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          Institute: MPI für Biochemie     Collection: Molecular Medicine (R. Fässler)     Display Documents



ID: 35295.0, MPI für Biochemie / Molecular Medicine (R. Fässler)
Defective laminin 5 processing in cylindroma cells
Authors:Tunggal, L.; Ravaux, J.; Pesch, M.; Smola, H.; Krieg, T.; Gaill, F.; Sasaki, T.; Timpl, R.; Mauch, C.; Aumailley, M.
Language:English
Date of Publication (YYYY-MM-DD):2002-02
Title of Journal:American Journal of Pathology
Journal Abbrev.:Am. J. Pathol.
Volume:160
Issue / Number:2
Start Page:459
End Page:468
Review Status:Peer-review
Audience:Not Specified
Abstract / Description:Cylindromas are benign skin tumors occurring as multiple nodules characteristically well circumscribed by an excess of basement membrane-like material. To determine the molecular defects leading to extracellular matrix accumulation, the ultrastructural, immunological, and biochemical properties of cylindroma tissue and isolated cells were analyzed. In cylindromas, hemidesmosomes are reduced in number, heterogeneous and immature compared to the normal dermal- epidermal junction. Expression of the alpha6beta4 integrin in tumor cells is weaker than in basal keratinocytes of the epidermis. Moreover, although in the epidermis alpha2beta1- integrin expression is restricted to the basal cell layer, it is found in all neoplastic cells within the nodules. Laminin 5 is present throughout the whole thickness of the basement membrane-like zone whereas laminin 10 is restricted to the interface adjacent to the tumor cells. Furthermore, laminin 5 is not properly processed and most of the alpha3A and gamma2 laminin chains remain as 165-kd and 155-kd polypeptides, respectively. Mature laminin 5 is thought to be necessary for correct hemidesmosome and basement membrane formation and its abnormal processing, as well as the low expression of alpha6beta4 integrins, could explain the lack of mature hemidesmosomes. Together, the results show that multiple molecular defects, including alteration of laminin 5 and its integrin receptors, contribute to structural aberrations of the basement membrane and associated structures in cylindromas.
Comment of the Author/Creator:Date: 2002, FEB
External Publication Status:published
Document Type:Article
Communicated by:N.N.
Affiliations:MPI für Biochemie/Emeriti Groups/Protein Chemistry (R. Timpl)
MPI für Biochemie/Molecular Medicine (R. Fässler)/Extracellular Matrix Proteins (T. Sasaki)
External Affiliations:Univ Cologne, Inst Biochem 2, Joseph Steizmann Str 52, D-50931; Cologne, Germany; Univ Cologne, Inst Biochem 2, D-50931 Cologne, Germany; Univ Cologne, Fac Med, Dept Dermatol, D-50931 Cologne, Germany; Univ Paris 06, Marine Biol Lab, Paris, France
Identifiers:ISI:000173733500010 [ID No:1]
ISSN:0002-9440 [ID No:2]
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