Prolapsus uteri in pelvic supportive disorders are common in elderly women, and their etiology remains unclear. We examined elastin-binding proteins (EBPs) and binding sites in cultured cardinal ligament fibroblasts derived from elderly patients with prolapsus uteri (HPLiF) and compared them with those from age-matched control subjects (HCLiF). Cell attachment to alpha-elastin was significantly lower in HPLiF than in HCLiF. Elastin suppressed the higher proliferative activity at near confluency in HPLiF. The 67-kDa EBP was detectable in HCLiF, whereas HPLiF expressed a 59-kDa EBP. The expression of EBP was significantly lower in HPLiF. The synthetic peptide Val-Gly-Val-Ala-Pro-Gly (VGVAPG), which contains a recognition sequence for the elastin receptor, inhibited the adhesion of HCLiF to alpha-elastin at 10(-5)-10(-4) M, but showed no inhibitory activity on the adhesion of HPLiF at 10(-5) M. These results suggest that fibroblasts derived from elderly women with prolapsus uteri can recognize alpha-elastin through interactions with the low-molecular-size (59-kDa) EBP for the sequence VGVAPG with low affinity and may contribute to the loss of supportive function in uterine connective tissues.
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