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Proteinase Inhibitors: An Overview of their Structure and Possible Function in the Acute Phase
Published in Andrzej Mackiewicz, Irving Kushner, Heinz Baumann, Acute Phase Proteins, 2020
Family 1 members lack intrachain disulfides, carbohydrate and signal peptides, and probably reside mainly in the cytoplasm, although small amounts (0.3 to 0.4 μM) of human cystatin A are found in saliva and amniotic fluid.121 The best-characterized members are human cystatin A and rat cystatin-α, and human cystatin B and rat cystatin-β. The rat cystatins are probably orthologs of the human proteins. There is currently no consensus for biological roles of family 1 members, so our ideas of possible functions are based mainly upon circumstantial evidence. Family 1 cystatins are found in most cells of the body, although the distribution of A and α differs from that of B and β. A and α are found predominantly in epidermal layers of the skin, epithelial cell types that line the gastrointestinal tract, and neutrophils, whereas B and β have a much more even distribution throughout cells and tissues. The restricted distribution of A and α, in cell types thought to be involved in “frontline defense” against pathogens, led Barrett and colleagues10 to speculate a function in the inhibition of pathogenic proteinases. The much broader distribution of B and β, reminiscent of the distribution of lysosomes, led the same authors to suggest a protective role for these inhibitors in regulating the activity of lysosomal cysteine proteinases.
Mammalian allergens
Published in Richard F. Lockey, Dennis K. Ledford, Allergens and Allergen Immunotherapy, 2020
Tuomas Virtanen, Marja Rytkönen-Nissinen
Fel d 3 is a 11-kDa protein containing 98 amino acids. There is one potential N-linked glycosylation site in the sequence. Fel d 3 exhibits approximately 80% amino acid identity with human cystatin A (BLAST). As endogenous protease inhibitors, cystatins control the function of cysteine proteases. Fel d 3 contains the signature motif conserved in cysteine protease inhibitors. Dog allergens, Can f 1 and Can f 2, which are lipocalins, show some homology with this sequence motif.
Glomerular Filtration Rate
Published in Lara Wijayasiri, Kate McCombe, Paul Hatton, David Bogod, The Primary FRCA Structured Oral Examination Study Guide 1, 2017
Lara Wijayasiri, Kate McCombe, Paul Hatton, David Bogod
Cystatin CEndogenous substance, freely filtered but limited due to wide variation in serum levels.At present, it has no clinical role in GFR measurement.
Expression of urinary exosomal miRNA-615-3p and miRNA-3147 in diabetic kidney disease and their association with inflammation and fibrosis
Published in Renal Failure, 2023
Jiaxin Wang, Yiying Tao, Fan Zhao, Tong Liu, Xiahong Shen, Ling Zhou
As a traditional inflammatory indicator, Cystatin C not only reflects the degree of renal damage but is also one of the important indicators of the micro-inflammatory state in DKD patients [46]. Cystatin C is a low molecular weight protein (13KD) produced by all nucleated human cells and is primarily catabolized by proximal tubular cells [47]. As an endogenous inhibitor of cysteine protein, it is not affected by age, gender, muscle mass, or protein intake [48]. However, studies [46] have shown that serum Cystatin C is positively correlated with the micro-inflammatory state of DKD and related inflammatory factors. Cystatin C is not only correlated with eGFR and other indicators of renal function damage but also in evaluating the degree and progression of inflammatory response in the course of DKD. The present study provided evidence that the expression level of urinary exosomal miRNA-615-3p correlated with serum Cystatin C, so urinary exosomal miRNA-615-3p might be useful as a marker of the inflammatory response and the progression of kidney damage in DKD.
Assessment of cystatin C in pediatric sickle cell disease and β-thalassemia as a marker of subclinical cardiovascular dysfunction: a case-control study
Published in Pediatric Hematology and Oncology, 2021
Diana Hanna, Mohamed Beshir, Naglaa Khalifa, Eman Baz, Ahmed Elhewala
Cystatin C is a protein encoded by the CST3 gene and it is mainly used as a biomarker of kidney function.14 Cystatin C has a low molecular weight and it is removed from the bloodstream by glomerular filtration in the kidneys. If kidney function and glomerular filtration rate decline, the blood levels of cystatin C rise.15 Cystatin C is a reliable marker of renal function, particularly when the renal function is only mildly or moderately impaired.16 Recently, it has been studied for its role in detection of new-onset or deteriorating cardiovascular disease (CVD).17 A high level of cystatin C has been reported to be positively associated with the increased risk of cardiovascular morbidity and mortality, this may be due to inflammation, atherosclerosis and association with vascular risk factors.17 Carotid intima–media thickness (CIMT) is a predictive marker of atherosclerosis and provides a noninvasive method for assessment of subclinical atherosclerosis.18
Cystatin C as a biomarker of chronic kidney disease: latest developments
Published in Expert Review of Molecular Diagnostics, 2020
Stefanie W. Benoit, Eileen A. Ciccia, Prasad Devarajan
Cystatin C, a 13-kDa cysteine proteinase inhibitor protein, is produced by all nucleated cells at a steady rate [6] and is freely filtered by the kidney with near-complete reabsorption and catabolism in the proximal tubule and no significant urinary excretion [7]. Thus, serum cystatin C levels are much less affected by such patient characteristics such as gender, age, body size and composition, and nutritional status. It was first proposed as a glomerular filtration biomarker in 1985, and its clinical utility in comparison to creatinine has been argued and vetted now for more than 30 years, as summarized in Table 1 [8]. In this review, we will address the most recent developments in the clinical application of serum cystatin C measurements and assess its value as a biomarker in CKD patients.