glomerular filtration rate increased significantly during ANP infusion in adult sheep but not in fetal and newborn lambs. Percentage changes in urinary excretion rate of Na (UNaV) during high ANP infusion rate were significantly higher in adult sheep (3,520 +/- 2,414%) than in newborn (157 +/- 106%) and fetal lambs (198 +/- 84%). These results suggest that the cardiovascular, renal hemodynamic, and possibly renal function responses to continuous ANP infusion increase during maturation, the overall response being larger in adult animals.


Subject(s)
Homeostasis , Kidney Glomerulus/physiology , Kidney Tubules/physiology , Prostaglandins/physiology , Animals , Imidazoles/pharmacology , Indomethacin/pharmacology , Male , Masoprocol/pharmacology , Piroxicam/pharmacology , Prostaglandins, Synthetic/pharmacology , Rats , Rats, Inbred Strains , Thromboxane A2/antagonists & inhibitors
2.
Biochemistry ; 24(27): 8070-4, 1985 Dec 31.
Article in English | MEDLINE | ID: mdl-4092056

ABSTRACT

Glia maturation factor (GMF) is purified 100 000-fold to apparent homogeneity from bovine brains by a procedure consisting of ammonium sulfate precipitation, column chromatography with diethylaminoethyl-Sephacel, Sephadex G-75, and hydroxylapatite, and a final step using C4 reverse-phase high-performance liquid chromatography. The product shows a single protein band in sodium dodecyl sulfate-polyacrylamide gel. It has a molecular weight of 14 000 and an isoelectric point of pH 5.2. Purified GMF stimulates cultured astroblasts to proliferate and to grow out cell processes with half-maximal activity at 8 ng/mL. A monoclonal antibody raised against partially purified GMF adsorbs the activity of pure GMF and immunologically binds the putative GMF protein band.


Subject(s)
Growth Substances/isolation & purification , Nerve Tissue Proteins/isolation & purification , Amino Acids/analysis , Animals , Antibodies, Monoclonal , Brain Chemistry , Cattle , Chromatography, High Pressure Liquid , Electrophoresis, Polyacrylamide Gel , Enzyme-Linked Immunosorbent Assay , Glia Maturation Factor , Mice , Mice, Inbred BALB C , Molecular Weight , Nerve Tissue Proteins/immunology
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