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

Lesiak, Marta; Auguściak‐Duma, Aleksandra; Szydło, Anna; Pruszczynska, Ksymena; Sieroń, Aleksander

doi:10.18388/abp.2008_3076

Cited by 4 publications

(1 citation statement)

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“…ADAMTS-2, 3, and 14 are upregulated in OA cartilage [ 66 ]. ADAMTS-2 processes type I procollagen, which is principally expressed in skin, while ADAMTS-3 principally processes type II procollagen in the cartilage.…”

Section: Extracellular Matrix In Osteoarthritismentioning

confidence: 99%

The Mechanism and Role of ADAMTS Protein Family in Osteoarthritis

Peng

et al. 2022

Biomolecules

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Osteoarthritis (OA) is a principal cause of aches and disability worldwide. It is characterized by the inflammation of the bone leading to degeneration and loss of cartilage function. Factors, including diet, age, and obesity, impact and/or lead to osteoarthritis. In the past few years, OA has received considerable scholarly attention owing to its increasing prevalence, resulting in a cumbersome burden. At present, most of the interventions only relieve short-term symptoms, and some treatments and drugs can aggravate the disease in the long run. There is a pressing need to address the safety problems due to osteoarthritis. A disintegrin-like and metalloprotease domain with thrombospondin type 1 repeats (ADAMTS) metalloproteinase is a kind of secretory zinc endopeptidase, comprising 19 kinds of zinc endopeptidases. ADAMTS has been implicated in several human diseases, including OA. For example, aggrecanases, ADAMTS-4 and ADAMTS-5, participate in the cleavage of aggrecan in the extracellular matrix (ECM); ADAMTS-7 and ADAMTS-12 participate in the fission of Cartilage Oligomeric Matrix Protein (COMP) into COMP lyase, and ADAMTS-2, ADAMTS-3, and ADAMTS-14 promote the formation of collagen fibers. In this article, we principally review the role of ADAMTS metalloproteinases in osteoarthritis. From three different dimensions, we explain how ADAMTS participates in all the following aspects of osteoarthritis: ECM, cartilage degeneration, and synovial inflammation. Thus, ADAMTS may be a potential therapeutic target in osteoarthritis, and this article may render a theoretical basis for the study of new therapeutic methods for osteoarthritis.

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Section: Extracellular Matrix In Osteoarthritismentioning

confidence: 99%

The Mechanism and Role of ADAMTS Protein Family in Osteoarthritis

Peng

et al. 2022

Biomolecules

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Procollagen C-Endopeptidase

Kessler

2013

Handbook of Proteolytic Enzymes

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Blocking angiogenesis with peptides that inhibit the activity of procollagen C-endopeptidase

Lesiak

Auguściak‐Duma

Szydło

et al. 2009

Pharmacological Reports

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Procollagen C-endopeptidase (BMP-1) is one of two key enzymes crucial for conversion of fibrillar procollagens to self-assembling collagen monomers. Recently, we have reported inhibition of the largest variant of BMP-1, a recombinant mammalian tolloid (mTld) in vitro, on procollagen type I using peptides with amino acid sequences in chordin conserved across different species. Here, we tested the same peptides as potent blockers of angiogenesis ex vivo in cultured rings of rat aorta, in vivo in chick embryos, and in vitro in cell cultures. Our results revealed that the peptides inhibited the angiogenic activity in rat aorta explants at micromolar concentrations; they also blocked blood vessel growth in chick embryos. The peptides were also tested on three types of human cells, e.g., umbilical vein endothelium, skin fibroblasts, and tumor HT-1080 cells. Since the three types of cells proliferated at a significantly lower rate or did not proliferate at all, we conclude that the anti-angiogenic effect observed in rat aorta ring explants and in chick embryos was related to inhibition of cell proliferation. In conclusion, we showed the ability to inhibit angiogenesis by blocking the activity of procollagen C-endopeptidase. The results strongly indicate crucial role(s) of this metalloproteinase in the formation of new blood vessels and maintenance of their growth.

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

Cited by 4 publications

References 50 publications

The Mechanism and Role of ADAMTS Protein Family in Osteoarthritis

The Mechanism and Role of ADAMTS Protein Family in Osteoarthritis

Procollagen C-Endopeptidase

Blocking angiogenesis with peptides that inhibit the activity of procollagen C-endopeptidase

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