Etiketter

onsdag 29 april 2020

Keltainen skorpioni, deathstalker scorpion

https://www.nyp.org/deathstalkerscorpion/scorpion_facts.html
Scorpion Facts
The Deathstalker (Leiurus quinquestriatus), is a species of scorpion, a member of the Buthidae family. It is also known as an Omdurman scorpion, or Israeli desert scorpion. The name Leiurus quinquestriatus roughly translates to “five-striped smooth-tail”. Other species of the genus Leiurus are often referred to as “deathstalkers” as well.
The Deathstalker is straw yellow in color, and can grow 3.5 to 4.5 inches (9 to 11.5 cm) in length. It is of a slight build compared to other scorpions, with a long thin tail and slender pedipalps. A dark segment on the tail is sometimes faint or even missing, which can complicate identification.
Most scorpions have a life span of two to six years.
Deathstalker scorpions are very small often tan or reddish colored with small weak pincers. The stinger tip and pincer tips can be darker, almost black colored. Females are larger than males to accommodate reproductive tasks.
Deathstalker scorpions can be found (if one is foolhardy enough to look for one) in dry desert areas and dry scrublands in northern Africa and the Middle East. It prefers a dry climate, and makes its home in natural burrows or under stones.
Scorpions may capture their prey with their pincers but in the case of the Deathstalker, the pincers are fairly weak so a sting must be administered quickly.
The size of the pincers of a scorpion can be a good measure of the potency of its venom. Scorpions with large, powerful pincers have no need for powerful toxins. Scorpions with small, weak pincers need to have strong poisons to subdue their prey and ward off enemies.
The Deathstalker scorpion has the strongest poison of any scorpion. If stung, a person will experience extreme pain, convulsions, paralysis and even death due to heart and respiratory failure.

 https://sverigesradio.se/sida/artikel.aspx?programid=406&artikel=5190601
 https://www.youtube.com/watch?v=mms2tTXLWZk

onsdag 26 februari 2020

MME(3q25.2) NEP ( Neprilysiini) , CD10 , membraanimetalloendopeptidaasi

Olen kertaamassa  RAAS- järjestelmää ja siinä on neprilysiinillä (NEP)  myös osa. 
ACE2 ja neprilysiini kehkeyttävät  angiotensiiniä Ang -(1-7)  . ACE2 tekee   sitä muodosta Ang-(1-8), joka on Angiotensiini-II.  Neprilysiini muodostaa sitä  Ang-(1-10).stä,  joka on Angiotensiini-I.  Ang-(1-7)  toimii renoprotektiivisesti ja kardioprotektiivisesti  ja käyttää GPCR-MAS aktivaatiotietä, joka  tie  opponoi ja vaimentaa   ACE- Angiotensiini II- välitteisen   verenpaineen säätelytien  monipuolisia reseptorivaikutuksia ja täten molemmat tiet osallistuvat verenpaineen säätelynhomeostaasiin. 
 
MME-geenin koodama neprilysiini (NEP) on tyypin II transmembraaniglykoproteiini ja  se tunnetaan myös  tavallisena akuutin leukemian antigeenina (CALLA) tärkeänä solupintamerkitsijänä diagnosoitaessa  akuuttia lymfaattista leukemiaa. koodautunutta proteiinia on  pre-B-fenotyyppisissä leukemisissa soluissa, joita on  85% ALL-solusita. Proteiini ei ole kutienkaan rajoittunut leukemisiin soluihin vaan sitä löytyy useissa normaalikudoksissa. proteiini on neutraali endopeptidaasi, joka  pilkkoo peptidejä hydrofobisten aminohappojen  aminopuoellta ja pystyy inaktivoimaan useita peptidihormoneja8 glukagonia, enkefaliineja, P-substanssia, neurotensiiniä, oksytosiinia, bradykiniiniä (BK). Geeniä ilmenee duodenumissa, munuaisessa ja 8 muussa kudoksessa. Neprilysiinillä on vaihtoehtoisia nimiä monta, mutta  suositeltu nimi on neprilysiini(NEP). Se tunnetaan  myös mm.  atriolysiininä,   yleisenä  akuuttin lymfosyyttileukemian antigeenina (CALLA)
kalvon metallo-endopeptidaasina (MME), neutraalina endopeptidaasina (NEP), enkefalinaasina, CD 10 (Cluster of Differentiation 10), iho-fibriblastielastaasina (SFE)  ja muitakin nimiä on ( kts. alla)

PubMed:
Official Symbol MME
  membrane metalloendopeptidase
Also known as
NEP; SFE; CD10; CALLA; CMT2T; SCA43
Summary
The protein encoded by this gene is a type II transmembrane glycoprotein and a common acute lymphocytic leukemia antigen that is an important cell surface marker in the diagnosis of human acute lymphocytic leukemia (ALL). The encoded protein is present on leukemic cells of pre-B phenotype, which represent 85% of cases of ALL. This protein is not restricted to leukemic cells, however, and is found on a variety of normal tissues. The protein is a neutral endopeptidase that cleaves peptides at the amino side of hydrophobic residues and inactivates several peptide hormones including glucagon, enkephalins, substance P, neurotensin, oxytocin, and bradykinin. [provided by RefSeq, Aug 2017]
Expression
Biased expression in duodenum (RPKM 88.5), kidney (RPKM 83.7) and 8 other tissues See more
Preferred Names
neprilysin
Names
atriopeptidase
common acute lymphocytic leukemia antigen
membrane metallo-endopeptidase (neutral endopeptidase, enkephalinase, CALLA, CD10)
membrane metallo-endopeptidase variant 1
membrane metallo-endopeptidase variant 2
neprilysin-390
neprilysin-411
neutral endopeptidase 24.11
skin fibroblast elastase
Neprilysiiniin  liittyvää lisätietoa PubMed artikkeleista.

Related articles in PubMed

See citations in PubMed for homologs of this gene provided by HomoloGe
 GeneRIF
 Tietoja  Neprilysiiniproteiinista
 https://www.ncbi.nlm.nih.gov/protein/NP_000893.2
Tässä on isoformi a (1..750 amiohappoa) TM kohta merkattutummalla (29..51) ,
Aktiivikohta merkattu isoilla kirjaimilla. 543N, 544A, 581V, 584H, 585E, 588H, 647E, 690F, 691A 712H, 718R.
Zinkkiä sitova kohta m, kolme aminohappoa osuu aktiiviin kohtaan, tummalla merkatut. 
Näkyy olevan yksi  motiivi llxxl  (674-680) (lie tumareseptori?) 
peptidista koko mitalta  79-748  on M12 peptidaasiperheen M12 endoteliinia konvertoiva entsyymi I (ECE-1) .
N-terminaalinen sytoplasminen osa:
1 mgksesqmdi tdintpkpkk kqrwtple
ORIGIN      
        1 mgksesqmdi tdintpkpkk kqrwtpleis lsvlvlllti iavtmialya tyddgickss
       61 dciksaarli qnmdattepc tdffkyacgg wlkrnvipet ssrygnfdil rdelevvlkd
      121 vlqepktedi vavqkakaly rscinesaid srggepllkl lpdiygwpva tenweqkyga
      181 swtaekaiaq lnskygkkvl inlfvgtddk nsvnhvihid qprlglpsrd yyectgiyke
      241 actayvdfmi svarlirqee rlpidenqla lemnkvmele keianatakp edrndpmlly
      301 nkmtlaqiqn nfsleingkp fswlnftnei mstvnisitn eedvvvyape yltklkpilt
      361 kysardlqnl mswrfimdlv sslsrtykes rnafrkalyg ttsetatwrr canyvngnme
      421 navgrlyvea afageskhvv edliaqirev fiqtlddltw mdaetkkrae ekalaikeri
      481 gypddivsnd nklnneylel nykedeyfen iiqnlkfsqs kqlkklrekv dkdewisgaa
      541 vvNAfyssgr nqivfpagil qppffsaqqs nslnyggigm VigHEitHgf ddngrnfnkd
      601 gdlvdwwtqq sasnfkeqsq cmvyqygnfs wdlaggqhln gintlgEnia dngglgqayr
      661 ayqnyikkng eekllpgldl nhkqlfflnF Aqvwcgtyrp eyavnsiktd vHspgnfRii
      721 gtlqnsaefs eafhcrknsy mnpekkcrvw
//


Tietoja Neprilysiinin  perheestä "M13".
Metallopeptidase family M13 includes neprilysin (NEP) and other members: 

M13 family of metallopeptidases includes
 neprilysin (neutral endopeptidase, NEP, enkephalinase, CD10, CALLA, EC 3.4.24.11),
endothelin-converting enzyme I (ECE-1, EC 3.4.24.71),
 erythrocyte surface antigen KELL (ECE-3),
phosphate-regulating gene on the X chromosome (PHEX),
 soluble secreted endopeptidase (SEP), and
 damage-induced neuronal endopeptidase (DINE)/X-converting enzyme (XCE).

 These proteins consist of a short N-terminal cytoplasmic domain,
 a single transmembrane helix,
and a larger C-terminal extracellular domain containing the active site.
Proteins in this family fulfill a broad range of physiological roles due to the greater variation in the S2' subsite allowing substrate specificity.

NEP is expressed in a variety of tissues including kidney and brain, and is involved in many physiological and pathological processes, including blood pressure and inflammatory response. It degrades a wide array of substrates such as substance P (SP), enkephalins, cholecystokinin (CCK), neurotensin and somatostatin. It is an important enzyme in the regulation of amyloid-beta (Abeta) protein that forms amyloid plaques that are associated with Alzeimers disease (AD).

 ECE-1 catalyzes the final rate-limiting step in the biosynthesis of endothelins via post-translational conversion of the biologically inactive big endothelins. Like NEP, it also hydrolyses bradykinin, substance P, neurotensin and Abeta.  

Endothelin-1 overproduction has been implicated in various diseases, including stroke, asthma, hypertension, and cardiac and renal failure.

 Kell is a homolog of NEP and constitutes a major antigen on human erythrocytes; it preferentially cleaves big endothelin-3 to produce bioactive endothelin-3, but is also known to cleave substance P and neurokinin A.

PHEX forms a complex interaction with fibroblast growth factor 23 (FGF23) and matrix extracellular phosphoglycoprotein, causing bone mineralization. A loss-of-function mutation in PHEX disrupts this interaction leading to hypophosphatemic rickets; X-linked hypophosphatemic (XLH) rickets is the most common form of metabolic rickets.

 ECEL1 is a brain metalloprotease involved in the critical role in the nervous regulation of the respiratory system, while

DINE (damage induced neuronal endopeptidase) is abundantly expressed in the hypothalamus and its expression responds to nerve injury as well.

 Thus, majority of these M13 proteases are prime therapeutic targets for selective inhibition.

 https://www.ncbi.nlm.nih.gov/pubmed

Liekö yhteyttä  ylläolevilla tekijöillä respiraation kerebraaliseen säätelyyn? Katsotaan,mitä tiede löytää lähi tulevaisuudesa.

2020 Feb 3;112:95-106. doi: 10.1016/j.neubiorev.2020.02.001. [Epub ahead of print]
Respiratory regulation & interactions with neuro-cognitive circuitry.
Abstract
It is increasingly being recognized that active control of breathing - a key aspect of ancient Vedic meditative practices, can relieve stress and anxiety and improve cognition. However, the underlying mechanisms of respiratory modulation of neurophysiology are just beginning to be elucidated. Research shows that brainstem circuits involved in the motor control of respiration receive input from and can directly modulate activity in subcortical circuits, affecting emotion and arousal. Meanwhile, brain regions involved in the sensory aspects of respiration, such as the olfactory bulb, are like-wise linked with wide-spread brain oscillations; and perturbing olfactory bulb activity can significantly affect both mood and cognition. Thus, via both motor and sensory pathways, there are clear mechanisms by which brain activity is entrained to the respiratory cycle. Here, we review evidence gathered across multiple species demonstrating the links between respiration, entrainment of brain activity and functional relevance for affecting mood and cognition. We also discuss further linkages with cardiac rhythms, and the potential translational implications for biorhythm monitoring and regulation in neuropsychiatric disorders.







 ----------------Päivitys 26.2. 2020

onsdag 22 januari 2020

MEPRIINIT, Mitä ne ovat. kalvoon sitoutuneita astasiineja! / metalloproteinaasiryhmkää metsinkiinien suoerperheestä)

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2650038/
Tämä ihmisen TRIM37 jossa on  peptidihännäss MATH domeeni eli Mepriini ja TRAF-  homologidomeeni9 on peroxisomaalinen proteiini ja jos MATHdomeenissa on mutaatio, siitäseuraa että kokoTRUIM37  sijoittautuu muualle kuin peroxisomiin. 
Muita trimejä ei´n löytänyt joissa olisi tämä mepriini- tunnusmerkki.  olisko peroksisomit  tulleet  ihmiseen jostain sieltä ihan "korallien ajoista" ?
Täytyy katsoa mistäniitä tuli ihmiseen.

Tässä linkissä on hyviä kaavoja metsinkiineistä. 

ihmisen Meprin 1A alfa ja beta
https://www.ncbi.nlm.nih.gov/protein/Q16819 
https://www.ncbi.nlm.nih.gov/protein/XP_011524315.1 

 Biochem. J. (2013)450, 253–264 (Printed in Great Britain)doi:10.1042/BJ20121751253
 REVIEW ARTICLE The metalloproteases meprinα and meprinβ: unique enzymes in inflammation, neurodegeneration, cancer and fibrosis 
Claudia BRODER and Christoph BECKER-PAULY

The  metalloproteases meprinα and meprinβ exhibit structural and functional features that are unique among all extracellular proteases. Although meprins were discovered more than 30 years ago, their precise substrates and physiological roles have been elusive. Both enzymes were originally found to be highly expressed in kidney and intestine, which focused research on these particular tissues and associated pathologies. Only recently it has become evident that meprins exhibit a much broader expression pattern, implicating functions in angiogenesis, cancer, inflammation, fibrosis and neurodegenerative diseases. Different animal models, as well as proteomics approaches for the identification of protease substrates, have helped to reveal more precise molecular signalling events mediated by meprin activity, such as activation and release of pro-inflammatory cytokines. APP (amyloid precursor protein) is cleaved by meprinβ in vivo, reminiscent of the β-secretase BACE1 (β-site APP-cleaving enzyme 1). The subsequent release of Aβ(amyloidβ)
peptides is thought to be the major cause of the neurodegenerative Alzheimer’s disease. On the other hand, ADAM10 (a disintegrin and metalloprotease domain 10), which is the constitutiveα-secretase, was shown to be activated by meprinβ, which is it self shed from the cell surface by ADAM10.
 In skin, both meprins are overexpressed in fibrotic tumours, characterized by massive accumulation of fibrillar collagens. Indeed, procollagen III is processed to its mature form by meprinα and meprinβ,an essential step in collagen fibril assembly. The recently solved crystal structure of meprinβ and the unique cleavage specificity of these proteases identified by proteomics will help to generate specific inhibitors that could be used as therapeutics to target meprins under certain pathological conditions .Key words: cancer, fibrosis, inflammation, meprin, metalloprotease, neurodegeneration, proteomics.

 Structure length function
Meprins are complex and highly glycosylated multi-domainenzymes that require post-translational modifications to reach fullactivity. They are expressed as proteolytically inactive zymogens that require the removal of their N-terminal propeptides by otherproteases. Several serine proteases have been identified as doingthis job [30–34], e.g. members of the tissue KLKs (kallikrein-related peptidases).Meprins belong to the astacin family of metalloproteases,comprising only six members in humans [35]. These enzymes are characterized by a conserved zinc-binding motif(HExxHxxGxxHxxxRxDR) and by a sequence in close proximity to the active-site cleft, the so called Met-turn, that includes a tyrosine residue as a fifth zinc ligand. Within the astacin family,meprins exhibit a unique domain composition. Human meprinα and β, encoded on chromosomes 6 and8 respectively, comprise an N-terminal signal peptide directing the polypeptide chain to the endoplasmic reticulum, an N-terminal propeptide, an astacin-like protease domain, a MAM(meprin A5 protein tyrosine phosphataseμ) domain and a TRAF(tumour-necrosis-factor-receptor-associated factor) domain, both of which are known to mediate protein–protein interactions, anEGF (epidermal growth factor)-like domain, a transmembranedomain, and a C-terminal cytosolic tail (Figure 1A)

 Mistä niit pre-peroxisomeja olisi tullut?
(Ehkä jokin niistä Cnidarioista hienolla injektiotekniikallaan on antanut "kykyjä"  monisoluisiin organismeihin, joisa kiertää veri ja on muutakin ravinnetta.  Siitä ajasta olisi peroxisomeihin jäänyt se  meoprin-MATH-pätkä TRIm37:ään kai.
 https://onlinelibrary.wiley.com/doi/full/10.1002/bies.201700050
 


Metzinkiinisuperperhe, alaperhe Astasiinit: Alaryhmä Mepriinit , Mepriini beta

Meprin beta
https://www.ncbi.nlm.nih.gov/pubmed/31604820
2019 Nov 22;294(47):17768-17776. doi: 10.1074/jbc.RA119.008310. Epub 2019 Oct 11.

Phosphorylation of the amyloid precursor protein (APP) at Ser-675 promotes APP processing involving meprin β.

Abstract

Alzheimer's disease (AD) is a neurodegenerative disorder characterized by abnormal deposition of β-amyloid (Aβ) peptides. Aβ is a cleavage product of the amyloid precursor protein (APP), and aberrant posttranslational modifications of APP can alter APP processing and increase Aβ generation. In the AD brain, seven different residues, including Ser-675 (APP695 numbering) in the APP cytoplasmic domain has been found to be phosphorylated. Here, we show that expression of a phosphomimetic variant of Ser-675 in APP (APP-S675E), in human neuroblastoma SK-N-AS cells, reduces secretion of the soluble APP ectodomain (sAPPα), even though the total plasma membrane level of APP was unchanged compared with APP levels in cells expressing APPwt or APP-S675A. Moreover, the level of an alternative larger C-terminal fragment (CTF) increased in the APP-S675E cells, whereas the CTF form that was most abundant in cells expressing APPwt or APP-S675A decreased in the APP-S675E cells. Upon siRNA-mediated knockdown of the astacin metalloprotease meprin β, the levels of the alternative CTF decreased and the CTF ratio was restored back to APPwt levels. Our findings suggest that APP-Ser-675 phosphorylation alters the balance of APP processing, increasing meprin β-mediated and decreasing α-secretase-mediated processing of APP at the plasma membrane. As meprin β cleavage of APP has been shown to result in formation of highly aggregation-prone, truncated Aβ2-40/42 peptides, enhanced APP processing by this enzyme could contribute to AD pathology. We propose that it would be of interest to clarify in future studies how APP-Ser-675 phosphorylation promotes meprin β-mediated APP cleavage.

KEYWORDS:

ADAM; APP-CTF; Alzheimer's disease; amyloid precursor protein (APP); amyloid-beta (Aβ); meprin β; neurodegeneration; proteolytic processing; β-secretase 1 (BACE1)
PMID:
31604820
PMCID:
PMC6879340
DOI:
10.1074/jbc.RA119.008310


Tässä katson TRIM37, jolla on domeenit RBC ja MATH ( (Meprin and TRAF Homolog). Kor. 17  sijainti.
Mitenkähän tämä toimii normaalisti?  Se vaikuttaa radioreistenssiä, joka havaitaan  silloin kun kätyetään cisplatiinia tuumoriin..

https://www.ncbi.nlm.nih.gov/pubmed/30254148 
 Conserved Domains (4) summary
smart00502
Location:132254
BBC; B-Box C-terminal domain
cd00162
Location:1558
RING; RING-finger (Really Interesting New Gene) domain, a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc; defined by the 'cross-brace' motif C-X2-C-X(9-39)-C-X(1-3)- H-X(2-3)-(N/C/H)-X2-C-X(4-48)C-X2-C; probably involved in ...
cd03773
Location:273406
MATH_TRIM37; Tripartite motif containing protein 37 (TRIM37) family, MATH domain; TRIM37 is a peroxisomal protein and is a member of the tripartite motif (TRIM) protein subfamily, also known as the RING-B-box-coiled-coil (RBCC) subfamily of zinc-finger proteins. ...https://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=239742
 The MATH domain of TRIM37 has been shown to interact with the TRAF domain of six known TRAFs in vitro, however, it is unclear whether this is physiologically relevant. Eleven TRIM37 mutations have been associated with Mulibrey nanism so far. One mutation, Gly322Val, is located in the MATH domain and is the only mutation that does not affect the length of the protein. It results in the incorrect subcellular localization of TRIM37.
pfam00643
Location:90132
zf-B_box;

Pseudomonas serralysin

https://www.ncbi.nlm.nih.gov/pubmed/31933178
https://www.ebi.ac.uk/interpro/entry/InterPro/IPR011049/

2019 Oct 31. pii: S1569-1993(19)30916-6. doi: 10.1016/j.jcf.2019.10.009. [Epub ahead of print]  Cystic fibrosis related diabetes in Europe: Prevalence, risk factors and outcome; Olesen et al.
Cystic fibrosis related diabetes (CFRD) has implications for morbidity and mortality with several risk factors identified. We studied the epidemiology of CFRD in the large dataset of the European Cystic Fibrosis Society Patient registry.
Data on CF patients were investigated for the prevalence of CFRD as well as for any association with suggested risk factors and effects.
CFRD increased by approximately ten percentage points every decade from ten years of age. Prevalence was higher in females in the younger age groups. CFRD was associated with severe CF genotypes (OR = 3.11, 95%CI: 2.77-3.48), pancreatic insufficiency (OR = 1.46, 95%CI: 1.39-1.53) and female gender (OR = 1.28, 95%CI: 1.21-1.34). Patients with CFRD had higher odds of being chronically infected with Pseudomonas aeruginosa, Burkholderia cepacia complex and Stenotrophomonas maltophilia than patients without CFRD, higher odds of having FEV1% of predicted <40 1.15-1.34="" 1.24="" 1.70-1.94="" 1.82="" 95="" and="" bmi="" cfrd="" having="" higher="" odds="" of="" p="" patients="" sds="" than="" without="">  CONCLUSIONS:
Severe genotype, pancreatic insufficiency and female gender remain considerable intrinsic risk factors for early acquisition of CFRD. CFRD is associated with infections, lower lung function and poor nutritional status. Early diagnosis and aggressive treatment of CFRD are more important than ever with increasing life span.

Diabetes on Egyptin tavallisin tauti. Kansanlääkevaikutuksesta (2019) : Proteus ja diabetes.

PubMEd : hakusana"Proteus, Diabetes"
Eräiä   vastauksia: 
(1) 2019;20(7):595-604. doi: 10.2174/1389201020666190613161212.
Antibacterial and Potential Antidiabetic Activities of Flavone C-glycosides Isolated from Beta vulgaris Subspecies cicla L. var. Flavescens (Amaranthaceae) Cultivated in Egypt.
Abstract
BACKGROUND:
Diabetes mellitus is the most common disease in Egypt. In this context, Beta vulgaris subspecies cicla L. var. flavescens is an edible plant that has been used in traditional medicine as a therapy for treating some diseases.
OBJECTIVES:
The current study was performed to evaluate the antibacterial and potential anti-diabetic activities of different extracts and isolated flavone C-glycoside compounds isolated from Beta vulgaris subspecies cicla L. var. flavescens leaves.
METHODS:
Phytochemical investigation of n-butanol extract led to the isolation of five phytoconstituents. Their structures were determined by spectroscopic tools, including 1D-NMR (1H- & 13C-NMR) and 2D-NMR (HMQC & HMBC) besides the comparison of the data with the literature. The extracts and phytoconstituents were evaluated in vitro for their activity against some bacterial pathogens, which represent prominent human pathogens, particularly in hospital settings. The antibacterial activity was examined against three Gram-positive bacterial strains (Staphylococcus aureus, Staphylococcus epidermidis & Enterococcus faecalis) and five Gram-negative ones (Pseudomonas aeruginosa, Proteus vulgaris, Klebsiella pneumoniae, Proteus mirabilis & Salmonella typhimurium) relative to Ciprofloxacin as a reference drug. Furthermore, the in vitro antidiabetic activity (Type II) was evaluated using the alpha-glucosidase inhibitory assay.
RESULTS:
Five flavone C-glycosides namely; Apigenin 8-C-β-D-glucopyranoside (vitexin) (1), 2''-Oxylopyranosylvitexin (2), acacetin 8-C-β-D-glucopyranoside (3), acacetin 8-C-α-L-rhamnoside (4), and 6,8-di-C-β-D-glucopyranosylapigenin (vecinin-II) (5) were isolated from n-butanol extract of B. vulgaris subspecies cicla L. var. flavescens. Compound 1 showed a promising antibacterial activity against most of the test bacterial strains with respect to the minimum inhibitory concentration values (MIC) ranged from 1.95 to 15.63 µg ml-1. On the other hand, compounds 1 and 3 demonstrated superior antidiabetic activities with IC50 values of 35.7 and 42.64 µg ml-1, respectively, while an inferior potential antidiabetic activity was recorded for compound 4 (IC50 = 145.5 µg ml-1) in comparison with Acarbose as a reference drug.
CONCLUSION:
B. vulgaris L. is an edible plant, which could be used as a natural source of antibiotic and hypoglycemic drugs.
KEYWORDS:
Amaranthaceae; Beta vulgaris subspecies cicla L. var. flavescens; antibacterial; antidiabetic; flavonoids; saponins.
DOI:
10.2174/1389201020666190613161212


(2)
2019 Sep;164(9):2265-2275. doi: 10.1007/s00705-019-04305-x. Epub 2019 Jun 14.
Elimination of multidrug-resistant Proteus mirabilis biofilms using bacteriophages.
Abstract
Proteus mirabilis is responsible for a wide range of infections that affect the urinary tract, the respiratory tract, burns, wounds and the feet of individuals with diabetes. They are highly resistant to antimicrobial agents, and new therapeutic options are therefore needed to combat this pathogen. The use of bacteriophages is one option that may be useful in treating multidrug-resistant (MDR) Proteus mirabilis infections, especially biofilm-based infections. The aim of this study was to control biofilms formed by MDR Proteus mirabilis using bacteriophages. Proteus mirabilis isolates were identified based on biochemical tests, and their resistance profiles were determined by the disk diffusion method. The biofilm-forming capacity of the isolates was assessed by the spectrophotometric method. Bacteriophages attacking Proteus mirabilis were isolated from sewage. The effect of phage on biofilm formation was investigated by the viable count method. A high rate of drug resistance was found (87.2%). Strong biofilm formation was observed in 80.5% of isolates, while moderate production was found in 19.5%. Five bacteriophages were isolated from sewage and were tested for their ability to eliminate biofilms. Significant disruption of pre-formed biofilms was observed that reached up to 99.9% decrease in the number of viable cells. The use of bacteriophages is considered a promising strategy against the biofilm infections caused by MDR Proteus mirabilis isolates.
PMID:
31197549
DOI:
10.1007/s00705-019-04305-x
[Indexed for MEDLINE]

Serralysin 2020, ( ilman kommenttiani)

https://id.nlm.nih.gov/mesh/C095666.html

About:

serralysin ^http://id.nlm.nih.gov/mesh/C095666

Type:

MeSH SCR ChemicalThese are chemicals, drugs, enzymes, vitamins, etc.
more types...

Related to

preferredConcept (MeSH Concept)
preferredMappedTo (MeSH TopicalDescriptor) preferredTerm (MeSH Term) frequency
  • "47"
active
  • "true"
dateCreated
  • "1995-10-17"
dateRevised
  • "2004-08-06"
identifier
  • "C095666"
note
  • "zinc metalloproteinases with broad similar specificity for cleavage of the oxidized insulin B chain"
source
  • "Methods Enzymol 1995;248:395-413"
label
  • "serralysin"
https://febs.onlinelibrary.wiley.com/doi/full/10.1111/j.1742-4658.2007.05739.x