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Updated: Aug 29, 2026

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve
Published on: June 14, 2017
Fibrillin and other matrix proteins in mitral valve prolapse syndrome
Joseph F Nasuti1, Paul J Zhang, Michael D Feldman
1Hospital of University of Pennsylvania, Philadelphia, PA, USA.
Background:
Unlike myxomatous degeneration in Marfan syndrome, which has been reported to result from a mutation in the gene that codes for the extracellular structural protein fibrillin, no specific molecular abnormality has been documented to be the underlying cause of myxomatous degeneration in mitral valve prolapse syndrome (MVPS). The present study examined the distribution of fibrillin and other extracellular matrix proteins in patients with isolated MVPS.
Methods:
Mitral valve leaflets from 7 MVPS patients and 5 rheumatic heart disease (RHD) patients were characterized immunohistochemically for fibrillin, elastin, collagen I, and collagen III distribution, and compared with five normal mitral valves.
Results:
In normal mitral valve leaflets immunostaining for fibrillin, elastin, collagen I, and collagen III revealed a fibrillary and laminar pattern in the atrialis and the spongiosa. In addition, both the collagens were present in the ventricularis, and the coarse bundles in the fibrosa exhibited alternating bandlike collagen I immunoreactivity. The staining patterns of fibrillin, elastin, and collagens I and III revealed distinctly different distribution in MVPS relative to the normal and RHD leaflets. MVPS leaflets in areas of myxoid degeneration displayed a more diffuse, weaker, and nonlaminar pattern of staining for fibrillin. Similar, but less severe abnormality of elastin, collagen I, and collagen III was also observed. Unlike diffuse abnormality in MVPS, the disruption of extracellular proteins in RHD only occurred at the site of the inflammatory damage, but the overall architecture was preserved.
Conclusions:
The results of the current study suggest a primary role for abnormal fibrillin and other matrix proteins in producing myxoid degeneration of mitral valve leaflets in MVPS.
Insights
Abnormalities in fibrillin and other matrix proteins likely cause myxomatous degeneration in mitral valve prolapse syndrome (MVPS). This study found distinct extracellular matrix protein distribution differences in MVPS leaflets compared to normal and rheumatic heart disease valves.
Area of Science:
- Cardiovascular Biology
- Extracellular Matrix Research
- Molecular Pathology
Background:
- Myxomatous degeneration in Marfan syndrome is linked to fibrillin gene mutations.
- The molecular cause of myxomatous degeneration in mitral valve prolapse syndrome (MVPS) remains unclear.
- This study investigates extracellular matrix protein distribution in isolated MVPS.
Purpose of the Study:
- To examine the distribution of fibrillin and other extracellular matrix proteins in mitral valve leaflets from patients with isolated MVPS.
- To compare these distributions with those in normal mitral valves and valves affected by rheumatic heart disease (RHD).
Main Methods:
- Immunohistochemical analysis of mitral valve leaflets from 7 MVPS patients, 5 RHD patients, and 5 normal controls.
- Characterization of fibrillin, elastin, collagen I, and collagen III distribution.
Main Results:
- Normal valves show a laminar pattern of fibrillin, elastin, and collagens.
- MVPS leaflets with myxoid degeneration exhibit diffuse, weaker, and nonlaminar staining for fibrillin and other matrix proteins.
- RHD valves show localized disruption of extracellular proteins, preserving overall architecture, unlike the diffuse changes in MVPS.
Conclusions:
- Abnormalities in fibrillin and other extracellular matrix proteins play a primary role in myxoid degeneration of mitral valve leaflets in MVPS.
- These findings highlight a distinct molecular basis for MVPS compared to other valvular diseases.
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