title: Polymeric grape-seed procyanidins, but not monomeric catechins and oligomeric procyanidins, impair degranulation and membrane ruffling in RBL-2H3 cells.
abstract: Grape-seed proanthocyanidins (GSPs) are catechin polymers that are predicted to form helices in their global minimum-energy conformation and to have a mean degree of polymerization of seven (mDP = 7). The highly polymerized GSP-H fraction (mDP = 10) was found to impair degranulation in RBL-2H3 cells after stimulation with an antigen (Ag) and treatment with the Ca-ATPase inhibitor thapsigargin (Tg). In addition, GSP-H affected actin cytoskeleton and inhibited membrane ruffling in these cells, resulting in the suppression of exocytosis. By contrast, monomeric epicatechin, the dimeric procyanidins PA-1, PA-2, and PB-2, and the oligomerized GSP-L (mDP = 3) had no effect on membrane ruffling and degranulation. These findings indicate that the molecular size and length of GSP-H are needed for the inhibition of membrane ruffling and degranulation in RBL-2H3 mast-cell lines.
authors.affiliation: Division of Foods, National Institute of Health Sciences, Kamiyoga 1-18-1, Setagaya, Tokyo 158-8501, Japan. kondo@nihs.go.jp
authors.forename: Kazunari
authors.initials: K
authors.lastname: Kondo
authors.forename: Riichiro
authors.initials: R
authors.lastname: Uchida
authors.forename: Shoichi
authors.initials: S
authors.lastname: Tokutake
authors.forename: Tamio
authors.initials: T
authors.lastname: Maitani
mesh_terms: D051339:Actin Depolymerizing Factors / Q000378:metabolism; D000199:Actins / Q000378:metabolism; D000818:Animals; D001704:Biopolymers / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D002392:Catechin / Q000031:analogs & derivatives / Q000737:chemistry / Q000494:pharmacology; D015550:Cell Degranulation / Q000187:drug effects; D002460:Cell Line; D002462:Cell Membrane / Q000187:drug effects / Q000648:ultrastructure; D003599:Cytoskeleton / Q000187:drug effects / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D051417:Focal Adhesion Kinase 1 / Q000378:metabolism; D047908:Intracellular Signaling Peptides and Proteins / Q000378:metabolism; D008407:Mast Cells / Q000187:drug effects* / Q000502:physiology / Q000648:ultrastructure; D051379:Mice; D008807:Mice, Inbred BALB C; D008958:Models, Molecular; D051419:Paxillin / Q000378:metabolism; D051966:Phospholipase C gamma / Q000378:metabolism; D044945:Proanthocyanidins / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D051381:Rats; D017455:Receptors, IgE / Q000378:metabolism; D012639:Seeds / Q000737:chemistry; D015398:Signal Transduction / Q000187:drug effects; D000072377:Syk Kinase; D027843:Vitis / Q000737:chemistry
chemical_list: D051339:Actin Depolymerizing Factors; D000199:Actins; D001704:Biopolymers; D047908:Intracellular Signaling Peptides and Proteins; D051419:Paxillin; D044945:Proanthocyanidins; C496063:Pxn protein, rat; D017455:Receptors, IgE; D002392:Catechin; D011505:Protein-Tyrosine Kinases; D051417:Focal Adhesion Kinase 1; C496052:Ptk2 protein, rat; D000072377:Syk Kinase; C000606897:Syk protein, mouse; C000606898:Syk protein, rat; D051966:Phospholipase C gamma