Chapter, 2024

Chapter 13 Type XIII collagen

Biochemistry of Collagens, Laminins and Elastin 9780443156175, Pages 123-129

Editors:

Publisher: Elsevier

DOI: 10.1016/b978-0-443-15617-5.00007-x

Contributors

Sinkeviciute, Dovile 0000-0003-4275-388X [1] Jansen, S M [1] Siebuhr, Anne Sofie 0000-0003-0802-8422 [1] Thudium, Christian Schneider [1] Karsdal, Morten Asser 0000-0002-4764-5100 [1]

Affiliations

  1. [1] Nordic Bioscience (Denmark)
    2. [NORA names: Nordic Bioscience; Private Research; Denmark; Europe, EU; Nordic; OECD]

Abstract

Type XIII collagen is a nonfibrillar, type II transmembrane collagen that belongs to a subgroup of collagens called membrane-associated collagens with interrupted triple helices. It comprises a short N-terminal cytosolic domain, a transmembrane domain, and a largely collagenous ectodomain, and exists as a soluble form due to ectodomain shedding. Type XIII collagen binds to proteins like fibronectin, perlecan, nidogen-2, vitronectin, type IV collagen, and α1β1 integrin. Its expression is more pronounced during development and postnatal growth but decreases toward adulthood. It is largely expressed in cells producing connective tissue, with higher expression in certain tumors, corneal wound healing, and renal fibrosis. Type XIII collagen is crucial to the normal structure and function of neuromuscular synapses. Loss of type XIII collagen is not lethal but affects maturation of both the pre- and postsynaptic specializations of the neuromuscular junctions. Overexpression of the normal type XIII collagen α-chain in cartilage and periosteal osteoblasts results in the development of massive bone overgrowth due to an enhanced osteoblast differentiation capacity. There are currently no biomarkers for type XIII collagen.

Keywords

A-chain, A1B1, IV collagen, N-terminal cytosolic domain, adulthood, biomarkers, bone overgrowth, capacity, cartilage, cells, collagen, collagenous ectodomain, connective tissue, corneal, corneal wound healing, cytosolic domain, decreases toward adulthood, development, differentiation capacity, domain, ectodomain, ectodomain shedding, expression, fibronectin, fibrosis, function, function of neuromuscular synapses, growth, healing, helix, integrin, interrupted triple helices, junction, loss, maturation, neuromuscular junction, neuromuscular synapses, nidogen-2, normal structure, osteoblast differentiation capacity, osteoblasts, overexpression, overgrowth, periosteal, periosteal osteoblasts, perlecan, postnatal growth, postsynaptic specializations, pre-, protein, renal fibrosis, shedding, specialization, structure, subgroups, synapses, tissue, transmembrane collagen, transmembrane domain, triple helix, tumor, type, type IV collagen, type XIII collagen, vitronectin, wound healing

Data Provider: Digital Science

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