onsdag 2 oktober 2019

Matalat aminohappopitoisuudet lisämunuaisylirasituksen merkki?

https://www.ncbi.nlm.nih.gov/pubmed/?term=19281806
Tämän viitteen löysin Fibromyalgiatutkimuksista, joita Riksstämman 2010 esitti.

Altered amino acid homeostasis in subjects affected by fibromyalgia.

Bazzichi L¹, Palego L, Giannaccini G, Rossi A, De Feo F, Giacomelli C, Betti L, Giusti L, Mascia G, Bombardieri S, Lucacchini A.

1: Department of Internal Medicine, Division of Rheumatology, University of Pisa, Via Roma 67, 56126 Pisa, Italy. l.bazzichi@int.med.unipi.it

Abstract

OBJECTIVES:

To evaluate plasma amino acid (AA) concentrations in patients affected by fibromyalgia (FM) and to study the relationships between their levels and FM clinical parameters.

DESIGN AND METHODS:

20 AAs were assessed in 34 FM patients and in 18 healthy volunteers by means of a modified version of the Waters picotag method.

RESULTS:

Significant lower plasma taurine, alanine, tyrosine (Tyr), valine, methionine, phenylalanine and threonine concentrations, and the sum of essential AAs were observed in FM patients vs healthy controls (P<0 .05="" aas="" and="" b="" brain="" caa="" competing="" fm="" for="" in="" of="" ratio="" reduced="" significantly="" sum="" the="" tryptophan="" tyr="" uptake="" were="" with="">A significant correlation was found between FM clinical parameters and certain AAs.

CONCLUSIONS:

Our results suggest probable defects of gut malabsorption of certain AAs in FM patients. Moreover, given the reduced Tyr CAA' ratio in FM patients, a possible impairment of the cathecolaminergic system in the FM syndrome may be suggested.

PMID:: 19281806
DOI:: 10.1016/j.clinbiochem.2009.02.025

[Indexed for MEDLINE]

lördag 13 juli 2019

Istukan välittämä tauriini ja sikiön neuronaalinen kehitys

https://www.ncbi.nlm.nih.gov/pubmed/28849440
Abstract

2017;975 Pt 1:17-25. doi: 10.1007/978-94-024-1079-2_2.

Functions of Maternally-Derived Taurine in Fetal and Neonatal Brain Development.

Tochitani S^1,^2,³.

Abstract

Taurine (2-aminoethanesulfonic acid) is a sulfur-containing organic acid, which has various physiological functions, including membrane stabilization, cell-volume regulation, mitochondrial protein translocation, anti-oxidative activity, neuroprotection against neurotoxicity and modulation of intracellular calcium levels. Taurine also activates GABA_A receptors and glycine receptors. Mammalian fetuses and infants are dependent on taurine delivered from their mothers via either the placenta or their mother's milk. Taurine is a molecule that links mother-fetus or mother-infant bonding.This review describes the functions of taurine and the mechanisms of action of taurine in fetal and brain development. Taurine is involved in regulating the proliferation of neural progenitors, migration of newly-generated neurons, and the synapse formation of neurons after migration during fetal and neonatal development. In this review, we also discuss the environmental factors that might influence the functional roles of taurine in neural development.

KEYWORDS:
Brain development; Environmental factor; Mother-infant relationship; Obesity; Obstetric complication; Placental transfer; Taurine

PMID:: 28849440
DOI:: 10.1007/978-94-024-1079-2_2

[Indexed for MEDLINE]

Kymmenen tunnettua sulfaatinkuljettajaa istukassa. Sikiö ei pysty syntetisoimaan sulfaattia.

2017 Jun;54:45-51. doi: 10.1016/j.placenta.2017.01.001. Epub 2017 Jan 4.

Review: Nutrient sulfate supply from mother to fetus: Placental adaptive responses during human and animal gestation.

Dawson PA¹, Richard K², Perkins A³, Zhang Z⁴, Simmons DG⁴.

Abstract

Nutrient sulfate has numerous roles in mammalian physiology and is essential for healthy fetal growth and development. The fetus has limited capacity to generate sulfate and relies on sulfate supplied from the maternal circulation via placental sulfate transporters. The placenta also has a high sulfate requirement for numerous molecular and cellular functions, including sulfate conjugation (sulfonation) to estrogen and thyroid hormone which leads to their inactivation. Accordingly, the ratio of sulfonated (inactive) to unconjugated (active) hormones modulates endocrine function in fetal, placental and maternal tissues. During pregnancy, there is a marked increase in the expression of genes involved in transport and generation of sulfate in the mouse placenta, in line with increasing fetal and placental demands for sulfate. The maternal circulation also provides a vital reservoir of sulfate for the placenta and fetus, with maternal circulating sulfate levels increasing by 2-fold from mid-gestation. However, despite evidence from animal studies showing the requirement of maternal sulfate supply for placental and fetal physiology, there are no routine clinical measurements of sulfate or consideration of dietary sulfate intake in pregnant women. This is also relevant to certain xenobiotics or pharmacological drugs which when taken by the mother use significant quantities of circulating sulfate for detoxification and clearance, and thereby have the potential to decrease sulfonation capacity in the placenta and fetus. This article will review the physiological adaptations of the placenta for maintaining sulfate homeostasis in the fetus and placenta, with a focus on pathophysiological outcomes in animal models of disturbed sulfate homeostasis.

NaSi-1 , SLC13A-1, munuaisen natriumsulfaatti ko-transportteri kuuluu viiden jäsenen SLC13-perheeseen.

https://www.ncbi.nlm.nih.gov/gene/6561

NAS1, SCL13A1, (7q31.32), NaSi-1, sulfaatin kuljettaja geeni

Official Symbol: SLC13A1
Official Full Name: solute carrier family 13 member 1
Also known as: NAS1; NaSi-1
Summary: The protein encoded by this gene is an apical membrane Na(+)-sulfate cotransporter involved in sulfate homeostasis in the kidney. Defects in this gene lead to many pathophysiologic problems. [provided by RefSeq, May 2016]
Expression: Biased expression in kidney (RPKM 26.2), small intestine (RPKM 5.7) and 1 other tissue See more
Orthologs mouse all

Preferred Names: solute carrier family 13 member 1

Names: Na(+)/sulfate cotransporter; renal sodium/sulfate cotransporter; solute carrier family 13 (sodium/sulfate symporters), member 1; solute carrier family 13 (sodium/sulphate symporters), member 1

NM_001324400.1 → NP_001311329.1 solute carrier family 13 member 1 isoform 2

GeneRIFs: Gene References Into Functions

Sulfaatinkuljetusgeenit : sulfaattipermeaasi perhe DRA (SLC26A3) ja SUT-1

Ihmisen sulfaattinkuljettajageeneistä 1) DRA ja 2) SUT-1

DRA mainitaan pubMed lähteessä lähinnä kloridin ja bikarbonaatin vaihtajana. Onko tällä jotain tekemistä sulfaatin kanssa?

SLC26A3, DRA, CLD (7q22.3-31.1)
https://www.ncbi.nlm.nih.gov/gene/1811

Also known as: CLD; DRA
Summary: The protein encoded by this gene is a transmembrane glycoprotein that transports chloride ions across the cell membrane in exchange for bicarbonate ions. It is localized to the mucosa of the lower intestinal tract, particularly to the apical membrane of columnar epithelium and some goblet cells. The protein is essential for intestinal chloride absorption, and mutations in this gene have been associated with congenital chloride diarrhea. [provided by RefSeq, Oct 2008]
Expression: Biased expression in colon (RPKM 709.1), duodenum (RPKM 299.0) and 1 other tissue See more
Orthologs mouse all

Preferred Names: chloride anion exchanger

Names down-regulated in adenoma protein solute carrier family 26 (anion exchanger), member 3

Features

NM_000111.2 → NP_000102.1 chloride anion exchanger
See identical proteins and their annotated locations for NP_000102.1

Conserved Domains (3) summary

cd07042
Location:526 → 712

STAS_SulP_like_sulfate_transporter; Sulphate Transporter and Anti-Sigma factor antagonist domain of SulP-like sulfate transporters, plays a role in the function and regulation of the transport activity, proposed general NTP binding function

COG0636
Location:376 → 432

AtpE; FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy production and conversion]

pfam00916
Location:73 → 475

Sulfate_transp; Sulfate permease family

Features: ( assosioituminen colon tauteihin ja kloridiripuliin)
https://www.ncbi.nlm.nih.gov/protein/NP_000102.1

 Protein         1..764
                     /product="chloride anion exchanger"
                     /note="down-regulated in adenoma protein; solute carrier
                     family 26 (anion exchanger), member 3"
                     /calculated_mol_wt=84374
     Region          73..475
                     /region_name="Sulfate_transp"
                     /note="Sulfate permease family; pfam00916"
                     /db_xref="CDD:279284"

 Region          376..432
                     /region_name="AtpE"
                     /note="FoF1-type ATP synthase, membrane subunit
                     c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy
                     production and conversion]; COG0636"

   Region          526..712
                     /region_name="STAS_SulP_like_sulfate_transporter"
                     /note="Sulphate Transporter and Anti-Sigma factor
                     antagonist domain of SulP-like sulfate transporters, plays
                     a role in the function and regulation of the transport
                     activity, proposed general NTP binding function; cd07042"

GeneRIF: TNFalpha may act reciprocally with DRA, leading to the
            development of intestinal inflammation.

Hypersulfatemia ilmenee ennen hyperfosfatemiaa - Onkonormaali plastinen sulfur kehon "havaitsematonta plasmaa"?

Talletin vuonna 2002 artikkelin :Fernandes I et al. Sulfate homeostasis, NaSi-1 cotransporter, and SAT-1 exhancer expression in chronic renal failure in rats. Kidney Int 2001 Jan ; 59(1):210-21. Jouduin K-vitamiinityöni yhteydessä katsomaan rikkiaineenvaihduntaa, koska osa K-vitamiinifunktioista toimi sillä alueella ( sulfotransferaasien ja arylsulfataasien tarvitsemana cofaktorina ja lipidisynteesien alueella myös sulfatidien synteesin varhaisvaihe vaati Kvitamiinia kuten päätösvaihekien. samoin myös B6-vitamiini. Rikistä oli varsin vähän tietoa ravinto-opin kirjoissa ja kuitenkin sen osuus proteiineissa on yhtä konventionelli kuin typen niin että niillä on proteiinistruktuurissa tietty normaali suhteensa N:S. Tässä artikkelissa jonka säästin, mainittiin viime lauseessa, että "kroonisessa munuaisviassa hypersulfatemia aiemmin kuin hyperfosfatemia". Kirjoitin joskus paperin reunaan: "Katso tämä asia!".
Tänään etsin PubMed hakulaitella sanalla Hypersulfatemia ja saan 8 vastausta, joisa on juuri tämä artikkeli numero 2.
Katson näitä nyt.

Search results

Items: 8

Select item 200679421.

A pharmacokinetics evaluation of a new, low-volume, oral sulfate colon cleansing preparation in patients with renal or hepatic impairment and healthy volunteers.

Pelham RW, Alcorn H Jr, Cleveland Mv.

J Clin Pharmacol. 2010 Mar;50(3):350-4. doi: 10.1177/0091270009339741. Epub 2010 Jan 12.

The pharmacokinetics (PK) of an oral sulfate solution (OSS) for bowel cleansing preparation was studied. OSS (30 g of sulfate) was split between 2 doses, 12 hours apart. Safety measures included electrocardiography, vital signs, adverse events, hematology, blood chemistry, and urinalysis. Six adult patients with moderate renal disease (MRD), 6 with mild-moderate hepatic disease (M/MHD), and 6 normal healthy volunteers (NHVs) completed the study. Adverse events were mild to moderate in severity and were mainly limited to headache and expected gastrointestinal symptoms. Serum sulfate levels were highly variable at all times, even after adjusting for baseline. Sulfate was higher in MRD in comparison to the other groups. The C(max) and AUC were higher in the patients, but no statistically significant differences emerged.

Sulfate levels returned to predose values within 54 hours after dosing. No electrolyte disturbances occurred. Urinary sulfate excretion was approximately 20% of the dose. OSS was well tolerated. The types and severity of adverse events were similar to those seen in large phase III trials. While patients with MRD had elevated sulfate, the levels were less than those in renal failure and did not alter biochemical parameters that are associated with hypersulfatemia.

Similar articles

Select item 111350732.

Sulfate homeostasis, NaSi-1 cotransporter, and SAT-1 exchanger expression in chronic renal failure in rats.

Fernandes I, Laouari D, Tutt P, Hampson G, Friedlander G, Silve C.

Kidney Int. 2001 Jan;59(1):210-21.

It is known that hypersulfatemia, like hyperphosphatemia, occurs in chronic renal failure (CRF). The aim of this study was to assess the effects of CRF on sulfate homeostasis and on sodium sulfate cotransport (NaSi-1) and sulfate/oxalate-bicarbonate exchanger (Sat-1) expression in the kidney. In addition, sulfate homeostasis was compared with phosphate homeostasis...Free Article

Select item 109839973.

The clinical chemistry of inorganic sulfate.

Cole DE, Evrovski J.

Crit Rev Clin Lab Sci. 2000 Aug;37(4):299-344. Review.

Although inorganic sulfate is an essential and ubiquitous anion in human biology, it is infrequently assayed in clinical chemistry today.

Serum sulfate is difficult to measure accurately without resorting to physicochemical methods, such as ion chromatography, although many other techniques have been described.

It is strongly influenced by a variety of physiological factors, including age, diet, pregnancy, and drug ingestion.

Urinary excretion is the principal mechanism of disposal for the excess sulfate produced by sulfur amino acid oxidation, and the kidney is the primary site of regulation.

In renal failure, sulfoesters accumulate and hypersulfatemia contributes directly to the unmeasured anion gap characteristic of the condition.

In contrast, sulfate in urine is readily assayed by a number of means, particularly nephelometry after precipitation as a barium salt.

Sulfate is most commonly assayed today as part of the clinical workup for nephrolithiasis, because sulfate is a major contributor to the ionic strength of urine and alters the equilibrium constants governing saturation and precipitation of calcium salts.

Total sulfate deficiency has hitherto not been described, although genetic defects in sulfate transporters have been associated recently with congenital osteochondrodystrophies that may be lethal.

New insights into sulfate transport and its hormonal regulation may lead to new clinical applications of sulfate analysis

in the future.

Similar articles

Select item 96829594.

Effect of hemodialysis on the hypersulfatemia of chronic renal failure.

Kirschbaum B.

ASAIO J. 1998 Jul-Aug;44(4):314-8.

Concentrations of sulfate can increase eightfold in the blood of patients with severe reductions in glomerular filtration rate. Sulfate enters the body almost exclusively as the amino acids cysteine and methionine, and leaves in the urine predominantly as inorganic sulfate. Concentrations in plasma may exceed 2.5 mol/L in renal failure, and raise the anion gap by 5 mEq/L.

In studies by the author and colleagues, hemodialysis using large dialyzers and brisk blood flow rates effectively lowered the concentrations of sulfate in plasma to normal in the immediate post dialysis period; the sulfate reduction ratio actually exceeded the urea reduction ratio.

Significant correlation was observed between the two ratios.

Concentrations of sulfate, in conjunction with other data, may prove useful for estimating dietary intake of protein and monitoring control of acid-base balance.

Similar articles

Select item 13372445.

[Physiopathology and treatment of metabolic changes in transintestinal urinary diversions].

Martínez-Piñeiro L, Mateos Antón F, Martínez-Piñeiro JA.

Arch Esp Urol. 1992 Nov;45(9):875-89. Review. Spanish.

PMID:: 1337244

Similar articles

Select item 20807926.

Influence of magnesium sulfate-induced hypermagnesemia on the anion gap: role of hypersulfatemia.

Ricci J, Oster JR, Gutierrez R, Schlessinger FB, Rietberg B, O'Sullivan MJ, Clerch AR, Vaamonde CA.

Am J Nephrol. 1990;10(5):409-11.

Although hypermagnesemia purportedly lowers the anion gap (AG), we have shown previously that increases in the serum concentration of the unmeasured cation (UC) Mg due to therapeutic infusion of MgSO4 are not associated with AG reduction. To assess our hypothesis that increases in serum SO4 (unmeasured anion, UA) offset the effect of elevated serum Mg on the AG, we prospectively studied 11 patients receiving MgSO4 intravenously for toxemia of pregnancy. After 6 h of MgSO4 infusion, serum Mg increased by 2.1 +/- 0.2 (SE) mEq/l (p less than 0.001) without a significant decrease in the AG. Concomitantly, serum SO4 increased by 1.4 +/- 0.2 mEq/l. Comparison of the renal handling of SO4 versus Mg showed a higher fractional excretion of the former, probably accounting in part for the smaller increment of serum SO4 than of Mg. Comparison of the change in serum SO4 minus that of Mg indicated that, on the average, 70% of the observed 1.0 +/- 0.7 mEq/l reduction in AG was accounted for by the observed changes in the two pertinent unmeasured ions. A small decrement in serum Ca probably was a quantitatively minor factor tending to obviate a greater decrease in AG. We conclude that hypersulfatemia attenuates the reduction in AG that would otherwise accompany MgSO4-induced hypermagnesemia.

Similar articles

Select item 68463357.

The effect of sulfate on serum ionized calcium.

Friedlander MA, Lemke JH, Johnston MJ, Freeman RM.

Am J Kidney Dis. 1983 May;2(6):660-3.

Serum sulfate concentrations may reach five to ten times normal in renal failure patients dialyzed on a sorbent cartridge system, and these patients have elevated alkaline phosphatase levels suggesting an increased incidence of renal oseodystrophy. We studied the effect of adding sulfate on ionized calcium (Ca2+) in human serum in vitro and in rat serum in vivo. K2SO4 or Na2SO4:NaCl mixtures were added to aliquots of serum from normal subjects to reproduce the observed biologic range of sulfate concentrations up to 10 mmol. Serum Ca2+ concentration was found to decrease linearly as serum sulfate concentration increased, for each subject. The weighted mean slope estimates of the effect of sulfate on ionized calcium in two experiments were -.0197 and -.0181. Rats were infused through the inferior vena cava with 2 mL of either 200 mmol NaCl (N = 5) or 100 mmol Na2SO4 (N = 6), after ligation of the renal arteries and veins and withdrawal of 2 mL blood for baseline studies. The animals were killed by exsanguination from the aorta after a five-minute equilibration period. In rats administered NaCl, no difference in Ca2+ or sulfate concentration was found between pre- and postinfusion sera. In the Na2SO4 treated rats, however, a significant mean increase of 0.635 mmol (p less than .005) in serum sulfate concentration was associated with a significant mean decrease of -0.062 mmol (p less than .01) in serum Ca2+ concentration. We conclude that the acute in vitro and in vivo addition of sulfate results in a decrease in serum Ca2+ concentration. Thus, hypersulfatemia, which is present chronically in patients on sorbent dialysis systems, may contribute to elevated alkaline phosphatase levels in these patients.

Similar articles

Select item 144643758.

[Is not hypersulfatemia the cause of the osteodystrophy in chronic renal insufficiency?].

LESTRADET H, FREDERICH A, RODRIGUEZ-SORIANO J.

Presse Med. 1962 Jan 27;70:211-2. French. No abstract available.

PMID:: 14464375

Similar articles

jatko: haen näsitä entsyymeistä tietoa NaSi1-cotransporter, SAT-1 exhancer jos löytyy ortologit ihmisestä.

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: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
//

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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
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
Serum Cystatin C Levels in Twin Pregnancy versus Singleton Pregnancy. Peng J, et al. Lab Med, 2019 Apr 8. PMID 30517681
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
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?

Submit: New GeneRIF Correction See all GeneRIFs (436)

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

Tauriini ja sulfaattihomeostasis

onsdag 2 oktober 2019

Matalat aminohappopitoisuudet lisämunuaisylirasituksen merkki?

Altered amino acid homeostasis in subjects affected by fibromyalgia.

Abstract

OBJECTIVES:

DESIGN AND METHODS:

RESULTS:

CONCLUSIONS:

lördag 13 juli 2019

Istukan välittämä tauriini ja sikiön neuronaalinen kehitys

Kymmenen tunnettua sulfaatinkuljettajaa istukassa. Sikiö ei pysty syntetisoimaan sulfaattia.

NaSi-1 , SLC13A-1, munuaisen natriumsulfaatti ko-transportteri kuuluu viiden jäsenen SLC13-perheeseen.

GeneRIFs: Gene References Into Functions

Sulfaatinkuljetusgeenit : sulfaattipermeaasi perhe DRA (SLC26A3) ja SUT-1

Hypersulfatemia ilmenee ennen hyperfosfatemiaa - Onkonormaali plastinen sulfur kehon "havaitsematonta plasmaa"?

Items: 8

torsdag 20 juni 2019

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

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

Kystatiini C- geeni (PubMed haku 20.6. 2019)

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

onsdag 19 juni 2019

Haku " rhodanese" Thiosulphate sulfurtransferase. Paljon uutisia. 2019

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