title: Structural and compositional analysis of the keratinocyte migration track.
abstract: Slowly migrating cells such as fibroblasts leave behind a "migration track," which has been assumed not to occur in fast-moving cells such as keratinocytes. Here we show that keratinocytes left behind "migration tracks" of cellular remnants consisting of membranous patches or macroaggregates that were anchored to a meshwork of extracellular matrix proteins consisting of collagen type IV, fibronectin, laminin, and laminin 5. According to their origin and localisation, two types of macroaggregates could be distinguished : (1) Spherical and elongated tubular structures (diameter about 50-110 nm) both of which were arranged like "pearls on a string" and that apparently derived from fragmentation of retracting fibres. (2) Spherical structures (diameter about 50 nm) left behind in the gaps between the retracting fibres and presumably derived from former focal adhesion sites. Both types of macroaggregates did not contain cytoplasmic proteins but carried on their surface adhesion proteins, particularly high amounts of integrins : type 1 macroaggregates contained alpha3beta1-integrins, whereas type 2 macroaggregates contained other types of integrins such as alpha6beta4-integrins. Modulation of keratinocyte adhesion by using poly-L-lysine coated cover slips resulted in an increased application of inhibitory beta1-antibodies and slightly reduced migration velocity and track formation. Within 24 h of migration, we observed a migration velocity-dependent loss of cellular beta1-integrin by macroaggregate formation of about 11% for fast and about 4% for slowly migrating keratinocytes. The physiological role of the migration track is unclear. However, with its multiple adhesion sites it may serve as a provisional basement membrane during reepithelialization of epidermal wounds.
authors.affiliation: Institute of Cell Biology, University of Bonn, Ulrich-Haberlandstrasse 61a, 53121 Bonn, Germany. g.kirfel@uni-bonn.de
authors.forename: Gregor
authors.initials: G
authors.lastname: Kirfel
authors.forename: Alexander
authors.initials: A
authors.lastname: Rigort
authors.forename: Bodo
authors.initials: B
authors.lastname: Borm
authors.forename: Carsten
authors.initials: C
authors.lastname: Schulte
authors.forename: Volker
authors.initials: V
authors.lastname: Herzog
mesh_terms: D016564:Amyloid beta-Protein Precursor / Q000378:metabolism; D000906:Antibodies / Q000494:pharmacology; D001485:Basement Membrane / Q000378:metabolism / Q000648:ultrastructure; D002448:Cell Adhesion / Q000502:physiology*; D002465:Cell Movement / Q000502:physiology*; D002478:Cells, Cultured; D003598:Cytoskeletal Proteins / Q000378:metabolism / Q000648:ultrastructure; D005109:Extracellular Matrix / Q000378:metabolism* / Q000648:ultrastructure; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D006801:Humans; D007231:Infant, Newborn; D019012:Integrin beta1 / Q000187:drug effects / Q000378:metabolism; D015603:Keratinocytes / Q000378:metabolism* / Q000648:ultrastructure; D007797:Laminin / Q000378:metabolism; D008854:Microscopy, Electron; D014945:Wound Healing / Q000502:physiology
chemical_list: D016564:Amyloid beta-Protein Precursor; D000906:Antibodies; D003598:Cytoskeletal Proteins; D016326:Extracellular Matrix Proteins; D019012:Integrin beta1; D007797:Laminin