Abstract
Collagen type I is a major constituent of animal bodies. It is found in large quantities in tendon, bone, skin, cartilage, blood vessels, bronchi, and the lung interstitium. It is also produced and accumulates in large amounts in response to certain inflammations such as lung fibrosis. Our understanding of the molecular organization of fibrillar collagen and cellular interaction motifs, such as those involved with immune-associated molecules, continues to be refined. In this study, antibodies raised against type I collagen were used to label intact D-periodic type I collagen fibrils and observed with atomic force microscopy (AFM), and X-ray diffraction (XRD) and immunolabeling positions were observed with both methods. The antibodies bind close to the C-terminal telopeptide which verifies the location and accessibility of both the major histocompatibility complex (MHC) class I (MHCI) binding domain and C-terminal telopeptide on the outside of the collagen fibril. The close proximity of the C-telopeptide and the MHC1 domain of type I collagen to fibronectin, discoidin domain receptor (DDR), and collagenase cleavage domains likely facilitate the interaction of ligands and receptors related to cellular immunity and the collagen-based Extracellular Matrix.
Highlights
Collagen fibrils present in different tissues such as tendons, ligaments, bone, cornea, cartilage, skin, blood vessels, large bronchi, and lung interstitium are constituted by a hierarchical packing of collagen molecules
These fibrils are remarkably well adapted to their respective mechanical and biochemical functions. Collagen fibrils and their constituent molecular components play an important role in tissue and cellular activities, including immune responses involving the major histocompatibility complex (MHC)
The location of the MHC domain of type I collagen and its potential role in the organizational relationship between collagen fibrils and cellular receptors are described in this study
Summary
Collagen fibrils present in different tissues such as tendons, ligaments, bone, cornea, cartilage, skin, blood vessels, large bronchi, and lung interstitium are constituted by a hierarchical packing of collagen molecules. These fibrils are remarkably well adapted to their respective mechanical and biochemical functions. Collagen fibrils and their constituent molecular components play an important role in tissue and cellular activities, including immune responses involving the major histocompatibility complex (MHC). MHC-mediated immunity involves the presentation of peptide sequences for the identification of foreign bodies or self-recognition. In the case of autoreactivity, self-peptides, are presented to T-cells leading to autoimmune responses such as in lung fibrosis. The location of the MHC domain of type I collagen and its potential role in the organizational relationship between collagen fibrils and cellular receptors are described in this study
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