Cystatiini C hyödynnetään munuaistutkimuksissa , CST3( 20p11.21), ARMD11, HEL-S-2.

https://lakemedelsboken.se/kapitel/nefrologi-urologi/skattning-av-njurfunktion.html

Yleistä  http://oyslab.fi/ohjekirja/1887.html

Sitaatti:  "Kystatiini C on emäksinen pienimolekyylinen (mp 13 000) proteiini, jonka fysiologisena tehtävänä on inhiboida kysteiiniproteaaseja. Kaikki elimistön tumalliset solut tuottavat kystatiini C:tä tasaisella nopeudella, se ei ole akuutin faasin proteiini, eivätkä lihasmassa, sukupuoli ja ravinto vaikuta sen seerumi/plasmapitoisuuteen. Kystatiini C eliminoituu lähes täysin glomerulussuodokseen, josta proksimaalisen tubuluksen solut sen reabsorboivat ja hajottavat. Kystatiini C:n ominaisuudet tekevät siitä kreatiniinia paremman glomerulusfunktion merkkiaineen".

Kystatiini C- geeni (PubMed haku 20.6. 2019)

https://www.ncbi.nlm.nih.gov/gene/1471

Official Symbol

CST3

Official Full Name

cystatin C

Also known as

ARMD11; HEL-S-2

Summary

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
•  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 chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in the cystatin locus and encodes the most abundant extracellular inhibitor of cysteine proteases, which is found in high concentrations in biological fluids and is expressed in virtually all organs of the body. A mutation in this gene has been associated with amyloid angiopathy. 

 Expression of this protein in vascular wall smooth muscle cells is severely reduced in both atherosclerotic and aneurysmal aortic lesions, establishing its role in vascular disease. In addition, this protein has been shown to have an antimicrobial function, inhibiting the replication of herpes simplex virus. Alternative splicing results in multiple transcript variants encoding a single protein. [provided by RefSeq, Nov 2014]

Expression

Ubiquitous expression in brain (RPKM 148.6), salivary gland (RPKM 118.0) and 25 other tissues See more

Orthologs mouse all

Preferred Names

cystatin-C

Names

bA218C14.4 (cystatin C)

cystatin 3

epididymis secretory protein Li 2    (HEL-S-2)

gamma-trace

neuroendocrine basic polypeptide

post-gamma-globulin

Conserved Domains (1) summary

smart00043
Location:34 → 144

CY; Cystatin-like domain. Cystatins are a family of cysteine protease inhibitors that occur mainly as single domain proteins. However some extracellular proteins such as kininogen, His-rich glycoprotein and fetuin also contain these domains.

FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.21"
     Protein         1..146
                     /product="cystatin-C precursor"
                     /note="cystatin 3; gamma-trace; post-gamma-globulin;
                     neuroendocrine basic polypeptide; bA218C14.4 (cystatin C);
                     epididymis secretory protein Li 2"
                     /calculated_mol_wt=13347
     sig_peptide     1..26
                     /calculated_mol_wt=2470
     mat_peptide     27..146
                     /product="cystatin-C"
                     /experiment="DESCRIPTION:antimicrobial
                     peptide[PMID:2153254]"
                     /calculated_mol_wt=13347
     Region          34..144
                     /region_name="CY"
                     /note="Cystatin-like domain; smart00043"
                     /db_xref="CDD:214484"
     Site            order(37,81..83,85)
                     /site_type="other"
                     /note="putative proteinase inhibition site"
                     /db_xref="CDD:238002"
     CDS             1..146
                     /gene="CST3"
                     /gene_synonym="ARMD11; HEL-S-2"
                     /coded_by="NM_000099.4:94..534"
                     /db_xref="CCDS:CCDS13158.1"
                     /db_xref="GeneID:1471"
                     /db_xref="HGNC:HGNC:2475"
                     /db_xref="MIM:604312"
ORIGIN      
        1 magplrapll llailavala vspaagsspg kpprlvggpm dasveeegvr raldfavgey
       61 nkasndmyhs ralqvvrark qivagvnyfl dvelgrttct ktqpnldncp fhdqphlkrk
      121 afcsfqiyav pwqgtmtlsk stcqda
//

Related articles in PubMed

1. Correlations of serum cystatin C level and gene polymorphism with vascular cognitive impairment after acute cerebral infarction. Zeng Q, et al. Neurol Sci, 2019 May. PMID 30805744
2. Baseline Serum Cystatin C Is a Potential Predictor for Acute Kidney Injury in Patients with Acute Pancreatitis. Chai X, et al. Dis Markers, 2018. PMID 30581500, Free PMC Article
3. Serum Cystatin C Levels in Twin Pregnancy versus Singleton Pregnancy. Peng J, et al. Lab Med, 2019 Apr 8. PMID 30517681
4. Cystatin C as an index of acute cerebral infraction recurrence: one-year follow-up study. Dong X, et al. Int J Neurosci, 2019 Jan. PMID 30033802
5. Association of maternal uric acid and cystatin C serum concentrations with maternal and neonatal cardiovascular risk markers and neonatal body composition: The Ulm SPATZ Health Study. Rothenbacher D, et al. PLoS One, 2018. PMID 30024915, Free PMC Article

See all (507) citations in PubMed

See citations in PubMed for homologs of this gene provided by HomoloGene

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

1. A high serum cystatin C level and CST3 B allele may be risk factors for vascular cognitive impairment after acute cerebral infarction.
2. In patients with STEMI treated by primary PCI, plasma NGAL and cystatin C did not provide additional value regarding contrast induced-acute kidney injury prediction compared with known risk factors such as baseline creatinine.
3. Studied serum levels of Cystatin C in singleton and twin pregnancies, both with and without preeclampsia.
4. the relationships of cystatin C-based glomerular filtration rate (eGFRcys) and creatinine-based GFR (eGFRcr), as well as their ratio with occurrence of osteoporotic fracture in postmenopausal osteoporotic women, were examined.
5. Study showed that serum cystatin C level is an independent prediction biomarker for acute cerebral infarction (ACI) recurrence.
6. he similarities between melanoma brain metastasis and stroke with respect to CysC expression by and secretion from microglia cells suggest that CysC may be involved in shared pathways between brain metastasis and post-stroke regeneration. This manifests the tendency of tumor cells to highjack physiological molecular pathways in their progression
7. Serum cystatin C and urinary NGAL were found to be predictors of long-term mortality in high-risk patients undergoing percutaneous mitral valve repair.
8. Serum cystatin C level was associated with acute kidney injury in patients with acute pancreatitis.
9. Serum Cys C is a good marker for detecting AKI [acute kidney injury] in liver cirrhosis, and the different levels of increase in Cys C may be useful in differentiating the different types of AKI.
10. Cystatin C plays immune regulatory roles at both cellular and molecular levels including antigen presentation, secretion of cytokines, synthesis of nitric oxide and apoptosis [Review].

Submit: New GeneRIF Correction See all GeneRIFs (436)

 

• Metalloproteinaasien  ADAM10/ADAM17 degradomi hajoittaa C-cystiinin:

Cell Mol Life Sci. 2019 Jun 17. doi: 10.1007/s00018-019-03184-4. [Epub ahead of print]

Degradome of soluble ADAM10 and ADAM17 metalloproteases.

Scharfenberg F¹, Helbig A²et al. Abstract

Disintegrin and metalloproteinases (ADAMs) 10 and 17 can release the extracellular part of a variety of membrane-bound proteins via ectodomain shedding important for many biological functions. So far, substrate identification focused exclusively on membrane-anchored ADAM10 and ADAM17. However, besides known shedding of ADAM10, we identified ADAM8 as a protease capable of releasing the ADAM17 ectodomain. Therefore, we investigated whether the soluble ectodomains of ADAM10/17 (sADAM10/17) exhibit an altered substrate spectrum compared to their membrane-bound counterparts. A mass spectrometry-based N-terminomics approach identified 134 protein cleavage events in total and 45 common substrates for sADAM10/17 within the secretome of murine cardiomyocytes. Analysis of these cleavage sites confirmed previously identified amino acid preferences. Further in vitro studies verified fibronectin, cystatin C, sN-cadherin, PCPE-1 as well as sAPP as direct substrates of sADAM10 and/or sADAM17. Overall, we present the first degradome study for sADAM10/17, thereby introducing a new mode of proteolytic activity within the protease web. KEYWORDS:

ADAM10; ADAM17; ADAM8; Ectodomain shedding; Proteolysis; TAILS