Endogenous natriuretic factors 1: sodium pump inhibition does not correlate with natriuretic or pressor activities from uremic urine
| Autor: | Rita Giebel, A. E. Bigornia, Tim Pham, Cynthia L. Rodgers, Elaine J. Benaksas, E. David Murray, Elaine S. Brubacher, Sally A. Dewind, William J. Wechter |
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| Rok vydání: | 1993 |
| Předmět: |
medicine.medical_specialty
Natriuresis Endogeny Blood Pressure Kidney General Biochemistry Genetics and Molecular Biology Cell Line Rats Sprague-Dawley Internal medicine medicine Animals Humans General Pharmacology Toxicology and Pharmaceutics Na+/K+-ATPase Chromatography High Pressure Liquid Uremia Chemistry Tissue Extracts Biological activity General Medicine medicine.disease Rats Ultrafiltration (renal) medicine.anatomical_structure Endocrinology Kidney Failure Chronic Cattle Female Sodium-Potassium-Exchanging ATPase Homeostasis |
| Zdroj: | Life sciences. 52(12) |
| ISSN: | 0024-3205 |
| Popis: | It is our purpose to isolate and characterize the putative “Natriuretic Hormone”, ostensibly responsible for ECF homeostasis, as well as identify endonenous pressors and compounds that induce prolonged natriuresis; we report here our initial progress in this area. Large volumes of pooled urine collected from uremic patients were fractionated, and the resulting isolates were evaluated for in vivo natriuretic and pressor effects and Na+/K+-ATPase inhibitory activity in renal cells. The purification steps involved ultrafiltration to obtain materials of less than 3000 da, gel filtration, and sequential reversed-phase high performance liquid chromatography (HPLC). After each HPLC step, the fractions were evaluated for their ability to elicit significant natriuresis and/or influence mean arterial pressure in the normal conscious female rat. Each fraction was also assayed for its ability to inhibit Na+/K+-ATPase as determined by the inhibition of 86Rb+ uptake into MDBK renal cells. While several of the fractions elicited profound natriuresis and/or pressor activity and other fractions inhibited Na+/K+-ATPase, there was no correlation among the activities in individual fractions. We have concluded that this plethora of bioactivities is responsible for much of the confusion and multiplicity of crude isolates claimed to be the putative hormone. Presently we are attempting to purify each of these activities to chemical homogeneity for structure determination. |
| Databáze: | OpenAIRE |
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