title: Basement membrane protein distribution in LYVE-1-immunoreactive lymphatic vessels of normal tissues and ovarian carcinomas.
abstract: The endothelial cells of blood vessels assemble basement membranes that play a role in vessel formation, maintenance and function, and in the migration of inflammatory cells. However, little is known about the distribution of basement membrane constituents in lymphatic vessels. We studied the distribution of basement membrane proteins in lymphatic vessels of normal human skin, digestive tract, ovary and, as an example of tumours with abundant lymphatics, ovarian carcinomas. Basement membrane proteins were localized by immunohistochemistry with monoclonal antibodies, whereas lymphatic capillaries were detected with antibodies to the lymphatic vessel endothelial hyaluronan receptor-1, LYVE-1. In skin and ovary, fibrillar immunoreactivity for the laminin alpha4, beta1, beta2 and gamma1 chains, type IV and XVIII collagens and nidogen-1 was found in the basement membrane region of the lymphatic endothelium, whereas also heterogeneous reactivity for the laminin alpha5 chain was detected in the digestive tract. Among ovarian carcinomas, intratumoural lymphatic vessels were found especially in endometrioid carcinomas. In addition to the laminin alpha4, beta1, beta2 and gamma1 chains, type IV and XVIII collagens and nidogen-1, carcinoma lymphatics showed immunoreactivity for the laminin alpha5 chain and Lutheran glycoprotein, a receptor for the laminin alpha5 chain. In normal lymphatic capillaries, the presence of primarily alpha4 chain laminins may therefore compromise the formation of endothelial basement membrane, as these truncated laminins lack one of the three arms required for efficient network assembly. The localization of basement membrane proteins adjacent to lymphatic endothelia suggests a role for these proteins in lymphatic vessels. The distribution of the laminin alpha5 chain and Lutheran glycoprotein proposes a difference between normal and carcinoma lymphatic capillaries.
authors.affiliation: Institute of Biomedicine/Anatomy, University of Helsinki, Haartmaninkatu 8, FI-00014, Helsinki, Finland. noora.vainionpaa@helsinki.fi
authors.forename: Noora
authors.initials: N
authors.lastname: Vainionpää
authors.forename: Ralf
authors.initials: R
authors.lastname: Bützow
authors.forename: Mika
authors.initials: M
authors.lastname: Hukkanen
authors.forename: David G
authors.initials: DG
authors.lastname: Jackson
authors.forename: Taina
authors.initials: T
authors.lastname: Pihlajaniemi
authors.forename: Lynn Y
authors.initials: LY
authors.lastname: Sakai
authors.forename: Ismo
authors.initials: I
authors.lastname: Virtanen
mesh_terms: D000328:Adult; D001485:Basement Membrane / Q000378:metabolism*; D015815:Cell Adhesion Molecules / Q000378:metabolism; D005260:Female; D041981:Gastrointestinal Tract / Q000166:cytology / Q000378:metabolism; D006801:Humans; D008188:Lutheran Blood-Group System; D042601:Lymphatic Vessels / Q000166:cytology / Q000378:metabolism* / Q000473:pathology; D008565:Membrane Proteins / Q000378:metabolism*; D009363:Neoplasm Proteins / Q000378:metabolism; D010051:Ovarian Neoplasms / Q000378:metabolism*; D010053:Ovary / Q000166:cytology / Q000378:metabolism / Q000473:pathology; D012867:Skin / Q000166:cytology / Q000378:metabolism; D033921:Vesicular Transport Proteins / Q000032:analysis* / Q000276:immunology*
chemical_list: C090228:BCAM protein, human; D015815:Cell Adhesion Molecules; C119248:LYVE1 protein, human; D008188:Lutheran Blood-Group System; D008565:Membrane Proteins; D009363:Neoplasm Proteins; D033921:Vesicular Transport Proteins