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P A Nejezchleb

Publications and source records attributed to P A Nejezchleb.

2 recordsLinked to original sources

Elastin is increased in abdominal aortic aneurysms.

The decrease in elastin concentration in abdominal aortic aneurysm (AAA) has been ascribed to elastolysis. The discordant response of the elastin and collagen genes in AAA suggests a different explanation: dilution of elastin because of higher levels of synthesis of collagen and other matrix proteins. The purpose of this study was to determine circumferential content of elastin, collagen, and total protein in aneurysmal (AAA), atherosclerotic, and normal (NL) infrarenal aorta. Standard serial extraction techniques of complete 1-cm rings of midinfrarenal aortic tissue were used to remove soluble protein, calcium, and lipids. Hydroxyproline (collagen), desmosine/isodesmosine (elastin), and total amino acid (total protein) content were determined by amino acid analysis. Means values (+/- SEM) were compared by ANOVA. Circumferential content of desmosine/isodesmosine was increased 2.5-fold in AAA compared to NL (P < 0.05). Collagen and total protein were increased 5.7- and 4.7-fold, respectively (P < 0.05). There was a high degree of correlation between circumference and collagen content (r = 0.89). These data demonstrate that significant synthesis of matrix proteins accompanies aortic dilatation. While both elastin and collagen are increased, there is a much greater increase in circumferential collagen content than elastin content. These data do not preclude proteolysis as a factor in AAA but suggest that the decrease in elastin concentration results from dilution of elastin by a greater increase in the synthesis of other matrix proteins and that synthesis is an important factor in AAA formation.

Adult

Elastin and fibrillin mRNA and protein levels in the ontogeny of normal human aorta.

Elastin associated microfibrils (EAMF) are ubiquitous connective tissue structures that are believed to provide tensile strength and flexibility to numerous tissues. In this study the ontogeny of EAMF in normal human aorta was examined using immunohistochemical analysis of fibrillin, an EAMF component, and mRNA levels of fibrillin and elastin. Specimens of infra-renal aorta from ages 11 months to 44 years were obtained following organ procurement. Decreasing amounts, as judged by computer digitized image analysis, of immunoreactive fibrillin when compared to elastin auto-fluorescence were observed in aortic sections with increasing age. Elastase treatment would un-mask the anti-fibrillin reactive epitope reinforcing the suggestion that EAMF act as a "scaffold" for elastin deposition. Northern and dot blot hybridizations demonstrated a decrease in relative fibrillin message levels with increasing age. The abundance of fibrillin in relation to elastin may suggest a role for EAMF independent of their association with elastin.

Actin Cytoskeleton