Chapter, 2024

Chapter 19 Type XIX collagen

Biochemistry of Collagens, Laminins and Elastin 9780443156175, Pages 175-179

Editors:

Publisher: Elsevier

DOI: 10.1016/b978-0-443-15617-5.00039-1

Contributors

Thorlacius-Ussing, Jeppe 0000-0002-3340-0786 [1] Karsdal, Morten Asser 0000-0002-4764-5100 [1] Nielsen, Signe Holm 0000-0002-4612-1014 [1] [2]

Affiliations

  1. [1] Nordic Bioscience (Denmark)
  2. [NORA names: Nordic Bioscience; Private Research; Denmark; Europe, EU; Nordic; OECD];
  3. [2] Technical University of Denmark
  4. [NORA names: DTU Technical University of Denmark; University; Denmark; Europe, EU; Nordic; OECD]

Abstract

Type XIX collagen is a member of the fibril-associated collagens with interrupted triple helices (FACIT) family. It is thought to organize the collagenous extracellular matrix (ECM) through its ability to act as a cross-bridge between fibrils and other ECM molecules. Type XIX collagen is a homotrimer composed of three α1 chains and is expressed in vascular, neuronal, mesenchymal, and epithelial basement membrane zones in the breast, colon, kidney, liver, placenta, prostate, skeletal muscle, skin, and spleen. Type XIX collagen is involved in the development of the brain as well as muscle tissue of the esophagus and the heart. In addition, type XIX collagen is lost during breast cancer progression and harbors signaling domains that may inhibit the growth of melanoma cells. Biomarkers are available for measuring type XIX collagen and have been used to demonstrate elevated circulating levels of type XIX collagen in the serum of non-small-cell lung cancer patients.

Keywords

A1 chain, XIX collagen, basement membrane zone, biomarkers, brain, breast, breast cancer progression, cancer patients, cancer progression, cells, chain, collagen, collagenous extracellular matrix, colon, cross-bridges, development, domain, epithelial basement membrane zone, esophagus, extracellular matrix, extracellular matrix molecules, fibril-associated collagens, fibrillation, growth, growth of melanoma cells, heart, helix, homotrimer, interrupted triple helices, kidney, liver, lung cancer patients, matrix, melanoma cells, members, membrane zone, molecules, muscle, muscle tissue, non-small-cell lung cancer patients, patients, placenta, progression, prostate, serum, signal, signaling domain, skeletal muscle, skin, spleen, tissue, triple helix, type, type XIX collagen, zone

Data Provider: Digital Science