Changes in elastin-binding protein in fibroblasts derived from cardinal ligaments of patients with prolapsus uteri

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.