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Evidence for cardiovascular remodeling in a patient with Bartter's syndrome (1994)

Schmitz, U. ; Ko, Y. ; Becher, H. ; [et al.]

Springer

Journal of molecular medicine 72 (1994), S. 874-877

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ISSN: 1432-1440

Keywords: Bartter's syndrome ; Cardiovascular remodeling ; Diastolic dysfunction ; Intima/media complex

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine

Notes: Abstract In a 56-year-old normotensive white male subject with a 12-year history of hypokalemic alkalosis, hyperreninemia, and aldosteronism, the diagnosis of Bartter's syndrome was established on the basis of an impaired maximal renal diluting capacity and decreased distal fractional chloride absorption [CH2O/(CH2O + CCl)]. Negative urine analysis for diuretics suggested that this renal tubular defect was not secondary to diuretic (ab)use. In this normotensive patient with hyperreninemia and secondary aldosteronism, significant cardiovascular remodeling could be observed. Thus, in spite of normal arterial blood pressure and normal left ventricular systolic function (ejection fraction 〉 70%), impaired left ventricular diastolic function was observed using pulsed-wave Doppler echocardiography. Moreover, duplex analysis of the common carotid artery revealed significant intima-media hypertrophy with an average intima-media diameter of 0.9 mm (normal ≤ 0.6 mm). Also, forearm venous occlusion plethysmography revealed an abnormally high minimal forearm vascular resistance following a 10-min period of forearm ischemia handgrip exercise suggesting remodeling within the peripheral arterioles. Thus, in a patient with Bartter's syndrome and activated neurohormonal systems such as the renin-angiotensin system, cardiac and vascular remodeling can be observed in the absence of hypertension. In analogy to the results of experimental studies showing that angiotensin II and noradrenaline act as growth factors on cardiac and vascular cells, cardiovascular remodeling present in our patient with Bartter's syndrome may be explained by increased activity of angiotensin II and/or noradrenaline.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00190744

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Electrophoretic purification of the alpha and beta subunits of phosphorylase kinase and evidence in support of the deduced amino acid sequences (1990)

Crabb, John W. ; Harris, William R. ; Johnson, Charles M. ; [et al.]

Weinheim : Wiley-Blackwell

Electrophoresis 11 (1990), S. 133-140

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ISSN: 0173-0835

Keywords: Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology

Notes: A simple, rapid sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) method is presented for isolating the α, α' and β subunits of rabbit muscle phosphorylase kinase. The SDS-PAGE procedure can yield milligram amounts of α and β from a single preparative gel and also allows isolation of the α' isozyme free of α. Notably the method provides the purified subunits in a form amenable to structural analysis. Edman degradation of α and α' reveal identical NH2-terminal structures. Amino acid analysis of the electrophoretically purified α and β subunits are in good agreement with their deduced primary structures. The amino acid sequence of 488 residues in α and 713 residues in β were determined by gas phase Edman degradation. The data support the recently deduced primary structures of α (Zander et al., Proc. Natl. Acad. Sci. USA 1988, 85, 2929-2933) and of β (Kilimann et al., Proc. Natl. Acad. Sci. USA, 1988, 85, 9381-9385).

Additional Material: 7 Ill.