W Woloszczuk

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Publications (2)10.44 Total impact

  • Article: Plasma atrial natriuretic peptide (ANP) fragments proANP (1-30) and proANP (31-67) measurements in chronic heart failure: a useful index for heart transplantation?
    E Cappellin, R Gatti, P Spinella, C B De Palo, W Woloszczuk, I Maragno, E F De Palo
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    ABSTRACT: The family of the atrial natriuretic peptides, proANP fragments and the active alphaANP, is strongly related to heart disease. The aim was to study in CHF subjects the relation of mdANP and NtANP with brain natriuretic peptide (BNP) and with other traditional medical parameters. Sixteen CHF patients (aged 51.9+/-13.7 years) and 16 healthy subjects age matched (50.8+/-5.9 years) were selected. Both NtANP and mdANP were higher in CHF patients than in healthy subjects (1436+/-288 vs. 288+/-22 pmol/l p<0.001 and 2305+/-383 vs. 423+/-65 pmol/l p<0.0001, respectively). BNP in CHF patients was 28.0+/-9 pmol/l (reference values 1.7+/-1.8 pmol/l). Both NtANP and mdANP demonstrated positive correlation with BNP, p<0.0001 and with left atrial end-systolic volume, p<0.05. BNP correlated with left ventricular mass, p<0.03. In conclusion, plasma NtANP and mdANP analyses are useful laboratory markers in CHF patient investigation and follow up. In particular, they could be employed as non-invasive parameters to follow up worsening of systolic dysfunction until heart transplantation is required.
    Clinica Chimica Acta 09/2001; 310(1):49-52. · 2.54 Impact Factor
  • Article: Circulating immunoreactive proANP(1-30) and proANP(31-67) in sedentary subjects and athletes.
    E F De Palo, W Woloszczuk, M Meneghetti, C B De Palo, H B Nielsen, N H Secher
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    ABSTRACT: Atrial natriuretic peptide (ANP) is synthesized and stored in myocytes as prohormone(1-126), which upon release is cleaved into proANP(1-98) and alpha-ANP(99-126). In addition, cleavage of proANP(1-98) produces proANP(1-30), proANP(31-67), and proANP(79-98) fragments. ProANP(1-30) and proANP(31-67) have roles in fluid and electrolyte homeostasis. The aim of the present study was to develop a plasma assay for proANP(1-30) and proANP(31-67) and to compare results in trained athletes and sedentary subjects. Two competitive enzyme immunoassays were established with affinity-purified sheep antiserum against synthetic ANP fragments. The immunoreactivity (ir) of proANP(1-30) and proANP(31-67) was measured in 10-microL plasma samples without extraction in a microwell-based assay. Plasma concentrations in sedentary male subjects (n = 22) and male endurance athletes (n = 14) were examined. In the assay for ir-proANP(1-30) and ir-proANP(31-67), the concentrations at 95% B/B(0) were 4.7 and 14.2 pmol/L, respectively. Within-run CVs were 4-6% and 5-6%, and between-run CVs were 9% for both assays. Both assays were linear on dilution (y = 0.9945x - 0. 7291 and y = 1.0001x - 3.428), and the recoveries were 102-112% and 102-106%, respectively. In the sedentary and athletic groups, the ir-proANP(1-30) concentrations were similar: 318 +/- 38 pmol/L and 312 +/- 25 pmol/L (mean +/- SE), respectively, whereas the ir-proANP(31-67) was higher in the rowers (713 +/- 81 pmol/L) than in the sedentary subjects (387 +/- 71 pmol/L; P <0.005). The proANP fragment assays are precise (CV <10%) and exhibit nearly quantitative recovery (102-112%). Only ir-proANP(31-67) responds to physical training.
    Clinical Chemistry 07/2000; 46(6 Pt 1):843-7. · 7.91 Impact Factor
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