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PubMed1991

Salivary cystatin SA-III, a potential precursor of the acquired enamel pellicle, is phosphorylated at both its amino- and carboxyl-terminal regions.

Cystatin SA-III was purified from human submandibular/sublingual glandular secretions by adsorption to hydroxyapatite, gel filtration chromatography, and reversed-phase HPLC. The amino acid sequence of its amino-terminus was deduced by sequential Edman degradation and found to be identical to the first 10 residues of cystatin HSP-12. The purified protein was digested with endoproteinase Asp-N and the digestion products were subjected to fast atom bombardment mass spectroscopy. m/z values corresponding to 12 peptides were aligned to the sequence of cystatin S preceded by the eight-residue amino-terminal peptide detected in HSP-12. This process resulted in the assignment of peptides corresponding with 118 out of the 121 amino acid residues predicted from the nucleotide sequence for cystatin SA-III. In order to align several peptides, it was necessary to substitute four residues of phosphoserine for four residues of serine. Fast atom bombardment mass spectrometry and additional Edman degradation procedures localized the phosphate moieties to Ser-3, Ser-99, Ser-112, and Ser-116. This is the first report of the structure of cystatin SA-III deduced by amino acid sequencing techniques and indicates the sites of phosphoserine within the molecule. Based on these assignments, cystatin SA-III is unique among salivary proteins in that it possesses phosphate groups at its amino-terminus as well as its carboxyl-terminus.

Amino Acid Sequence↗
PubMed1989

Growth stimulation of 3T3 fibroblasts by cystatin.

Treatment of cultures of mouse 3T3 fibroblasts with Cystatin C, a thiol-proteinase inhibitor isolated from chicken egg white, resulted in an enhanced rate of cell proliferation. This stimulation was demonstrated using two independent assay systems: (a) assessment of total cell number and (b) measurement of [3H]thymidine incorporated into acid-precipitable DNA. In both assays, the dose-response curves of Cystatin stimulation showed a rising function that plateaued at a concentration of approximately 120 micrograms/ml. The addition of Cystatin to cultures of Kirsten murine sarcoma virus-transformed 3T3 cells also enhanced DNA synthesis in these target cells. Control experiments showed that the presence of Cystatin did not alter the level of binding of radioactively labeled epidermal growth factor and platelet derived growth factor to 3T3 cells. These results argue against the possibility that the observed growth stimulation by Cystatin was due to growth factor contamination of the Cystatin preparation.

Animals↗
PubMed1988

Two rat homologues of human cystatin C.

Two immunochemically related forms of cystatin C-like inhibitors which differ in their Mr app and isoelectric point have been found both in urine and seminal vesicles of rats. Amino-terminal sequences of these two cystatins are identical within the same fluid and exhibit a high degree of homology with that of human cystatin C. However, cystatins C purified from urine lack eight residues at their amino-terminal end when compared to those of seminal vesicles. The occurrence of two cystatin C-like components in rat fluids has been found to be due to the presence of a glycosylated form reported here as cystatin Cg which specifically binds concanavalin A and is susceptible to endo-beta-N-acetylglucosaminidase treatment.

Amino Acid Sequence↗
PubMed2005

Absence of the protease inhibitor cystatin C in inflammatory cells results in larger plaque area in plaque regression of apoE-deficient mice.

Matrix remodelling plays an important role in regulating plaque stability. Cystatin C, an inhibitor of the elastin-degrading cysteine proteases of the cathepsin family, is believed to be one of the key protease inhibitors in this process. The aim of the present study was to investigate the role of leukocyte-specific cystatin C expression under conditions that favour plaque regression. Apolipoprotein E-deficient mice (apoE-/-) were given a Western-type diet 15 weeks prior transplantation with bone marrow from mice lacking cystatin C (cysC-/-) or cystatin C positive (cysC+/+) mice, in both cases apoE+/+ to create conditions favouring plaque regression. Transplantations were verified with PCR and Western analyses. Transplanted mice showed a 70% decrease in lipid content and reduction in plaque area compared to baseline ApoE-/- mice, demonstrating plaque regression due to apoE expression in macrophages. apoE-/- mice transplanted with cysC-/- bone marrow were then compared to mice transplanted with cysC+/+ bone marrow. Mice receiving cysC-/- bone marrow had a 30% larger plaque area, despite absence of significant differences in plasma cholesterol and lipid contents in plaque. Unexpectedly, mice transplanted with cystatin C-deficient bone marrow cells had increased elastin and collagen content in lesions. These observations suggest that leukocyte-specific expression of cystatin C is actively involved in matrix remodelling associated with plaque regression.

Animals↗
PubMed2005

Neuronal cell death induced by cystatin C in vivo and in cultured human CNS neurons is inhibited with cathepsin B.

Cystatin C, a cysteine protease inhibitor, is implicated in pathogenesis of late-onset Alzheimer's disease and other neurological disorders. Our recent study showed that cystatin C injection into rat hippocampus induced neuronal cell death in granule cell layer of dentate gyrus in vivo. We further confirmed that cystatin C neurotoxicity was inhibited by simultaneous coapplication of cathepsin B, a cysteine protease. In vitro cytotoxicity was also studied in cultures of human CNS neurons, mixed cultures with astrocytes and A1 human hybrid neurons. Cystatin C induced neuronal cell death in a dose-dependent manner, which accompanied increased number of TUNEL (+) cells, up-regulation of active caspase-3 and DNA ladder. The results of the present study indicate that cystatin C participates in the process of apoptotic neuronal cell death in experimental conditions by means of inhibitory activity of cysteine proteases, and that cystatin C might be involved in the pathogenesis in human neurological disorders including Alzheimer's disease.

Animals↗
PubMed2004

Serum cystatin C in patients with head and neck carcinoma.

BACKGROUND: The balance between proteinases of various classes and their inhibitors was found to be of critical importance for local invasion and metastasizing of tumor cells. The aim of the present study was to determine the changes in the serum cystatin C concentration in patients with squamous cell carcinoma of the head and neck. METHODS: In the sera of 34 patients with squamous cell carcinoma of the head and neck, the concentration of cysteine proteinase inhibitor cystatin C was determined using ELISA. The serum samples were collected at diagnosis (group A) and 7 to 407 days (median, 59 days) after the therapy (group B). The sera of 30 healthy blood donors served as controls (group C). RESULTS: A significant increase in the median concentration of cystatin C was found in the patients' sera (group A: 573 ng/ml, P<0.0001; group B: 551 ng/ml, P<0.0001) compared to control group C (320 ng/ml), whereas no difference was observed between groups A and B (P>0.05). Cystatin C concentrations in the sera of group A correlated with the site of primary tumor (P=0.035), being higher in the patients with non-laryngeal tumors (658 ng/ml) than in those with larynx primaries (529 ng/ml). There was a significant trend (RS=-0.535, P=0.049) towards lower cystatin C concentrations with an increasing time delay in post-treatment serum sampling (group B), which was observed in the patients with no relapse of the disease and a sampling later than 45 days after the completion of therapy. CONCLUSIONS: These results add to the knowledge of the role of cystatin C in invasive behavior of squamous cell carcinoma of the head and neck, and suggest its potential role as a tumor marker in this particular type of cancer.

Adult↗
PubMed2005

Assessing glomerular filtration rate in renal transplant recipients by estimates derived from serum measurements of creatinine and cystatin C.

BACKGROUND: Assessing glomerular filtration rate (GFR) is of importance in the surveillance of renal transplant recipients. As serum markers alone are inaccurate for estimating GFR, several equations have been developed with the aim of translating a serum value into a corresponding and more accurate GFR. The present study investigated the diagnostic characteristics of GFR estimates obtained by the simplified MDRD formula and the cystatin C based estimate described by Larsson et al. METHODS: Prospective study in 29 stable renal transplant recipients. GFR was assessed with (125)I-Iothalamate clearance, creatinine was measured with a modified Jaffe method on Dimension RxL (Dade-Behring, Dudingen, Switzerland), cystatin C was determined by particle enhanced turbidimetric immunassay (PETIA; Dako, Glostrup, Denmark). Bias, precision and diagnostic accuracy of the two GFR estimates were assessed with Bland-Altman method and receiver-operating characteristics (ROC) analysis. The latter was performed at a GFR cut-off of 60 ml/min/1.73 m2. RESULTS: The cystatin C based GFR estimate normalized to a body surface area of 1.73 m2 exhibited a bias of -4.7 ml/min/1.73 m2, the 95% limits of agreement were -25.5-16 ml/min/1.73 m2 with an AUC of 0.87. The MDRD estimates obtained from the original creatinine revealed biased results. Thus, non-constant recalibration of creatinine was done. Recalibrated creatinine gave an MDRD GFR estimate with a bias of 1.7 ml/min/1.73 m2. The limits of agreement were -23.1-26.4 ml/min/1.73 m2. ROC analysis revealed an AUC 0.8 and was not significantly different from the cystatin C based GFR estimate. CONCLUSIONS: In renal transplant recipients, the cystatin C based GFR estimate exhibits similar diagnostic characteristics like the simplified MDRD formula. In contrast to cystatin C measurement, recalibration of creatinine might be necessary before implementing the simplified MDRD formula into clinical routine.

Adult↗
PubMed2005

Evaluation of Cystatin C as a marker of renal injury following on-pump and off-pump coronary surgery.

OBJECTIVE: Cardiopulmonary bypass is regarded as an important contributor to renal injury, whereas off-pump surgery is considered less damaging. Cystatin C, a cystine protease inhibitor, is more sensitive and specific than creatinine in the assessment of renal function. We assessed the value of Cystatin C in quantifying clinical and subclinical renal injury following on-pump and off-pump cardiac surgery. METHODS: Sixty consecutive patients were recruited: 30 patients undergoing on-pump CABG and 30 patients undergoing off-pump CABG. Blood samples were collected pre-operatively and on days 1, 2 and 4 postoperatively to measure serum creatinine and serum Cystatin C. Urinary samples were collected concurrently to measure microalbumin and N-acetyl-beta-glucosaminidase, denoting changes in renal glomerular and tubular function respectively. RESULTS: The off-pump group were older (65+/-11 vs. 61+/-8 years; P=0.046), had a higher mean Parsonnet score (9.4+/-6.2 vs. 5.4+/-3.6, P<0.01) and received fewer grafts (2.4+/-0.9 vs. 3.1+/-0.7; P<0.01) compared to the on-pump group. The groups were otherwise matched with respect to preoperative renal function and left ventricular function. Patients undergoing on-pump CABG had greater increases in all four parameters of renal injury. Adjustment for preoperative differences increased the size and significance of the effect of off-pump vs. on-pump surgery (percent difference 13%; 95% CI 2-26 for creatinine, and 16%; 95% CI 4-29 for Cystatin C). Cystatin and creatinine were strongly correlated with each other. CONCLUSIONS: Avoidance of cardiopulmonary bypass may reduce renal injury particularly in higher risk patients. Cystatin C proved to be a simple and sensitive measure of overall renal function and can be used in the routine assessment of renoprotective strategies.

Aged↗
PubMed2005

Cystatin-C and mortality in elderly persons with heart failure.

OBJECTIVES: We sought to evaluate cystatin-C, a novel measure of renal function, as a predictor of mortality in elderly persons with heart failure (HF) and to compare it with creatinine. BACKGROUND: Renal function is an important prognostic factor in patients with HF, but creatinine levels, which partly reflect muscle mass, may be insensitive for detecting renal insufficiency. METHODS: A total of 279 Cardiovascular Health Study participants with prevalent HF and measures of serum cystatin-C and creatinine were followed for mortality outcomes over a median of 6.5 years. RESULTS: Median creatinine and cystatin-C levels were 1.05 mg/dl and 1.26 mg/l. Each standard deviation increase in cystatin-C (0.35 mg/l) was associated with a 31% greater adjusted mortality risk (95% confidence interval [CI] 20% to 43%, p < 0.001), whereas each standard deviation increase in creatinine (0.39 mg/dl) was associated with a 17% greater adjusted mortality risk (95% CI 1% to 36%, p = 0.04). When both measures were combined in a single adjusted model, cystatin-C remained associated with elevated mortality risk (hazard ratio 1.60, 95% CI 1.32 to 1.94), whereas creatinine levels appeared associated with lower risk (hazard ratio 0.73, 95% CI 0.57 to 0.95). CONCLUSIONS: Cystatin-C is a stronger predictor of mortality than creatinine in elderly persons with HF. If confirmed in future studies, this new marker of renal function could improve risk stratification in patients with HF.

Age Factors↗
PubMed2006

Checking the conformational stability of cystatin C and its L68Q variant by molecular dynamics studies: why is the L68Q variant amyloidogenic?

Human L68Q cystatin C is one of the known human amyloidogenic proteins. In its native state it is a monomer with alpha/beta structure. Experimental evidence suggests that L68Q variant associates into dimeric intermediates and that the dimers subsequently self-assemble to form amyloid deposits and insoluble fibrils. Details of the pathway of L68Q mutant amyloid formation are unclear; however, different experimental approaches with resolutions at molecular level have provided some clues. Probably, the stability and flexibility of monomeric L68Q variant play essential roles in the early steps of amyloid formation; thus, it is necessary to characterize early conformational changes of L68Q cystatin C monomers. In this paper, we demonstrate the possibility that the differences between the monomeric forms of wild-type (wt) cystatin C and its L68Q variant are responsible for higher tendency of the L68Q cystatin C amyloidogenesis. We started our studies with the simulations of wt and L68Q cystatin C monomers. Nanosecond time scale molecular dynamics simulations at 308K were performed using AMBER7.0 program. The results show that the structure of the L68Q monomer was changed, relative to the wt cystatin C structure. The results support earlier speculation that the L68Q point mutation would easily lead to dimer formation.

Amino Acid Substitution↗
PubMed2005

Cystatin C modulates neurodegeneration and neurogenesis following status epilepticus in mouse.

Brain damaging insults cause alterations in neuronal networks that trigger epileptogenesis, and eventually lead to the appearance of spontaneous seizures. The present experiments were designed to study the cellular expression and functions of a cysteine proteinase inhibitor, cystatin C, whose gene expression is previously shown to be upregulated in the rat hippocampus during status epilepticus (SE)-induced epileptogenesis. The present data showed that the expression of cystatin C protein increased in the mouse hippocampus 7 days following SE and localized mainly to astrocytes and microglia. Acute neuronal death in the hippocampus at 24 h after SE was reduced in cystatin C-/- mice. Also, the basal level of neurogenesis in the subgranular layer of dentate gyrus was decreased in cystatin C-/- mice compared to wildtype littermates. Interestingly, migration of newly born neurons within the granule cell layer was attenuated in cystatin C-/- mice. These data demonstrate that cystatin C has a role in neuronal death and neurogenesis during SE-induced network reorganization.

Animals↗
PubMedDate not supplied

Serum cystatin C as an index of renal function in kidney transplant patients.

Management of renal transplant patients requires periodic measurement of renal function, which is usually assessed by measuring the glomerular filtration rate (GFR). The most commonly used marker for GFR is serum creatinine, although muscle wasting and tubular secretion may lead to overestimation of the actual GFR. Serum concentrations of the low-molecular-weight proteins, cystatin C and beta(2)-microglobulin (B(2)M), may afford useful markers to determine a reduced GFR. We investigated whether these molecules provide reliable indicators of renal function in 75 renal transplant patients. Cystatin C and B(2)M correlated significantly with creatinine (r =.648, P <.05 and r =.578, P <.05, respectively). Inverse serum creatinine was superior to inverse cystatin C and inverse B(2)M when renal function equations were used (r =.95, P <.05, according to MDRD; r =.87, P <.05, according to Cockroft-Gault). Receiver operating characteristic (ROC) analysis was performed to quantitate the accuracy of the different markers to detect reduced GFR using a cutoff value of 70 mL/min. No significant difference between the areas under the ROC curves comparing cystatin C and B(2)M was observed; however, serum creatinine demonstrated a significantly greater value than cystatin C (.981 vs.724, P =.001). We conclude that serum creatinine is a more efficacious marker than serum cystatin C to assess renal function.

Adult↗
PubMed2002

Relationship between serum cystatin C and creatinine in kidney and liver transplant patients.

BACKGROUND: The results obtained for serum cystatin C, which has been proposed as a novel marker of glomerular filtration rate (GFR), in kidney and liver transplant are still very limited. In our study, the relationship between serum cystatin C and creatinine in kidney and liver transplant patients was investigated. METHODS: Serum cystatin C and creatinine concentrations were determined in 182 samples from 52 kidney transplant patients and 71 samples from 28 liver transplant patients at 1-9870 days post-transplantation time. Eighty-seven serum samples from 66 patients with different types of chronic kidney disease were also analysed. RESULTS: The serum creatinine (r=-0.517, p<0.001) and cystatin C (r=-0.409, p<0.001) concentrations were negatively correlated with the post-transplantation time in the kidney transplant patients. In the liver transplant patients, the correlation between these variables is not statistically significant. The creatinine/cystatin C ratio in the liver transplant group is significantly lower than in the other group of patients (p<0.001). This ratio in the kidney transplant patients groups is significantly lower than in the kidney disease group (p<0.001). In the kidney transplant patients the creatinine/cystatin C ratio and the post-transplantation time were negatively correlated (r=-0.523, p<0.001); however, in the liver transplant patients the correlation between these variables was not significant. CONCLUSIONS: In the groups of kidney disease and kidney transplant patients, as renal function decreases, there is an increase in the creatinine/cystatin C ratio. This may be due to the fact that, since creatinine is eliminated by glomerular filtration and tubular secretion, as renal function is impaired, its serum concentration increases to a greater extent than that of cystatin C, which is only eliminated by glomerular filtration. In the liver transplant patients, the creatinine/cystatin C ratio is lower than in the other groups. This may be due to better preserved renal function, lower muscular mass and a reduced rate of creatine formation and creatinine production in some of these patients. The serum cystatin C would be a better GFR marker than the widely used creatinine in liver transplant patients.

Adult↗
PubMed2002

Salivary cystatins induce interleukin-6 expression via cell surface molecules in human gingival fibroblasts.

Recently, family 2 cystatins have been demonstrated to upregulate interleukin-6 (IL-6) production by human gingival fibroblasts [Biol. Chem. 381 (2000) 1143]. To elucidate the mechanism of the IL-6 inducing activity of cystatins, we tested NF-kappa B activation with salivary cystatins SA1 and SA2-stimulated human gingival fibroblast whole cell lysates. The IL-6 production by human fibroblasts in response to these cystatins was inhibited by tyrosine kinase inhibitors and an inhibitor of NF-kappa B activation. The IL-6 inducing activity of the cystatins was depressed by the anti-CD58 monoclonal antibody. These findings supply evidence that cystatins SA1 and SA2 adhere to human fibroblasts and that the event results in tyrosine phosphorylation and upregulation of the release of IL-6 mediated enhancement of NF-kappa B activity.

Cell Line↗
PubMed1997

Molecular cloning and N-terminal analysis of bovine cystatin C. Identification of a full-length N-terminal region.

The N-terminal region of human cystatin C has been shown to be of crucial importance for the interaction of the inhibitor with cysteine proteinases. However, several studies have been unable to identify the corresponding region in bovine cystatin C, indicating that the binding of proteinases to the bovine inhibitor may not be dependent on this region. With the aim to resolve this apparent discrepancy and to elucidate the relation of bovine cystatin C to other cystatins, we have isolated a cDNA clone encoding bovine precystatin C. The sequence of this cDNA was similar to that of the human inhibitor and showed a putative signal peptidase cleavage site consistent with the N-terminal regions of the bovine and human inhibitors being of comparable size. This suggestion was verified by determination of the relative molecular mass of the mature bovine inhibitor isolated from cerebrospinal fluid under conditions minimising proteolysis. The N-terminal of the purified inhibitor was blocked, but the sequence of the N-terminal peptide produced by digestion with endopeptidase LysC could be unequivocally determined by tandem mass spectroscopy. Together, these results show that bovine cystatin C has 118 residues, in contrast with 110-112 residues reported previously, and has an N-terminal region analogous to that of human cystatin C. This region presumably is of similar importance for tight binding of target proteinases as in the human inhibitor.

Amino Acid Sequence↗
PubMed2000

Autonomic regulation of cystatin S gene expression in rat submandibular glands.

Innervation of rat submandibular and parotid glands by the autonomic nervous system regulates saliva volume, its rate of secretion and its composition. The autonomic nervous system also plays a regulatory role in the differentiation and growth of salivary glands, and in the expression of specific sets of genes. Rat cystatin S, a member of family 2 of the cysteine proteinase inhibitor superfamily, is expressed in submandibular and parotid glands of human and rat. In the rat, cystatin S gene expression is tissue- and cell type-specific, is temporally regulated during postnatal development, and not observed in adult animals. The beta-adrenergic agonist isoproterenol (IPR) induces hypertrophic and hyperplastic enlargements of rat salivary glands and the expression of a number of genes including cystatin S. Sympathectomy reduces, but does not completely block, IPR-induced expression of the cystatin S gene in submandibular glands of adult female rats, indicating the participation of sympathetic factor(s) in its regulation. Bilateral parasympathectomy also reduces IPR-induced cystatin S gene expression, suggesting a role of the parasympathetic nervous system in its regulation. Experiments described in this paper suggest that similar factor(s) arising from both the sympathetic and parasympathetic branches of the autonomic nervous system simultaneously participate in IPR-induced cystatin S gene expression in submandibular glands.

Animals↗
PubMed1995

Serum cystatin C measured by automated immunoassay: a more sensitive marker of changes in GFR than serum creatinine.

Serum cystatin C has been suggested as a new marker of GFR. For the introduction of this marker into clinical use a rapid and automated method is required. We have developed and validated an assay for serum cystatin C using latex particle-enhanced immunoturbidimetry. Intra- and inter-assay precision were < 3% and < 5% across the assay range. Analytical recovery was 93 +/- 3.8% and no lack of parallelism was demonstrated. Regression analysis of a method comparison with an enzyme-enhanced radial-immunodiffusion method, gave PETIA = 0.074 + 0.93 x SRID, r = 0.98, N = 100. Inter-assay precision profiles showed cystatin C was measured with two-fold better precision than creatinine on the same analyzer. Cystatin C measurement was neither interfered with by icterus nor by hemolysis. 1/cystatin C versus 1/creatinine concentrations gave r = 0.67, N = 469. Comparison of Cr EDTA GFR with 1/cystatin C and 1/creatinine gave r = 0.81 and 0.50, respectively, N = 206. Calculating diagnostic sensitivity for abnormal GFR showed cystatin C to be significantly (P < 0.05) more sensitive than creatinine (71.4 vs. 52.4%). Cystatin C measurement using PETIA technology can be automated on the same instruments used routinely for the measurement of creatinine and offers better analytical performance and probably improved clinical sensitivity as a screening test for early renal damage.

Biomarkers↗
PubMed1994

Local pH-dependent conformational changes leading to proteolytic susceptibility of cystatin C.

Cystatin C, a cysteine protease inhibitor, was subject to hydrolysis at two sites when complexed with papain and in the presence of excess papain. A pH-dependent cleavage at His-86 increases Asp-87 was observed, as well as a pH-independent one at Gly-4 increases Lys-5. His-86 increases Asp-87 hydrolysis increased with decreasing pH and was characterized kinetically. It could be described by a single ionization with pKa = 3.4 +/- 0.2 and (kcat./Km)max. = 1.4 (+/- 0.4) x 10(4) M-1.s-1 at I = 0.3 M. C.d. spectroscopy, also at I = 0.3 M, demonstrated a conformational change with pKa = 3.2 +/- 0.2, indicating that the pH-dependence of hydrolysis was due to a conformational change in cystatin C. At I = 0.15 M, the pKa of the conformational change observed by c.d. shifted to 4.1 +/- 0.1. This indicates that at physiological ionic strength of 0.15 M, a significant proportion of cystatin C complexed with protease would be in a proteolytically labile conformation over the pH range 4.5 to 5, which is encountered in lysosomes. This may constitute a mechanism for clearing inappropriately localized cystatins. A pH-dependent conformational variability in this region of the inhibitor could explain the differences in the X-ray crystallographic and n.m.r. structures of the homologous chicken cystatin. The ionic-strength dependence of ionization indicates a hydrophobic stabilization of the ionizable group. The lack of pH-dependence of hydrolysis at Gly-4 increases Lys-5, with kcat./Km = 220 +/- 41 M-1.s-1 in the pH range 3.89 to 7.96 was unexpected in light of the normal, bell-shaped pH-dependence of papain-catalysed hydrolyses. This may reflect a different rate-limiting step of cystatin C hydrolysis.

Amino Acid Sequence↗