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Updated: Jun 7, 2026
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Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
Published on: September 28, 2020
Type XVII collagen (BP180) can function as a cell-matrix adhesion molecule via binding to laminin 332
F Van den Bergh1, S L Eliason, G J Giudice
1Department of Medicine, Division of Rheumatology, Medical College of Wisconsin, Milwaukee, USA.
Summary
Collagen XVII (COL17), a cell surface protein, enhances keratinocyte attachment to laminin 332. This interaction is crucial for cell adhesion to the extracellular matrix, supported by increased cell binding forces.
Area of Science:
- Cell Biology
- Biochemistry
- Dermatology
Background:
- Collagen XVII (COL17) is a transmembrane glycoprotein found on basal epidermal keratinocytes.
- Prior research suggests COL17 interacts with laminin 332 (an extracellular matrix protein) to anchor basal keratinocytes to the basement membrane.
Purpose of the Study:
- To investigate the interaction between Collagen XVII (COL17) and extracellular matrix (ECM) components.
- To determine COL17's role in cell adhesion to substrates like laminin 332.
Main Methods:
- Induced COL17 expression in SK-MEL1 and K562 cell lines.
- Assessed cell adhesion to various ECM proteins (laminin 332, collagen types I and IV, fibronectin).
- Quantified cell adhesive forces and utilized siRNA for COL17 knock-down.
Main Results:
- COL17-expressing cells showed preferential adhesion to laminin 332 and, to a lesser extent, type IV collagen.
- Adhesive forces for COL17-positive cells were over 7-fold greater on laminin 332 compared to COL17-negative cells.
- COL17-dependent attachment to laminin 332 was reduced by COL17 knock-down or specific antibodies.
Conclusions:
- Cell surface COL17 interacts with laminin 332, significantly contributing to cell adherence to the extracellular matrix.
- This interaction plays a vital role in basal keratinocyte attachment to the basement membrane.
- Findings validate the hypothesis of COL17-laminin 332 mediated cell adhesion.
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