Kallikreins
نویسندگان
چکیده
منابع مشابه
Kallikreins and lupus nephritis.
The kidney kallikrein-kinin system plays important roles in inflammation, coagulation, angiogenesis, and regulation of vessel tone and permeability. In this issue of the JCI, Liu et al. provide data that suggest a protective role for kallikrein in animal models of anti-glomerular basement membrane(GBM) antibody-induced nephritis, an experimental model of Goodpasture disease (see the related art...
متن کاملHuman tissue kallikreins: a road under construction.
BACKGROUND The human tissue kallikrein gene family, located at chromosome 19q13.4, is the largest contiguous family of proteases in the human genome. The locus encodes all 15 members of the family, 13 of which have been reported as potential biomarkers for several carcinomas and other non-neoplastic diseases. Kallikreins are expressed by a wide range of tissues and implicated in a number of phy...
متن کاملKallikreins: unravelling the genetics of autoimmune glomerulonephritis.
Human disease gene discovery has entered a new era where genome-wide associations (GWA), and high throughput sequencing technologies are providing a first survey of the complex genetic architecture of common diseases. Immune-mediated glomerulonephritis, a shared pathological feature of systemic lupus erythematosus (SLE), systemic vasculitis and Goodpasture syndrome, displays a strong genetic co...
متن کاملEvolutionary History of Tissue Kallikreins
The gene family of human kallikrein-related peptidases (KLKs) encodes proteins with diverse and pleiotropic functions in normal physiology as well as in disease states. Currently, the most widely known KLK is KLK3 or prostate-specific antigen (PSA) that has applications in clinical diagnosis and monitoring of prostate cancer. The KLK gene family encompasses the largest contiguous cluster of ser...
متن کاملKallikreins in Humans and Other Species
residue (cysteine proteases), aspartate (aspartate proteases), metal ion (metalloproteases) or serine (serine proteases). Serine proteases are a family of enzymes that utilizes a uniquely activated serine residue in the substrate-binding site to catalytically hydrolyze peptide bonds (Schultz and Liebman, 1997). This active site is characterized by the irreversible interaction with diisopropylfl...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1969
ISSN: 0306-3283
DOI: 10.1042/bj1150004p