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the 3rd letter of the Roman alphabet (同)c
(music) the keynote of the scale of C major
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carbonの化学記号
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/08/17 12:58:31」(JST)

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Cystatin C or cystatin 3 (formerly gamma trace, post-gamma-globulin or neuroendocrine basic polypeptide),^[3] a protein encoded by the CST3 gene, is mainly used as a biomarker of kidney function. Recently, it has been studied for its role in predicting new-onset or deteriorating cardiovascular disease. It also seems to play a role in brain disorders involving amyloid (a specific type of protein deposition), such as Alzheimer's disease. In humans, all cells with a nucleus (cell core containing the DNA) produce cystatin C as a chain of 120 amino acids. It is found in virtually all tissues and body fluids. It is a potent inhibitor of lysosomal proteinases (enzymes from a special subunit of the cell that break down proteins) and probably one of the most important extracellular inhibitors of cysteine proteases (it prevents the breakdown of proteins outside the cell by a specific type of protein degrading enzymes). Cystatin C belongs to the type 2 cystatin gene family.

Role in medicine

Kidney function

Glomerular filtration rate (GFR), a marker of kidney health, is best measured by injecting compounds such as inulin, radioisotopes such as ⁵¹chromium-EDTA, ¹²⁵I-iothalamate, ^99mTc-DTPA or radiocontrast agents such as iohexol, but these techniques are complicated, costly, time-consuming and have potential side-effects.^[4]^[5] Creatinine is the most widely used biomarker of kidney function. It is inaccurate at detecting mild renal impairment, and levels can vary with muscle mass but not with protein intake. Urea levels might change with protein intake.^[6] Formulas such as the Cockcroft and Gault formula and the MDRD formula (see Renal function) try to adjust for these variables.

Cystatin C has a low molecular weight (approximately 13.3 kilodaltons), 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. Serum levels of cystatin C are a more precise test of kidney function (as represented by the glomerular filtration rate, GFR) than serum creatinine levels.^[5]^[7] This finding is based mainly on cross-sectional studies (on a single point in time). Longitudinal studies (that follow cystatin C over time) are scarcer; some studies show promising results.^[8]^[9]^[10] Cystatin C levels are less dependent on age, sex, race and muscle mass compared to creatinine. Cystatin C measurements alone have not been shown to be superior to formula-adjusted estimations of kidney function.^[11] As opposed to previous claims, cystatin C has been found to be influenced by body composition.^[12]^[13] It has been suggested that cystatin C might predict the risk of developing chronic kidney disease, thereby signaling a state of 'preclinical' kidney dysfunction.^[14]

Studies have also investigated cystatin C as a marker of kidney function in the adjustment of medication dosages.^[15]^[16]

Cystatin C levels have been reported to be altered in patients with cancer,^[17]^[18]^[19] (even subtle) thyroid dysfunction^[20]^[21]^[22] and glucocorticoid therapy in some^[23]^[24] but not all^[25] situations. Other reports have found that levels are influenced by cigarette smoking and levels of C-reactive protein.^[26] Levels seem to be increased in HIV infection, which might or might not reflect actual renal dysfunction.^[27]^[28]^[29] The role of cystatin C to monitor GFR during pregnancy remains controversial.^[30]^[31] Like creatinine, the elimination of cystatin C via routes other than the kidney increase with worsening GFR.^[32]

Death and cardiovascular disease

Kidney dysfunction increases the risk of death and cardiovascular disease.^[33]^[34] Several studies have found that increased levels of cystatin C are associated with the risk of death, several types of cardiovascular disease (including myocardial infarction, stroke, heart failure, peripheral arterial disease and metabolic syndrome) and healthy aging.^{[citation needed]}^{[clarification needed]} Some studies have found cystatin C to be better in this regard than serum creatinine or creatinine-based GFR equations.^[35]^[36]^[37]^[38]^[39]^[40]^[41]^[42]^[43]^[44]^[45]^[46] Because the association of cystatin C with long term outcomes has appeared stronger than what could be expected for GFR, it has been hypothesized that cystatin C might also be linked to mortality in a way independent of kidney function.^[47] In keeping with its housekeeping gene properties, it has been suggested that cystatin C might be influenced by the basal metabolic rate.^[48]

Neurologic disorders

Mutations in the cystatin 3 gene are responsible for the Icelandic type of hereditary cerebral amyloid angiopathy, a condition predisposing to intracerebral haemorrhage, stroke and dementia.^[49]^[50] The condition is inherited in a dominant fashion.

Since cystatin 3 also binds amyloid β and reduces its aggregation and deposition, it is a potential target in Alzheimer's disease.^[51]^[52] Although not all studies have confirmed this, the overall evidence is in favor of are role for CST3 as a susceptibility gene for Alzheimer's disease.^[53] Cystatin C levels have been reported to be higher in subjects with Alzheimer's disease.^[54]

The role of cystatin C in multiple sclerosis and other demyelinating diseases (characterized by a loss of the myelin nerve sheath) remains controversial.^[55]

Other roles

Cystatin C levels are decreased in atherosclerotic (so-called 'hardening' of the arteries) and aneurysmal (saccular bulging) lesions of the aorta.^[56]^[57]^[58]^[59] Genetic and prognostic studies also suggest a role for cystatin C.^[60]^[61] Breakdown of parts of the vessel wall in these conditions is thought to result from an imbalance between proteinases (cysteine proteases and matrix metalloproteinases, increased) and their inhibitors (such as cystatin C, decreased).

A few studies have looked at the role of cystatin C or the CST3 gene in age-related macular degeneration.^[62]^[63] Cystatin C has also been investigated as a prognostic marker in several forms of cancer.^[64]^[65] Its role in pre-eclampsia remains to be confirmed.^[66]^[67]^[68]^[69]

Laboratory measurement

Cystatin C can be measured in a random sample of serum (the fluid in blood from which the red blood cells and clotting factors have been removed) using immunoassays such as nephelometry or particle-enhanced turbidimetry.^[70] It is a more expensive test than serum creatinine (around $2 or $3, compared to $0.02 to $0.15), which can be measured with a Jaffé reaction.^[71]^[72]^[73]

Reference values differ in many populations and with sex and age. Across different studies, the mean reference interval (as defined by the 5th and 95th percentile) was between 0.52 and 0.98 mg/L. For women, the average reference interval is 0.52 to 0.90 mg/L with a mean of 0.71 mg/L. For men, the average reference interval is 0.56 to 0.98 mg/L with a mean of 0.77 mg/L.^[70] The normal values decrease until the first year of life, remaining relatively stable before they increase again, especially beyond age 50.^[74]^[75]^[76] Creatinine levels increase until puberty and differ according to gender from then on, making their interpretation problematic for pediatric patients.^[75]^[77]

In a large study from the United States National Health and Nutrition Examination Survey, the reference interval (as defined by the 1st and 99th percentile) was between 0.57 and 1.12 mg/L. This interval was 0.55 - 1.18 for women and 0.60 - 1.11 for men. Non-Hispanic blacks and Mexican Americans had lower normal cystatin C levels.^[74] Other studies have found that in patients with an impaired renal function, women have lower and blacks have higher cystatin C levels for the same GFR.^[11] For example, the cut-off values of cystatin C for chronic kidney disease for a 60-year-old white women would be 1.12 mg/L and 1.27 mg/L in a black man (a 13% increase). For serum creatinine values adjusted with the MDRD equation, these values would be 0.95 mg/dL to 1.46 mg/dL (a 54% increase).^[78]

Based on a threshold level of 1.09 mg/L (the 99th percentile in a population of 20- to 39-year-olds without hypertension, diabetes, microalbuminuria or macroalbuminuria or higher than stage 3 chronic kidney disease), the prevalence of increased levels of cystatin C in the United States was 9.6% in subjects of normal weight, increasing in overweight and obese individuals.^[79] In Americans aged 60 and 80 and older, serum cystatin is increased in 41% and more than 50%.^[74]

Molecular biology

The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions, where they appear to provide protective functions. The cystatin locus on the short arm of chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes.

The CST3 gene is located in the cystatin locus and comprises 3 exons (coding regions, as opposed to introns, non-coding regions within a gene), spanning 4.3 kilo-base pairs. It encodes the most abundant extracellular inhibitor of cysteine proteases. It is found in high concentrations in biological fluids and is expressed in virtually all organs of the body (CST3 is a housekeeping gene). The highest levels are found in semen, followed by breastmilk, tears and saliva. The hydrophobic leader sequence indicates that the protein is normally secreted. There are three polymorphisms in the promoter region of the gene, resulting in two common variants.^[80] Several single nucleotide polymorphisms have been associated with altered cystatin C levels.^[81]

Cystatin C is a non-glycosylated, basic protein (isoelectric point at pH 9.3). The crystal structure of cystatin C is characterized by a short alpha helix and a long alpha helix which lies across a large antiparallel, five-stranded beta sheet. Like other type 2 cystatins, it has two disulfide bonds. Around 50% of the molecules carry a hydroxylated proline. Cystatin C forms dimers (molecule pairs) by exchanging subdomains; in the paired state, each half is made up of the long alpha helix and one beta strand of one partner, and four beta strands of the other partner.^[82]

History

Cystatin C was first described as 'gamma-trace' in 1961 as a trace protein together with other ones (such as beta-trace) in the cerebrospinal fluid and in the urine of patients with renal failure.^[83] Grubb and Löfberg first reported its amino acid sequence.^[83] They noticed it was increased in patients with advanced renal failure.^[84] It was first proposed as a measure of glomerular filtration rate by Grubb and coworkers in 1985.^[85]^[86]

Use of serum creatinine and cystatin C was found very effective in accurately reflecting the GFR in a study reported in the July 5, 2012 issue of the New England Journal of Medicine.

Footnotes

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^ "Mouse PubMed Reference:".
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^ Lamb EJ, O'Riordan SE, Webb MC, Newman DJ (November 2003). "Serum cystatin C may be a better marker of renal impairment than creatinine". J Am Geriatr Soc. 51 (11): 1674–1675. doi:10.1046/j.1532-5415.2003.515244.x. PMID 14687406.
^ Peake M, Whiting M (November 2006). "Measurement of serum creatinine - current status and future goals". Clin Biochem Rev. 27 (4): 173–84. PMC 1784008. PMID 17581641.
^ Myers GL, Miller WG, Coresh J, et al. (January 2006). "Recommendations for improving serum creatinine measurement: a report from the Laboratory Working Group of the National Kidney Disease Education Program". Clin. Chem. 52 (1): 5–18. doi:10.1373/clinchem.2005.0525144. PMID 16332993.
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External links

Cystatin: a protein that flips out! QUite Interesting PDB Structure article at PDBe
The MEROPS online database for peptidases and their inhibitors: I25.004

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. 腎機能の評価 assessment of kidney function
2. アミロイド疾患の遺伝的要因 genetic factors in the amyloid diseases
3. 老化する腎臓 the aging kidney
4. 心腎症候群：予後および治療 cardiorenal syndrome prognosis and treatment
5. 成人における慢性腎臓病の定義および病期分類 definition and staging of chronic kidney disease in adults

English Journal

Combined biomarkers evaluation for diagnosing kidney injury in preeclampsia.

Xiao J, Niu J, Ye X, Yu Q, Gu Y.SourceDivision of Nephrology, The Fifth People's Hospital of Shanghai, Fudan University , Shanghai , People's Republic of China .
Hypertension in pregnancy : official journal of the International Society for the Study of Hypertension in Pregnancy.Hypertens Pregnancy.2013 Nov;32(4):439-49. doi: 10.3109/10641955.2013.827203. Epub 2013 Aug 19.
Objective: To identify novel potential biomarkers and evaluate combined biomarkers for diagnosing kidney injury with considerable accuracy in preeclampsia. Methods: The level of serum and urine neutrophil gelatinase-associated lipocalin (NGAL), kidney injury molecule-1 (KIM-1), retinol-binding prote
PMID 23957217

Renal biomarkers predict nephrotoxicity after paraquat.

Wunnapuk K, Liu X, Peake P, Gobe G, Endre Z, Grice JE, Roberts MS, Buckley NA.SourceTherapeutics Research Centre, School of Medicine, The University of Queensland, Brisbane, QLD, Australia; Department of Forensic Medicine, Faculty of Medicine, Chiang Mai University, Chiang Mai, Thailand.
Toxicology letters.Toxicol Lett.2013 Oct 9;222(3):280-8. doi: 10.1016/j.toxlet.2013.08.003. Epub 2013 Aug 14.
Paraquat is a widely used herbicide which has been involved in many accidental and intentional deaths. Nephrotoxicity is common in severe acute paraquat poisoning. We examined seven renal injury biomarkers, including cystatin-C, kidney injury molecule-1, β2-microglobulin, clusterin, albumin, neutro
PMID 23954200

Impact of Cystatin C and RIFLE on Renal Function Assessment After Cardiac Surgery.

Magro MC, Vattimo Mde F.Source1University of Brasilia, Brasilia, DF, Brazil.
Biological research for nursing.Biol Res Nurs.2013 Oct;15(4):451-8. doi: 10.1177/1099800412446742. Epub 2012 May 24.
The lack of a consensus classification system and of a specific, sensitive, and early-stage biomarker for kidney injury frequently results in late diagnosis of acute kidney injury (AKI). The aim of the present study was to characterize the discriminatory power of cystatin C and the RIFLE and Acute K
PMID 22626587

Japanese Journal

クレアチニンとシスタチンCによる小児の年齢と腎機能評価 (成長と臨床検査値)

上村治
臨床検査 56(5), 476-482, 2012-05
NAID 40019292522

ラテックス凝集反応により測定した犬の血漿シスタチンC濃度の有用性の検討

宮川優一
日本獣医生命科学大学研究報告 (60), 29-32, 2011-12
NAID 40019203166

Related Pictures

★リンクテーブル★

リンク元	「シスタチンC」
関連記事	「C」「Cs」「cystatin」「Cd」「c」

「シスタチンC」

CST3
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1G96, 1R4C, 1TIJ, 3GAX, 3NX0, 3PS8, 3QRD, 3S67, 3SVA
Identifiers
Aliases	CST3, ARMD11, HEL-S-2, cystatin C
External IDs	OMIM: 604312 MGI: 102519 HomoloGene: 78 GeneCards: 1471
Gene ontology
Molecular function	• peptidase inhibitor activity; • cysteine-type endopeptidase inhibitor activity; • beta-amyloid binding; • protease binding; • protein binding; • identical protein binding; • endopeptidase inhibitor activity;
Cellular component	• cytoplasm; • multivesicular body; • vesicle; • cell projection; • nuclear membrane; • extracellular space; • extracellular region; • basement membrane; • axon; • neuronal cell body; • endoplasmic reticulum; • perinuclear region of cytoplasm; • contractile fiber; • lysosome; • extracellular exosome; • extracellular matrix;
Biological process	• eye development; • negative regulation of proteolysis; • cellular protein metabolic process; • regulation of programmed cell death; • defense response; • negative regulation of peptidase activity; • response to estradiol; • male gonad development; • response to hypoxia; • response to organic cyclic compound; • circadian sleep/wake cycle, REM sleep; • negative regulation of extracellular matrix disassembly; • regulation of tissue remodeling; • negative regulation of cell death; • Sertoli cell development; • response to oxidative stress; • cell activation; • negative regulation of blood vessel remodeling; • positive regulation of DNA replication; • salivary gland development; • brain development; • negative regulation of elastin catabolic process; • response to nutrient levels; • response to axon injury; • positive regulation of cell proliferation; • response to inorganic substance; • cellular response to oxidative stress; • extracellular fibril organization; • response to carbohydrate; • response to toxic substance; • embryo implantation; • response to drug; • negative regulation of collagen catabolic process; • cellular response to hydrogen peroxide; • apoptotic process; • negative regulation of endopeptidase activity;
	Sources:Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	1471
	13010
	ENSG00000101439
	ENSMUSG00000027447
	P01034
	P21460
	NM_001288614; NM_000099
	NM_009976
	NP_000090.1; NP_001275543.1
	NP_034106.2
	Wikidata
View/Edit Human	View/Edit Mouse

　　[★]

英: cystatin C, post-γ-globulin, γ-trace

「C」

　　[★]

炭素 carbon
シトシン cytosine
システイン cysteine
シチジン
セルシウス度摂氏 degrees Celsius degree C
産婦人科領域で「子宮外頚子宮外頚部 exocervix」を表現するための略語

「Cs」

　　[★] セシウム, caesium, cesium 　

「cystatin」

　　[★]

シスタチン

関: oryzacystatin

「Cd」

　　[★] カドミウム

関: cadmium

「c」

　　[★]

光速, speed of light

[1] "Human PubMed Reference:".

[2] "Mouse PubMed Reference:".

[Alzforum-3] "Alzforum: AlzGene".

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[pmid9836733-19] Kos J, Stabuc B, Cimerman N, Brünner N (December 1998). "Serum cystatin C, a new marker of glomerular filtration rate, is increased during malignant progression". Clin. Chem. 44 (12): 2556–7. PMID 9836733.

[pmid12675875-20] Fricker M, Wiesli P, Brändle M, Schwegler B, Schmid C (May 2003). "Impact of thyroid dysfunction on serum cystatin C". Kidney Int. 63 (5): 1944–1947. doi:10.1046/j.1523-1755.2003.00925.x. PMID 12675875.

[pmid15966508-21] Manetti L, Pardini E, Genovesi M, et al. (April 2005). "Thyroid function differently affects serum cystatin C and creatinine concentrations". J. Endocrinol. Invest. 28 (4): 346–9. doi:10.1007/bf03347201. PMID 15966508.

[pmid14637271-22] Wiesli P, Schwegler B, Spinas GA, Schmid C (December 2003). "Serum cystatin C is sensitive to small changes in thyroid function". Clin. Chim. Acta. 338 (1–2): 87–90. doi:10.1016/j.cccn.2003.07.022. PMID 14637271.

[pmid11673383-23] Risch L, Herklotz R, Blumberg A, Huber AR (November 2001). "Effects of glucocorticoid immunosuppression on serum cystatin C concentrations in renal transplant patients". Clin. Chem. 47 (11): 2055–9. PMID 11673383.

[pmid10958865-24] Cimerman N, Brguljan PM, Krasovec M, Suskovic S, Kos J (October 2000). "Serum cystatin C, a potent inhibitor of cysteine proteinases, is elevated in asthmatic patients". Clin. Chim. Acta. 300 (1–2): 83–95. doi:10.1016/S0009-8981(00)00298-9. PMID 10958865.

[pmid12089191-25] Bökenkamp A, van Wijk JA, Lentze MJ, Stoffel-Wagner B (July 2002). "Effect of corticosteroid therapy on serum cystatin C and beta2-microglobulin concentrations". Clin. Chem. 48 (7): 1123–6. PMID 12089191.

[pmid15086483-26] Knight EL, Verhave JC, Spiegelman D, et al. (April 2004). "Factors influencing serum cystatin C levels other than renal function and the impact on renal function measurement". Kidney Int. 65 (4): 1416–1421. doi:10.1111/j.1523-1755.2004.00517.x. PMID 15086483.

[pmid17998494-27] Odden MC, Scherzer R, Bacchetti P, et al. (November 2007). "Cystatin C level as a marker of kidney function in human immunodeficiency virus infection: the FRAM study". Arch. Intern. Med. 167 (20): 2213–2219. doi:10.1001/archinte.167.20.2213. PMC 3189482. PMID 17998494.

[pmid1569212-28] Collé A, Tavera C, Prévot D, et al. (1992). "Cystatin C levels in sera of patients with human immunodeficiency virus infection. A new avidin-biotin ELISA assay for its measurement". J Immunoassay. 13 (1): 47–60. doi:10.1080/15321819208019824. PMID 1569212.

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cystatin C