» Articles » PMID: 9074757

Emerging Roles for Cysteine Proteases in Human Biology

Overview
Publisher Annual Reviews
Specialty Physiology
Date 1997 Jan 1
PMID 9074757
Citations 198
Authors
Affiliations
Soon will be listed here.
Abstract

Cysteine proteases have traditionally been viewed as lysosomal mediators of terminal protein degradation. However, recent findings refute this limited view and suggest a more expanded role for cysteine proteases in human biology. Several newly discovered members of this enzyme class are regulated proteases with limited tissue expression, which implies specific roles in cellular physiology. These roles appear to include apoptosis, MHC class II immune responses, prohormone processing, and extracellular matrix remodeling important to bone development. The ability of macrophages and other cells to mobilize elastolytic cysteine proteases to their surfaces under specialized conditions may also lead to accelerated collagen and elastin degradation at sites of inflammation in diseases such as atherosclerosis and emphysema. The development of inhibitors of specific cysteine proteases promises to provide new drugs for modifying immunity, osteoporosis, and chronic inflammation.

Citing Articles

Aquaporins modulate the cold response of Haemaphysalis longicornis via changes in gene and protein expression of fatty acids.

Wang H, Bai R, Pei T, Meng J, Nwanade C, Zhang Y Parasit Vectors. 2025; 18(1):70.

PMID: 39994701 PMC: 11849292. DOI: 10.1186/s13071-025-06718-x.


Assessment of the diagnostic value of serum cathepsin S and its correlation with HDL subclasses in patients with non-Hodgkin's lymphoma.

Mirjanic-Azaric B, Stankovic S, Radic-Savic Z, Malcic-Zanic D, Ninic A, Vukovic M J Med Biochem. 2024; 43(5):711-719.

PMID: 39712508 PMC: 11662951. DOI: 10.5937/jomb0-48959.


Autophagy-lysosomal pathway impairment and cathepsin dysregulation in Alzheimer's disease.

Mancano A, Pina J, Froes B, Sciani J Front Mol Biosci. 2024; 11:1490275.

PMID: 39544403 PMC: 11560772. DOI: 10.3389/fmolb.2024.1490275.


Advances in the treatment of atherosclerosis with ligand-modified nanocarriers.

Deng X, Wang J, Yu S, Tan S, Yu T, Xu Q Exploration (Beijing). 2024; 4(3):20230090.

PMID: 38939861 PMC: 11189587. DOI: 10.1002/EXP.20230090.


Cathepsin X deficiency alters the processing and localisation of cathepsin L and impairs cleavage of a nuclear cathepsin L substrate.

Xu B, Anderson B, Mountford S, Thompson P, Mintern J, Edgington-Mitchell L Biol Chem. 2024; 405(5):351-365.

PMID: 38410910 DOI: 10.1515/hsz-2023-0355.