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Title: Ultrastructural Location and Interactions of the Immunoglobulin Receptor Binding Sequence within Fibrillar Type I Collagen

Journal Article · · International Journal of Molecular Sciences (Online)
DOI:https://doi.org/10.3390/ijms21114166· OSTI ID:1798827
 [1]; ORCiD logo [2];  [3];  [3];  [4];  [3]; ORCiD logo [2]
  1. Northwest A&F Univ., Yangling (China). Inst. of Biophysics; Illinois Institute of Technology, Chicago, IL (United States); Illinois Institute of Technology, Chicago, IL (United States). Pritzker Inst. of Biomedical Science and Engineering
  2. Illinois Institute of Technology, Chicago, IL (United States); Illinois Institute of Technology, Chicago, IL (United States). Pritzker Inst. of Biomedical Science and Engineering
  3. Illinois Institute of Technology, Chicago, IL (United States)
  4. Illinois Institute of Technology, Chicago, IL (United States); Argonne National Lab. (ANL), Lemont, IL (United States)

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.

Research Organization:
Argonne National Laboratory (ANL), Argonne, IL (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES). Scientific User Facilities Division; Fundamental Research Funds for the Central Universities; National Institutes of Health (NIH)
Grant/Contract Number:
AC02-06CH11357; 2452019074; 9 P41 GM103622
OSTI ID:
1798827
Journal Information:
International Journal of Molecular Sciences (Online), Vol. 21, Issue 11; ISSN 1422-0067
Publisher:
MDPICopyright Statement
Country of Publication:
United States
Language:
English

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