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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
The chief characteristic of cystatins, as implied by their name, is the ability to inhibit cysteine proteinases. Cystatins do not inhibit proteinases with other catalytic mechanisms, and they are usually thought to be selective for cysteine proteinases of the papain superfamily, which include the lysosomal proteinases cathepsin B, H, and L, and the cytosolic calpains. Some evidence suggests that other types of cysteine proteinases, including clostripain and polioviral proteinases, may be inhibited, although the interactions have not been studied in detail. Members of this superfamily are unique among the inhibitors considered in this chapter, since some of the members of families 1 and 2 are able to inhibit the exopeptidase known as dipeptidyl peptidase I, an enzyme that sequentially removes dipeptides from the N terminus of proteins.
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.
Mammalian Allergens
Published in Richard F. Lockey, Dennis K. Ledford, Allergens and Allergen Immunotherapy, 2014
Tuomas Virtanen, Tuure Kinnunen, 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 about 80% amino acid identity with human cystatin A (SBNS). 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, exhibit some degree of conservation with the sequence motif.
Association of beta-2-microglobulin, cystatin C and lipocalin-2 with stroke risk in the general Chinese population
Published in Annals of Medicine, 2023
Juanying Zhen, Shuyun Liu, Ryan Yan Lam Kam, Guoru Zhao, Hao Peng, Jianguo Liang, Aimin Xu, Chao Li, Lijie Ren, Jun Wu, Bernard Man Yung Cheung
Cystatin C was significantly associated with stroke risk in our study. The role of cystatin C in stroke has been controversial. Our results are consistent with those in the China Health and Retirement Longitudinal Study [21] and Cardiovascular Health Study [22]. In the China Health and Retirement Longitudinal Study reported recently, 410 (5.8%) out of 7064 participants developed new-onset stroke after 7 years of follow-up. Cystatin C was associated with new-onset stroke (HR: 1.19; 95% CI: 1.14, 1.25) [21], thereby confirming our findings. In the Cardiovascular Health Study, cystatin C was significantly associated with incident ischemic stroke and was a marker of poor outcome (shorter survival, cognitive decline and activities of daily living decline) after ischemic stroke in old adults [22]. However, conflicting results have been reported in other studies. A Mendelian randomization study using participant data from 16 prospective cohorts showed that cystatin C was not causally associated with CVD (RR: 1.00; 95% CI: 0.82, 1.22) and stroke (RR: 0.82; 95% CI: 0.57, 1.18) [9]. Thus, it seems that cystatin C is more a marker than a cause of vascular disease, although in animal models, cystatin C plays a role in endogenous neuroprotection and helps to maintain lysosomal membrane integrity [10]. Our study confirms the significant association between cystatin C and stroke, but further studies are needed to elucidate the mechanisms involved.
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
In the present study, both SCD and β-thalassemia patients with heart dysfunction had significantly higher levels of cystatin C than those without. This finding is consistent with Tantawy et al18 measured cystatin C levels in 53 children and adolescents with SCD and found that patients with SCD having heart disease had significantly higher levels than those without. To the best of our knowledge, no other studies have previously explored the relation between serum cystatin C and subclinical heart disease among patients with hemoglobinopathies. A possible explanation for the predictive value of cystatin C for further cardiovascular events is that, independently from renal Tubular dysfunction, elevated serum concentrations of this marker would reflect a defensive response against the augmented secretion of lysosomal cathepsin associated to inflammatory processes related to the atherosclerotic disease.14 Ge et al42 investigated plasma cystatin C in a total of 126 consecutive patients with coronary artery disease (CAD). They found elevated plasma cystatin C in CAD. Moreover, during a 6-month follow-up, 26 patients were found with adverse cardiovascular events and had significantly higher cystatin C levels than the 22 control patients at admission. Cystatin C plays an important role in the development of coronary artery disease (CAD) and is a strong predictor for risk of cardiovascular events.42
A nomogram based on serum cystatin C for predicting acute kidney injury in patients with traumatic brain injury
Published in Renal Failure, 2021
Ruo Ran Wang, Min He, Xiying Gui, Yan Kang
Previous studies have illustrated the prognostic role of serum cystatin C in a variety of critically ill patients [35–41]. Non-survivors commonly had higher initial or mean serum cystatin C level than survivors. For patients with neurological diseases, it has been confirmed that level of cystatin C was positively related with severity and adverse outcome of acute ischemic stroke, aneurysmal subarachnoid hemorrhage [42–46]. One study found that concentration of cystatin C in cerebrospinal fluid would increase in TBI patients [47]. Increase of serum cystatin C was also observed in patients suffering acute spinal cord injury [48]. Actually, increased production of cystatin C was an auto neural-protective response to protease hyperactivation in brain tissue and was beneficial for blood-brain barrier integrity and attenuation of early brain injury [47,49–51]. Therefore, we could infer that increased serum cystatin C was partially attributable to brain injury severity and the real value of cystatin C on reflecting renal function may be confounded by the injury severity. However, after adjusting the confounding effects of GCS, an indicator of brain injury severity, in multivariate logistic regression analysis, we found that higher cystatin C was independently associated with occurrence of AKI which indicated that increased cystatin C was an effective and accurate marker of declined renal function in TBI patients.