ArticleMatrix biology : journal of the International Society for Matrix Biology2011
Type XVII collagen (BP180) can function as a cell-matrix adhesion molecule via binding to laminin 332.
Article in Matrix biology : journal of the International Society for Matrix Biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 54 citations in OpenAlex.
- Foot-and-mouth disease virus 3C protease as virulence determinant plays multiple roles in cleaving viral polyprotein and host factors.Virulence · 2026Review
- High-Level Secretory Expression of Recombinant Type XVII Human-like Collagen inInternational journal of molecular sciences · 2026Article
- Essential Role of Integrin-Linked Kinase in Keratinocyte Responses to Mechanical Strain.International journal of molecular sciences · 2026Article
- Hemidesmosome Mutations Contribute to the Onset and Severity of Acquired Autoimmune Bullous Diseases.MedComm · 2026Article
- Ergothioneine, collagen peptides, and sodium hyaluronate ameliorate facial skin aging via modulating oxidative stress, inflammation, and extracellular matrix homeostasis.Frontiers in nutrition · 2026Article
- Collagen XVII Promotes Pancreatic Ductal Adenocarcinoma Tumor Growth through Regulation of PIK3R5.Cancer research communications · 2025Article
- Recombinant human collagen XVII protects skin basement membrane integrity by inhibiting the MAPK and Wnt signaling pathways.Molecular medicine reports · 2025Article
- Case reports of immune-related cystitis and the antibody combination hypothesis.Immunotherapy · 2024Article
- Extracellular matrix in skin diseases: The road to new therapies.Journal of advanced research · 2023Review
- Functional analysis of Collagen 17a1: A genetic modifier of junctional epidermolysis bullosa in mice.PloS one · 2023Article
- Autoimmunity against laminin 332.Frontiers in immunology · 2023Review
- Junctional epithelium and hemidesmosomes: Tape and rivets for solving the "percutaneous device dilemma" in dental and other permanent implants.Bioactive materials · 2022Review
- Foot-and-Mouth Disease Virus 3CViruses · 2022Article
- Tapping basement membrane motifs: Oral junctional epithelium for surface-mediated soft tissue attachment to prevent failure of percutaneous devices.Acta biomaterialia · 2022Article
- Skin Substitute Preparation Method Induces Immunomodulatory Changes in Co-Incubated Cells through Collagen Modification.Pharmaceutics · 2021Article
- The Human Epidermal Basement Membrane: A Shaped and Cell Instructive Platform That Aging Slowly Alters.Biomolecules · 2020Review
- Keratinocyte-Specific Peptide-Based Surfaces for Hemidesmosome Upregulation and Prevention of Bacterial Colonization.ACS biomaterials science & engineering · 2020Article
- Surface Immobilization Chemistry of a Laminin-Derived Peptide Affects Keratinocyte Activity.Coatings (Basel, Switzerland) · 2020Article
- Multiple Skin Squamous Cell Carcinomas in Junctional Epidermolysis Bullosa Due to Altered Laminin-332 Function.International journal of molecular sciences · 2020Article
- High Expression of COL17A1 Predicts Poor Prognosis and Promotes the Tumor Progression via NF-Journal of oncology · 2020Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Collagen XVII (COL17) is a transmembrane glycoprotein that is expressed on the basal surface of basal epidermal keratinocytes. Previous observations have led to the hypothesis that an interaction between COL17 and laminin 332, an extracellular matrix protein, contributes to the attachment of the basal keratinocyte to the basement membrane. In order to isolate and manipulate COL17 interactions with ECM components, we induced COL17 expression in two cells lines, SK-MEL1 and K562, that exhibit little or no capacity to attach to our test substrates, including laminin 332, types I and IV collagen, and fibronectin. Cells expressing high levels of COL17 preferentially adhered to a laminin 332 matrix, and, to a lesser extent, type IV collagen, while showing little or no binding to type I collagen or fibronectin. A quantitative analysis of cell adhesive forces revealed that, compared with COL17-negative cells, COL17-positive cells required over 7-fold greater force to achieve 50% detachment from a laminin 332 substrate. When a cell preparation (either K562 or SK-MEL1) with heterogeneous COL17 expression levels was allowed to attach to a laminin 332 matrix, the COL17-positive and COL17-negative cells differentially sorted to the bound and unbound cell fractions, respectively. COL17-dependent attachment to laminin 332 could be reduced or abolished by siRNA-mediated knock-down of COL17 expression or by adding to the assay wells specific antibodies against COL17 or laminin 332. These findings provide strong support for the hypothesis that cell surface COL17 can interact with laminin 332 and, together, participate in the adherence of a cell to the extracellular matrix.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.