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måndag 13 januari 2020

HISTAMIINI kalasäilykkeissä Skombroidi ruokamyrkytys liiasta histamiinista

Kalojen histamiinipitoisuus
J Food Prot. 2020 Jan;83(1):136-141. doi: 10.4315/0362-028X.JFP-19-288.
US FDA raja sallitulle histamiinille elintarvikeessa : 50 mg /kg.


  • Tuna in oil with vegetables Tonnikala öljyssä , vihanneksia
  • Tuna in brine , Tonnikala suolaliemessä
  • Kilka in oil, Kilohaili öljyssä
  • Sardine in oil, Sardiini öljyssä
  • Mackerel in oil , Makrilli öljyssä

Occurrence of Histamine in Canned Fish Samples (Tuna, Sardine, Kilka, and Mackerel) from Markets in Tehran. Peivasteh-Roudsari L1,2,3, Rahmani A4, Shariatifar N1, Tajdar-Oranj B5, Mazaheri M6, Sadighara P1, Khaneghah AM7.


1 Food Safety and Hygiene Division, Department of Environmental Health, Faculty of Public Health, Tehran University of Medical Sciences, Tehran, Iran.
2 Students' Scientific Research Center, Tehran University of Medical Sciences, Tehran, Iran.
3 Halal Research Center of IRI, Food and Drug Administration, Tehran, Iran.
4 Department of Food and Agriculture, Standard Research Institute, Karaj, Iran.
5 Department of Biology Research and Iran Secretariat of CCCF & CCGP, Faculty of Food & Agriculture, Standard Research Institute, Karaj, Iran.
6 Student Research Committee, Department of Food Technology, Faculty of Nutrition Sciences and Food Technology and National Nutrition and Food Technology Research Institute, Shahid Beheshti University of Medical Sciences, Tehran, Iran.
7 Department of Food Science, Faculty of Food Engineering, University of Campinas, Rua Monteiro Lobato 80, Caixa Postal 6121, CEP 13083-862, Campinas, São Paulo, Brazil (ORCID: https://orcid.org/0000-0001-5769-0004 [A.M.K.]).
Abstract
Food poisoning is one of the most addressed health issues and has raised notable concerns. Histamine is the biogenic amine responsible for scombroid poisoning, which is due to the histidine decarboxylation by bacterial decarboxylases in various types of fish and fish products. The present investigation was conducted to measure the concentration of histamine in canned fish samples of tuna in oil (n = 18), tuna in oil with vegetables (n = 15), tuna in brine (n = 9), kilka in oil (n = 9), sardine in oil (n = 3), and mackerel in oil (n = 6) collected from markets in Tehran, Iran. Histamine concentrations were determined with a high-performance liquid chromatography device equipped with a UV detector. For method validation, the correlation coefficient (R2), recovery percentage, relative standard deviation for repeatability, limit of detection, and limit of quantification were 0.99, 82%, 1.3%, 1.5 mg/kg, and 5 mg/kg, respectively. Histamine was detected in 46.6% of the samples, and 18.3% of samples exceeded the histamine limit stipulated by the U.S. Food and Drug Administration (50 mg/kg). The overall mean histamine concentration was 17.36 ± 15.44 mg/kg, with a range of 0 to 88 mg/kg. A significant difference in histamine concentration was found between canned tuna in oil and canned tuna in brine (P < 0.05).
 However, no significant difference in histamine concentration was found among samples of canned tuna in brine, canned sardine in oil, canned kilka in oil, and canned mackerel in oil. Because of the high histamine concentrations detected in some brands of Iranian canned tuna, precise control programs, hazard analysis critical control point systems, and good hygiene practices should be implemented.
KEYWORDS: Canned fish; Histamine; Kilka; Mackerel; Sardine; Tuna
PMID:
31855616
DOI:
10.4315/0362-028X.JFP-19-288
 https://fi.wikipedia.org/wiki/Makrillit
 
Skombroidista ruokamyrkytystä
(https://safefood360.com/wp-content/uploads/2018/12/Scombrotoxin.pdf)
havaitaan joskus SCOMBRIDAE- kalaperheestä.

SCOMBRIDAE- alaperheiksi katsotaan:
(1) GASTEROCISMATNA: 
Genus: Gasterochisma.

(2) SCOMBRINAE:

Heimo
Scombrini: Makrillit.
Genus: SCOMBER
makrilli, SCOMBER SCOMBRUS, mackerel. makrill

Heimo:
Scomberomorini: Espanjalaiset makrillit

Heimo:
Sardini: Boniti. Atlantin bonito SARDA SARDA

Heimo:
Thunnini : Tonnikalat.
Genus: THUNNUS
tonnikala, THUNNUS THYNNUS, Bluefin tuna, tonfisk
MuistiiN 13.1. 2019

torsdag 12 december 2019

Treoniini. Treoniini käyttyy vastasyntyneessä ensisijaisesti suoliston mucuskerroksen luomiseen.

MUSIINIRAKENNE ja treoniinin merkitys:
2017 Feb;147(2):202-210. doi: 10.3945/jn.116.236786. Epub 2017 Jan 4.

Protein Synthesis in Mucin-Producing Tissues Is Conserved When Dietary Threonine Is Limiting in Piglets.

Abstract BACKGROUND:
The neonatal gastrointestinal tract extracts the majority of dietary threonine on the first pass to maintain synthesis of threonine-rich mucins in mucus. As dietary threonine becomes limiting, this extraction must limit protein synthesis in extraintestinal tissues at the expense of maintaining protein synthesis in mucin-producing tissues.
OBJECTIVE: The objective was to determine the dietary threonine concentration at which protein synthesis is reduced in various tissues.
METHODS:
Twenty Yucatan miniature piglets (10 females; mean ± SD age, 15 ± 1 d; mean ± SD weight, 3.14 ± 0.30 kg) were fed 20 test diets with different threonine concentrations, from 0.5 to 6.0 g/100 g total amino acids (AAs; i.e., 20-220% of requirement), and various tissues were analyzed for protein synthesis by administering a flooding dose of [3H]phenylalanine. The whole-body requirement was determined by [1-14C]phenylalanine oxidation and plasma threonine concentrations.
RESULTS:
Breakpoint analysis indicated a whole-body requirement of 2.8-3.0 g threonine/100 g total AAs. For all of the non-mucin-producing tissues as well as lung and colon, breakpoint analyses indicated decreasing protein synthesis rates below the following concentrations (expressed in g threonine/100 g total AAs; mean ± SE): gastrocnemius muscle, 1.76 ± 0.23; longissimus dorsi muscle, 2.99 ± 0.50; liver, 2.45 ± 0.60; kidney, 3.81 ± 0.97; lung, 1.95 ± 0.14; and colon, 1.36 ± 0.29. Protein synthesis in the other mucin-producing tissues (i.e., stomach, proximal jejunum, midjejunum, and ileum) did not change with decreasing threonine concentrations, but mucin synthesis in the ileum and colon decreased over threonine concentrations <4 .54="" 1.50="" 4.70="" aas="" and="" g="" nbsp="" p="" respectively.="" total="">CONCLUSIONS:
breakpoint; indicator amino acid oxidation; intestine; organ; requirement PMID: 28053172 DOI: 10.3945/jn.116.236786 [Indexed for MEDLINE]




AIEMPIA muistiinpanoja treoniinista:
Utkast
0
3
2017-07-05

0
58
2017-07-05

3
36
2017-07-05

0
91
2017-07-04
Threonine
Kuten sanottu  1900-luvun puolella  tiedettiin että treoniini on essentielli,mutta pohdittiin mihin sitä oikein tarvitaan ja mitkä sen funktiot ovat. Nyt olen sitä mieltä että sen merkitys  proteiinistruktuureissa on sen osuus musiinien rakenteessa. ja  sen kuluminen musiinien rakentumiseen  voi olla proteiinimetabolian rajoittava tekijä.  MUSIINIT ja TREONIINI aiheesta. 2019, joulukuun 12 päivä.

lördag 12 oktober 2019

PRRG2 (PPXY ja PY motiivin omaava proliinipitoinen VKDP proteiini.

 Tästä proteiini PRGP2 tekstistä käy ilmi, että myös tämä sitoo hyaluronaania ja juuri sen GLA-domeeni toimii hyaluronaania sitovana. Siis  hyaluronaanin sitovuus riippuu  K1-vitamiinistatuksesta.
 
Official Symbol
PRRG2provided by HGNC
Official Full Name
proline rich and Gla domain 2
Also known as
PRGP2
Summary
The protein encoded by this gene is a single-pass transmembrane protein containing an N-terminal gamma-carboxyglutamic acid (Gla) domain and tandem Pro/Leu-Pro-Xaa-Tyr (PY) motifs at its C-terminal end. The Gla domain is exposed on the cell surface while the PY motifs are cytoplasmic. The PY motifs of the encoded protein have been shown to interact with YAP1, a WW domain-containing protein. Therefore, it is thought that the encoded protein may be part of a signal transduction pathway. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2015]
Expression
Broad expression in duodenum (RPKM 5.0), thyroid (RPKM 4.3) and 18 other tissues See more
Orthologs

HA ja hyaluronaania sitova proteiini PRGP1

https://www.degruyter.com/view/j/revneuro.2017.28.issue-8/revneuro-2017-0017/revneuro-2017-0017.xml
2017:  Abstract
Mutant mice deficient in hyaluronan (HA) have an epileptic phenotype.
 HA is one of the major constituents of the brain extracellular matrix.
HA has a remarkable hydration capacity, and a lack of HA causes reduced extracellular space (ECS) volume in the brain.
Reducing ECS volume can initiate or exacerbate epileptiform activity in many in vitro models of epilepsy.
 There is both in vitro and in vivo evidence of a positive feedback loop between reduced ECS volume and synchronous neuronal activity.

  Reduced ECS volume promotes epileptiform activity primarily via enhanced ephaptic interactions and increased extracellular potassium (kalium) concentration; however, the epileptiform activity in many models, including the brain slices from HA synthase-3 (HAS3)  knockout mice, may still require glutamate-mediated synaptic activity. In brain slice epilepsy models, hyperosmotic solution can effectively shrink cells and thus increase ECS volume and block epileptiform activity. However, in vivo, the intravenous administration of hyperosmotic solution shrinks both brain cells and brain ECS volume. Instead, manipulations that increase the synthesis of high-molecular-weight HA or decrease its breakdown may be used in the future to increase brain ECS volume and prevent seizures in patients with epilepsy. The prevention of epileptogenesis is also a future target of HA manipulation. Head trauma, ischemic stroke, and other brain insults that initiate epileptogenesis are known to be associated with an early decrease in high-molecular-weight HA, and preventing that decrease in HA may prevent the epileptogenesis.
Keywords: anticonvulsant; ephaptic; epilepsy; extracellular matrix; hyaluronic acid; potassium

Mitä Hyaluronaanista sanotaan: Sitä esiintyy  solun ulko ja sisäpuolella. 

Löytyy tuoretta artikkelia solun sisällä olevasta hyaluronaanista. 
2019 Jul 2. pii: S1044-579X(19)30130-0. doi: 10.1016/j.semcancer.2019.07.002. [Epub ahead of print]
Intracellular hyaluronan: Importance for cellular functions.
Hyaluronan-rich matrices are abundant in ECM and are involved in biological processes, such as cell growth and migration.
Hyaluronan is synthesized by the hyaluronan synthase family of enzymes, HAS1, HAS2 and HAS3; the HAS1 and HAS3 genes give rise to different transcripts through alternative splicing, and the HAS2 gene to a non-coding RNA antisense transcript in addition to the protein-coding transcript. Biosynthesis of hyaluronan increases during inflammation and cancer and is regulated by cytokines and growth factors.
In addition to extracellular hyaluronan-rich matrices,
cytoplasmic and nuclear forms of hyaluronan have been detected in normal and pathological processes.
Extra- and intra-cellular hyaluronan binds to hyaluronan binding proteins, such as CD44, RHAMM, CDC37 and USP17, affecting cellular behavior.
 Although neither the exact mechanisms by which hyaluronan is present in the intracellular compartments, nor its function at these sites are currently understood, there are evidence that intracellular hyaluronan has important regulatory roles during cell cycle, cell motility, RNA translation and splicing, and autophagy.
KEYWORDS:
CD44; Cancer; Cellular stress; HAS; Hyaluronan; Inflammation; RHAMM

Synapsin kuva  alla. se on uutta   elokuulta 2019. 

 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6747153/figure/ijms-20-04108-f001/
t:

torsdag 20 juni 2019

Tyrosiinin katabolia: Maleylasetoasetaatti.-isomeraasi GSTZ1(14q24.3), MAA1

https://www.ncbi.nlm.nih.gov/gene/2954
Official Symbol
GSTZ1p
Official Full Name
glutathione S-transferase zeta 1
Also known as
MAI; MAAI; MAAID; GSTZ1-1
Summary
This gene is a member of the glutathione S-transferase (GSTs) super-family which encodes multifunctional enzymes important in the detoxification of electrophilic molecules, including carcinogens, mutagens, and several therapeutic drugs, by conjugation with glutathione. This enzyme catalyzes the conversion of maleylacetoacetate to fumarylacetoacatate, which is one of the steps in the phenylalanine/tyrosine degradation pathway. Deficiency of a similar gene in mouse causes oxidative stress. Several transcript variants of this gene encode multiple protein isoforms. [provided by RefSeq, Jul 2015]
Expression  Broad expression in liver (RPKM 23.8), testis (RPKM 10.9) and 24 other tissues See more  Orthologs mouse all
 
Preferred Names
maleylacetoacetate isomerase
Names
S-(hydroxyalkyl)glutathione lyase
glutathione S-alkyltransferase
glutathione S-aralkyltransferase
glutathione S-aryltransferase
glutathione transferase zeta 1
maleylacetone isomerase
 Features: https://www.ncbi.nlm.nih.gov/protein/NP_001299589.1
Conserved Domains (1) summary
cl25459
Location:1156
GstA; Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]
 
  Related articles PubMed

GeneRIFs: Gene References Into Functions


Tyrosiinin katabolia. Tyrosinemia i on katabolian viimeisen entsyymin FAH vajetta .

Jos FAH-geeni(15q25.19 on mutatoitunut ja FAH-entsyymistä on puutetta, ilmenee perinnöllistä tyypin 1 tyrosiiniemiaa. Tähän ollaan kehittelemässä  geenikorjausterapiaa ja geenitutkimus edistyy, kertoo Duodecim  12/2019, s. 1120.
Official Symbol
FAH
Official Full Name
fumarylacetoacetate hydrolase
Summary
This gene encodes the last enzyme in the tyrosine catabolism pathway. FAH deficiency is associated with Type 1 hereditary tyrosinemia (HT). [provided by RefSeq, Jul 2008]
Expression Broad expression in liver (RPKM 62.1), fat (RPKM 60.9) and 20 other tissues See more
 https://www.ncbi.nlm.nih.gov/gene/2184

Preferred Names
fumarylacetoacetase
Names
FAA
beta-diketonase
epididymis secretory sperm binding protein
fumarylacetoacetate hydrolase (fumarylacetoacetase)


fumarylacetoacetase
This enzyme catalyzes the final step in the breakdown of tyrosine or phenylalanine to fumarate and acetoacetate. [Energy metabolism, Amino acids and amines]
 
 
Live donor liver transplantation for type 1 tyrosinemia: An analysis of 15 patients.

Abstract

Type 1 tyrosinemia is a rare metabolic disorder of the tyrosine degradation pathway. Due to the rarity of the disease, the best evidence literature offers is limited to guidelines based on expert opinions and optimal treatment is still a debate. LT serves as a definitive treatment of the defective metabolic pathway in the liver along with other serious disease manifestations such as LF and HCC. Nitisinone is a relatively new agent that is currently recommended for the medical management of the disease. Its mechanism of action is well understood, and efficacy is well established when started presymptomatically. This study aims to evaluate outcomes of 15 patients with type 1 tyrosinemia who underwent LT in nitisinone era and discuss its effect on prevention of HCC.
A LT database of 1037 patients was reviewed.
 Data from 15 patients with type 1 tyrosinemia were retrospectively analyzed. All the patients except one were treated with nitisinone prior to LT. Most common indications for LT were LF and suspicious nodules. Seven patients had HCC. Mortality rate was 20% (n = 3). Nitisinone treatment has opened new horizons in the management of type 1 tyrosinemia, but LT still remains the only option for the patients developing LF and in the event of HCC. Neonatal screening programs utilizing blood succinyl acetone as the marker should be encouraged especially in the countries, such as Turkey, with high prevalence of consanguineous marriages.

KEYWORDS:

AFP; HCC; NTBC; live donor; phenylalanine restriction


 Bildresultat för fumarylacetoacetate

fredag 10 maj 2019

"Kokonainen sardiini!" Kalan edut nahkoineen ruotoineen.Gelatiini sitagliptiiniin verrattuna

 Asialla on  muitakin ajattelijoita! Eilen jopa!

https://www.ncbi.nlm.nih.gov/pubmed/31068055
2019 May 9:1-10. doi: 10.1080/15321819.2019.1613243. [Epub ahead of print] The proportion-ratio on dipeptidyl aminopeptidase-4 (DP-4) inhibition by gelatin compared to synthetic sitagliptin.

 Dipeptidyyliaminopeptidaasin (DP-4)  esto  gelatiinilla  verrattuna synteettisen sitogliptiinin vaikuttamaan estoon.

Tiivistelmän suomennosta. Abstract

Tässä tutkimuksessa on ollut tarkoituksena määrittää gelatiinin inhibitorinen aktiivisuus  dipeptidyyliaminopeptidaasia 4 (DP-4) kohtaan. Tutkittiin kahta markkinoilla olevaa gelatiinia, naudan gelatiinia ja kalannahan gelatiinia ja yhtä laboratoriossa uutettua gelatiinia, nim. kalan luun ( eli ruodon) gelatiinia , jotka valittiin analyysiin. Joka gelatiinilla on sama protiinimalli( 75- 245 kDa)   geelielektroforeesissa  (Na-dodekyylisulfaattipolyakryyliamidigeeli-elektroforeesissa) keskimääräisen proteiinikonsentraation ollessa 1,72 mg/mL.  Kun mitattiin DP-4-entsyymin estoaktiivisuutta , käytettiin Gly-Pro- p-nitroanilidia  ( dipeptidi-p-nitroanilidia)  substraattina.  Standardina, johon verrattiin, käytettiin  diabeteslääkettä sitogliptiini. Prosentuaaliseen estokykyyn perustuen osoittautui  gelatiini olevan  prospketiivinen DP-inhibiittori.

  • The current study aims to determine the inhibition activity gelatin against dipeptidyl aminopeptidase 4 (DP-4). Two commercial gelatins, i.e., bovine and fish skin gelatin and one extracted (in our laboratory) gelatin, i.e., fish bone gelatin were selected for analysis. Each gelatin have same protein pattern (75-245 kDa) on sodium dodecyl sulfate polyacrylamide gel electrophoresis with mean of protein concentration of 1.72 mg/mL. The inhibition activity was measured on the capacity to inhibit DP-4 by using Gly-Pro-p-nitroanilide as their substrate. The sitagliptin was used as standard comparison. Based on the percent inhibition, gelatin has been shown to be the prospective DP-4 inhibitor.

KEYWORDS:

IV (DPP-4); diabetes mellitus type 2; gelatin; incretin; inhibitory activity
PMID:
31068055
DOI:
10.1080/15321819.2019.1613243
Huom  kulinaarinen virhe: otetaan sardiinista nahka ja ruodot pois- silloin vähenee tämä  sitagliptiinin kaltainen vaikutus. Osa maailman valmiista sardiinipurkkimärästä on näitä ruodottomia ja nahkattomia.