title: Changes in elastin-binding protein in fibroblasts derived from cardinal ligaments of patients with prolapsus uteri.
abstract: 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.
authors.affiliation: Department of Cell Biology, Tokyo Metropolitan Institute of Gerontology, 35-2 Sakae-cho, Itabashi-ku, Tokyo, 173-0015, Japan.
authors.forename: Mari
authors.initials: M
authors.lastname: Yamamoto
authors.forename: Kenji
authors.initials: K
authors.lastname: Akazawa
authors.forename: Masaru
authors.initials: M
authors.lastname: Aoyagi
authors.forename: Naofumi
authors.initials: N
authors.lastname: Yamamoto
authors.forename: Kiyotaka
authors.initials: K
authors.lastname: Yamamoto
mesh_terms: D001665:Binding Sites; D002448:Cell Adhesion; D002455:Cell Division; D002478:Cells, Cultured; D024042:Collagen Type I / Q000378:metabolism; D024061:Collagen Type III / Q000378:metabolism; D003240:Connective Tissue Diseases / Q000378:metabolism*; D004549:Elastin / Q000378:metabolism; D005109:Extracellular Matrix / Q000378:metabolism; D005260:Female; D005347:Fibroblasts / Q000166:cytology / Q000378:metabolism / Q000502:physiology; D006801:Humans; D008022:Ligaments / Q000166:cytology; D010388:Pelvis / Q000002:abnormalities*; D011956:Receptors, Cell Surface / Q000378:metabolism*
chemical_list: D024042:Collagen Type I; D024061:Collagen Type III; D011956:Receptors, Cell Surface; C054901:elastin-binding proteins; D004549:Elastin