Specific inhibition of procollagen C-endopeptidase activity by synthetic peptide with conservative sequence found in chordin

• Published in: Acta biochimica polonica Vol. 55; no. 2; pp. 297 - 305
• Main Authors: Lesiak, Marta, Augusciak-Duma, Aleksandra, Szydlo, Anna, Pruszczynska, Ksymena, Sieron, Aleksander L
• Format: Journal Article
• Language: English
• Published: Poland 01.01.2008
• Subjects: ADAM Proteins - metabolism; ADAMTS Proteins; ADAMTS4 Protein; Amino Acid Sequence; Animals; Binding Sites; Bone Morphogenetic Protein 1; Bone Morphogenetic Proteins - antagonists & inhibitors; Bone Morphogenetic Proteins - chemistry; Bone Morphogenetic Proteins - genetics; Cattle; Conserved Sequence; Glycoproteins - genetics; Humans; Intercellular Signaling Peptides and Proteins - genetics; Metalloendopeptidases - antagonists & inhibitors; Metalloendopeptidases - chemistry; Metalloendopeptidases - genetics; Metalloproteases - antagonists & inhibitors; Metalloproteases - chemistry; Metalloproteases - genetics; Molecular Sequence Data; Peptides - genetics; Peptides - pharmacology; Procollagen N-Endopeptidase - metabolism; Protease Inhibitors - pharmacology; Protein Structure, Tertiary; Recombinant Proteins - antagonists & inhibitors; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Tolloid-Like Metalloproteinases

Procollagen C-endopeptidase (BMP-1) and N-endopeptidase (ADAMTS-2) are key enzymes for correct and efficient conversion of fibrillar procollagens to their self assembling monomers. Thus, they have an essential role in building and controlling the quality of extracellular matrices (ECMs). Here, we te...