lördag 13 juli 2019

Istukan välittämä tauriini ja sikiön neuronaalinen kehitys

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

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.
 
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 GABAA 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.
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_001324400.1NP_001311329.1  solute carrier family 13 member 1 isoform 2


Related articles in PubMed
GeneRIFs: Gene References Into Functions
Löydän tässä kokonaisen SLC13 perheen: 


NaS1 ja NaS2  kuljettavat sulfaattia, selenaattia ja tiosulfaattia.
NaXD1, NaCD3 ja NACDT kuljettavat di- ja trikarboksylaatteja kuten meripihkahappoa, sitraattia ja alfa-ketoglutaraattia. 
2006 Feb;451(5):597-605. Epub 2005 Oct 7.
Molecular properties of the SLC13 family of dicarboxylate and sulfate transporters.
Pajor AM1. Abstract
The SLC13 gene family consists of five members in humans, with corresponding orthologs from different vertebrate species. All five genes code for sodium-coupled transporters that are found on the plasma membrane. Two of the transporters, NaS1 and NaS2, carry substrates such as sulfate, selenate and thiosulfate. The other members of the family (NaDC1, NaDC3, and NaCT) are transporters for di- and tri-carboxylates including succinate, citrate and alpha-ketoglutarate. The SLC13 transporters from vertebrates are electrogenic and they produce inward currents in the presence of sodium and substrate.
 Substrate-independent leak currents have also been described.
 Structure-function studies have identified the carboxy terminal half of these proteins as the most important for determining function. Transmembrane helices 9 and 10 may form part of the substrate permeation pathway and participate in conformational changes during the transport cycle. This review also discusses new members of the SLC13 superfamily that exhibit both sodium-dependent and sodium-independent transport mechanisms. The Indy protein from Drosophila, involved in determining lifespan, and the plant vacuolar malate transporter are both sodium-independent dicarboxylate transporters, possibly acting as exchangers. The purpose of this review is to provide an update on new advances in this gene family, particularly on structure-function studies and new members of the family.
Free PMC Article

NAS2 , SLC13A4 (7q33), SUT-1, SUT1   
https://www.ncbi.nlm.nih.gov/gene
Official Symbol SLC13A4
Official Full Name solute carrier family 13 member 4
Also known as NAS2; SUT1; SUT-1
Expression;Biased expression in placenta (RPKM 28.4) and testis (RPKM 3.0) See more
Related articles in PubMed

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

    Conserved Domains (3) summary
    cd07042
    Location:526712
    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:376432
    AtpE; FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy production and conversion]
    pfam00916
    Location:73475
    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

1.
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.
2.
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
 
3.
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.
4.
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.
5.
Martínez-Piñeiro L, Mateos Antón F, Martínez-Piñeiro JA.
Arch Esp Urol. 1992 Nov;45(9):875-89. Review. Spanish.
PMID:
1337244
6.
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.
7.
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.
8.
LESTRADET H, FREDERICH A, RODRIGUEZ-SORIANO J.
Presse Med. 1962 Jan 27;70:211-2. French. No abstract available.
PMID:
14464375
 
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: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
 
 

onsdag 19 juni 2019

Haku " rhodanese" Thiosulphate sulfurtransferase. Paljon uutisia. 2019

https://www.ncbi.nlm.nih.gov/pubmed/?term=rhodanese
 Search results Items: 1 to 20 of 1062

1.
Bełtowski J.
Methods Mol Biol. 2019;2007:1-8. doi: 10.1007/978-1-4939-9528-8_1.
In addition to nitric oxide (NO) and carbon monoxide (CO), hydrogen sulfide (H2S) has recently emerged as the novel gasotransmitter involved in the regulation of the nervous system, cardiovascular functions, inflammatory response, gastrointestinal system, and renal function. H2S is synthesized from L-cysteine and/or L-homocysteine by cystathionine β-synthase, cystathionine γ-lyase, and cysteine aminotransferase together with 3-mercaptopyruvate sulfurtransferase. In addition, H2S is enzymatically metabolized in mitochondria by sulfide:quinone oxidoreductase, persulfide dioxygenase, and sulfite oxidase to thiosulfate, sulfite, and sulfate which enables to regulate its level by factors such as oxygen pressure, mitochondria density, or efficacy of mitochondrial electron transport.
 H2S modifies protein structure and function through the so-called sulfuration or persulfidation, that is, conversion of cysteine thiol (-SH) to persulfide (-SSH) groups. This, as well as other signaling mechanisms, is partially mediated by more oxidized H2S-derived species, polysulfides (H2Sn). In addition, H2S is able to react with reactive oxygen and nitrogen species to form other signaling molecules such as thionitrous acid (HSNO), nitrosopersulfide (SSNO-), and nitroxyl (HNO). All H2S-synthesizing enzymes are expressed in the vascular wall, and H2S has been demonstrated to regulate vascular tone, endothelial barrier permeability, angiogenesis, vascular smooth muscle cell proliferation and apoptosis, and inflammatory reaction. H2S-modifying therapies are promising approach for diseases such as arterial hypertension, diabetic angiopathy, and atherosclerosis.
PMID:
31148102
2.
Hepowit NL, Maupin-Furlow JA.
J Bacteriol. 2019 May 13. pii: JB.00254-19. doi: 10.1128/JB.00254-19. [Epub ahead of print]
PMID:
31085691
3.
Selles B, Moseler A, Rouhier N, Couturier J.
J Exp Bot. 2019 May 4. pii: erz213. doi: 10.1093/jxb/erz213. [Epub ahead of print]
PMID:
31055601
4.
Nagahara N, Tanaka M, Tanaka Y, Ito T.
Antioxidants (Basel). 2019 May 1;8(5). pii: E116. doi: 10.3390/antiox8050116.
5.
Moseler A, Selles B, Rouhier N, Couturier J.
New Phytol. 2019 Apr 29. doi: 10.1111/nph.15870. [Epub ahead of print]
PMID:
31032955
6.
Sharma M, Akhter Y, Chatterjee S.
World J Microbiol Biotechnol. 2019 Apr 22;35(5):70. doi: 10.1007/s11274-019-2643-8. Review.
PMID:
31011828
7.
Li H, Liu H, Chen Z, Zhao R, Wang Q, Ran M, Xia Y, Hu X, Liu J, Xian M, Xun L.
Redox Biol. 2019 Jun;24:101179. doi: 10.1016/j.redox.2019.101179. Epub 2019 Mar 26.
8.
Suman SG, Gretarsdottir JM.
Met Ions Life Sci. 2019 Jan 14;19. pii: /books/9783110527872/9783110527872-020/9783110527872-020.xml. doi: 10.1515/9783110527872-020.
PMID:
30855115
9.
Tang T, Sun H, Li Y, Chen P, Liu F.
Mol Immunol. 2019 Mar;107:115-122. doi: 10.1016/j.molimm.2019.01.016. Epub 2019 Feb 1.
PMID:
30716562
10.
Wells M, McGarry J, Gaye MM, Basu P, Oremland RS, Stolz JF.
J Bacteriol. 2019 Mar 13;201(7). pii: e00614-18. doi: 10.1128/JB.00614-18. Print 2019 Apr 1.
PMID:
30642986
11.
Fránová J, Koloniuk I, Lenz O, Sakalieva D.
Folia Microbiol (Praha). 2019 May;64(3):373-382. doi: 10.1007/s12223-018-0660-x. Epub 2018 Oct 30.
PMID:
30377990
12.
Florentino AP, Pereira IAC, Boeren S, van den Born M, Stams AJM, Sánchez-Andrea I.
Environ Microbiol. 2019 Jan;21(1):209-225. doi: 10.1111/1462-2920.14442. Epub 2018 Nov 15.
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Eukaryotic ubiquitin-like proteins (UBLs) have evolved from prokaryotic sulfur-carrier proteins (SCPs). Ubiquitin related modifier 1 (Urm1) shares biochemical and structural features of UBLs and SCPs and is essential for 2-thiolation of cytoplasmic tRNA.

 This chemical modification of wobble uridine is highly conserved amongst species and is achieved via Urm1 thiocarboxylation by the non-canonical ubiquitin activating 4 enzyme (Uba4), which contains an E1- and a Rhodanese (RHD) domain. While the RHD catalyzes the last step in Urm1-thiocarboxylate formation, the previous steps in Urm1 activation and the interplay between the two domains have remained elusive. To define the underlying mechanism, we established an Urm1 in vitro thiocarboxylation assay, which combined with structure-function and chemical profiling analyses revealed a critical thioester linkage between Urm1 and Uba4 residue Cys225. This linkage is indispensable for the Urm1 intramolecular transfer between the two domains of Uba4 and it is thus, essential for tRNA thiolation in vivo
. These findings contribute to a deeper understanding of UBL evolution.
PMID:
29718331
PMCID:
PMC6007339
DOI:
10.1093/nar/gky312