torsdag 20 juni 2019

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:34144
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

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

 
  • Metalloproteinaasien  ADAM10/ADAM17 degradomi hajoittaa C-cystiinin:
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
 
 

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