Post-translational modification of type IV collagen with 3-hydroxyproline affects its interactions with glycoprotein VI and nidogens 1 and 2

• Published in: The Journal of biological chemistry Vol. 293; no. 16; pp. 5987 - 5999
• Main Authors: Montgomery, Nathan T., Zientek, Keith D., Pokidysheva, Elena N., Bächinger, Hans Peter
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 20.04.2018; American Society for Biochemistry and Molecular Biology
• Subjects: Animals; basement membrane; Calcium-Binding Proteins; Cell Adhesion Molecules; Cell Line; collagen; collagen IV; Collagen Type IV - metabolism; Glycobiology and Extracellular Matrices; Hydroxyproline - metabolism; mass spectrometry (MS); Membrane Glycoproteins - metabolism; Mice; Platelet Membrane Glycoproteins - metabolism; post-translational modification (PTM); protein chemistry; Protein Interaction Maps; protein interactions; Protein Processing, Post-Translational; tandem mass spectrometry; post-translational modification (PTM); protein interactions; basement membrane; tandem mass spectrometry; collagen; protein chemistry; collagen IV; mass spectrometry (MS)

Type IV collagen is a major component of the basement membrane and interacts with numerous other basement membrane proteins. Many of these interactions are poorly characterized. Type IV collagen is abundantly post-translationally modified with 3-hydroxyproline (3-Hyp), but 3-Hyp’s biochemical role i...