Abstract
Human high‐temperature requirement protein 1 (HTRA1) is a member of serine proteases and consists of four well‐defined domains—an IGFBP domain, a Kazal domain, a protease domain and a PDZ domain. HTRA1 is a secretory protein and also present intracellularly and associated with microtubules. HTRA1 regulates a broad range of physiological processes via its proteolytic activity. This review examines the role of HTRA1 in bone biology, osteoarthritis, intervertebral disc (IVD) degeneration and tumorigenesis. HTRA1 mediates diverse pathological processes via a variety of signalling pathways, such as TGF‐β and NF‐κB. The expression of HTRA1 is increased in arthritis and IVD degeneration, suggesting that HTRA1 protein is attributed to cartilage degeneration and disease progression. Emerging evidence also suggests that HTRA1 has a role in tumorigenesis. Further understanding the mechanisms by which HTRA1 displays as an extrinsic and intrinsic regulator in a cell type–specific manner will be important for the development of HTRA1 as a therapeutic target.
Highlights
Human high-temperature requirement protein 1 (HTRA1), known as L56, or serine protease 11 was first isolated from human fibroblasts as a putative serine protease.[1]
HTRA1 takes part in many biological processes and cellular signalling pathways, and is implicated in pathogenesis including osteoporosis, osteoarthritis, Alzheimer's disease, age-related macular degeneration and cancer.[3-6]. This topical review discusses recent findings pointing to the role of HTRA1 in bone biology, arthritis and tumorigenesis
Some inconsistent results regarding the effects of HTRA1 on bone formation may be due to complex interactions between HTRA1 and TGF-β family proteins in different cells and dosages of HTRA1 used in each experimental design
Summary
Human high-temperature requirement protein 1 (HTRA1), known as L56, or serine protease 11 was first isolated from human fibroblasts as a putative serine protease.[1].
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