Collagen heterogeneity in pig heart valves

Mannschott, Philippe; Herbage, D.; Weiss, Michel; Buffevant, Chantal

doi:10.1016/0005-2795(76)90048-9

Cited by 12 publications

(6 citation statements)

References 9 publications

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“…There has been significant controversy in the literature about the types of collagen present in the heart valves. For example, type-III collagen in heart valve was previously shown by Mannschott et al (1976). Collins et al (1975), on the other hand, suggested the exclusive presence of type-I collagen in this tissue, and Morris & McClain (1972) showed similarities in some CNBr peptides between valvular collagen and collagen from cartilage.…”

Section: Discussionmentioning

confidence: 82%

“…173 in the present study. The conditions of pepsin extraction may also contribute to the differences, since our extraction was carried out at 15°C, whereas it was performed at 20°C by Mannschott et al (1976). Photograph of Coomassie Blue-stained gels of collagens from mitral valve All gels were obtained under non-reducing conditions, except for gel 3, which was obtained in the presence of 0.1°.…”

Section: Discussionmentioning

confidence: 99%

“…Identification of the collagen types present in heart valves has yielded conflicting results . Mannschott et al (1976) characterized the collagens extracted by limited pepsin digestion of pig heart valves, and showed the presence of both type-I and -III collagens in these extracts.…”

mentioning

confidence: 99%

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Characterization of pepsin-solubilized bovine heart-valve collagen

Bashey¹,

Bashey²,

Jimenez³

1978

Biochemical Journal

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Collagens extracted from heart valves by using limited pepsin digestion were fractionated by differential salt precipitation. Collagen types were identified by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, amino acid analysis and cleavage with CNBr. Heart-valve collagen was heterogeneous in nature, consisting of a mixture of type-I and type-III collagens. The identity of type-III collagen was established on the basis of (a) insolubility in 1.7 M-NaC1 at neutral pH, (b) behaviour of this collagen fraction on gel electrophoresis under reducing and non-reducing conditions, (c) amino acid analysis showing a hydroxyproline/proline ratio greater than 1, and (d) profile of CNBr peptides on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis showing a peak characteristic for type-III collagen containing peptides alpha1(III)CB8 and alpha1(III)CB3. In addition to types-I and -III collagen, a collagen polypeptide not previously described in heart valves was identified. This polypeptide represented approx. 30% of the collagen fraction precipitated at 4.0 M-NaCl, it migrated between beta- and alpha1-collagen chains on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and its electrophoretic behaviour was not affected by disulphide-bond reduction. All collagen fractions from the heart valves contained increased amounts of hydroxylysine when compared with type-I and -III collagens from other tissues. The presence of beta- and gamma-chains and higher aggregates in pepsin-solubilized collagen indicated that these collagens were highly cross-linked and suggested that some of these cross-links involved the triple-helical regions of the molecule. It is likely that the higher hydroxylysine content of heart-valve collagen is responsible for the high degree of intermolecular cross-linking and may be the result of an adaptive mechanism for the specialized function of these tissues.

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Section: Discussionmentioning

confidence: 82%

Section: Discussionmentioning

confidence: 99%

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Characterization of pepsin-solubilized bovine heart-valve collagen

Bashey¹,

Bashey²,

Jimenez³

1978

Biochemical Journal

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“…O principal colágeno presente na valva aórtica é o do tipo I, composto por duas cadeias distintas de polipeptídeos, a α1 (I) e a α2 (I). Também está presente o colágeno tipo III, composto de três cadeias α1 (BASHEY, et al, 1978;MANNSCHOTT, et al, 1976;. As fibras do colágeno funcionam como pontes de união dos folhetos valvares às paredes da aorta, comportando-se como cabos de uma suspensão, transmitindo as forças impostas aos folhetos, pelo retorno do sangue, à parede da aorta durante a diástole .…”

Section: Longitudinalunclassified

“…O colágeno compõe cerca de 50% do peso seco do folheto valvar, enquanto a elastina representa cerca de 13% (Bashey et al, 1967). O colágeno tipo I, encontrado principalmente em tendão, osso e pele é o mais abundante na valva, mas também está presente o colágeno tipo III (Mannschott, et al, 1976;Bashey, et al, 1978; comumente encontrado em pele, vasos, membranas fetais e órgãos hemocitopoiéticos. A presença de fibras elásticas permite à valva sofrer distensão durante a abertura dos folhetos .…”

Section: Documentação Fotográficaunclassified

Estudo estrutural e bioquimico do tecido conjuntivo da valva aortica de porco

Mazon¹,

Pimentel²

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Inhibition of aortic wall calcification in bioprosthetic heart valves by ethanol pretreatment: Biochemical and biophysical mechanisms

Lee

Vyavahare

Zand

et al. 1998

J. Biomed. Mater. Res.

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The effectiveness of ethanol pretreatment on preventing calcification of glutaraldehyde-fixed porcine aortic bioprosthetic heart valve (BPHV) cusps was previously demonstrated, and the mechanism of action of ethanol was attributed in part to both lipid removal and a specific collagen conformational change. In the present work, the effect of ethanol pretreatment on BPHV aortic wall calcification was investigated using both rat subdermal and sheep circulatory implants. Ethanol pretreatment significantly inhibited calcification of BPHV aortic wall, but with less than complete inhibition. The maximum inhibition of calcification of BPHV aortic wall was achieved using an 80% ethanol pretreatment; calcium levels were 71.80+/-8.45 microg/mg with 80% ethanol pretreatment compared to the control calcium level of 129.90+/-7.24 microg/mg (p = 0.001). Increasing the duration of ethanol exposure did not significantly improve the inhibitory effect of ethanol on aortic wall calcification. In the sheep circulatory implants, ethanol pretreatment partly prevented BPHV aortic wall calcification with a calcium level of 28.02+/-4.42 microg/mg compared to the control calcium level of 56.35+/-6.14 microg/mg (p = 0.004). Infrared spectroscopy (ATR-FTIR) studies of ethanol-pretreated BPHV aortic wall (vs. control) demonstrated a significant change in protein structure due to ethanol pretreatment. The water content of the aortic wall tissue and the spin-lattice relaxation times (T1) as assessed by proton nuclear magnetic resonance spectroscopy did not change significantly owing to ethanol pretreatment. The optimum condition of 80% ethanol pretreatment almost completely extracted both phospholipids and cholesterol from the aortic wall; despite this, significant calcification occurred. In conclusion, these results clearly demonstrate that ethanol pretreatment is significantly but only partially effective for inhibition of calcification of BPHV aortic wall and this effect may be due in part to lipid extraction and protein structure changes caused by ethanol. It is hypothesized that ethanol pretreatment may be of benefit for preventing bioprosthetic aortic wall calcification only in synergistic combination with another agent.

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Collagen heterogeneity in pig heart valves

Cited by 12 publications

References 9 publications

Characterization of pepsin-solubilized bovine heart-valve collagen

Characterization of pepsin-solubilized bovine heart-valve collagen

Estudo estrutural e bioquimico do tecido conjuntivo da valva aortica de porco

Inhibition of aortic wall calcification in bioprosthetic heart valves by ethanol pretreatment: Biochemical and biophysical mechanisms

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