Leta i den här bloggen

onsdag 21 maj 2014

Tulevaisuudessa kai sitten saa kudosteknologisen uusen ohuensuolen ja voi sitten syödä sitä vehnää.

Käytännössä olisi kyllä  halvempi ratkaisu hydrolysoida ja elintarviketeknologisesti muutenkin käsitellä  viljat niin,  että ne eivät ole suolta tuhoavia antigeenejä. Tässä näyttää kohta olevan   tulossa suoliputkeakin teknisesti. kun vain asian avain löytyy.

Isolation and characterization of human primary enterocytes from small intestine using a novel method.

Artikel, refereegranskad vetenskaplig
Författare Priti Chougule
Gustaf Herlenius
Nidia Maritza Hernandez
Pradeep B Patil
Bo Xu
Suchitra Sumitran-Holgersson
Publicerad i Scandinavian journal of gastroenterology
Volym 47
Nummer/häfte 11
Sidor 1334-43
ISSN 1502-7708
Publiceringsår 2012
Publicerad vid Institutionen för kliniska vetenskaper, sektionen för kirurgi och kirurgisk gastroforskning, Avdelningen för kirurgi
Sidor 1334-43
Länkar dx.doi.org/10.3109/00365521.2012.70...
Ämneskategorier Gastroenterologi


Abstract Cell culture studies of enterocytes are important in many fields. However, there are difficulties in obtaining cell lines from adult human intestine, such as microbial contamination of cultures from the tissue samples, short life span of enterocytes, overgrowth of mesenchymal cells, etc. Various model used to obtain adult intestinal cell lines are very complex requiring use of feeder layer or gel matrices. The aim of this study was to establish a novel method for the simple and reproducible isolation of human enterocytes. Enterocytes were isolated from SI samples (n = 5) obtained from cadaveric donors using a mechanical procedure, and separation with immunomagnetic beads coated with anti-EpCAM antibodies. Light and electron microscopy, flow cytometry and immunocytochemistry techniques were used to characterize the isolated cells. Immunohistochemical staining of normal SB biopsies confirmed that the cell cultures maintained an in vivo phenotype as reflected in cytokeratin expression CK18, CK20 and expression of intestine-specific markers such as sucrase isomaltase and maltase glucoamylase. Furthermore, the cells strongly expressed TLR-5, 6, 7, 8 and 10 and several molecules such as CD40, CD86, CD44, ICAM-1 and HLA-DR which are important in triggering cell-mediated immune responses. This novel technique provides a unique in vitro system to study the biology of enterocytes in normal conditions as well as to study inflammatory processes in various small bowel disorders.
Till sidans topp

måndag 19 maj 2014

Gluteenittoman dieetin pioneeri W K Dicke (1905- 1962)

Pioneer in the gluten free diet: Willem-Karel Dicke 1905-1962, over 50 years of gluten free diet.

Author information ► Copyright and License information ►

Willem Karel Dicke

From Wikipedia, the free encyclopedia
Willem Karel Dicke (15 February 1905, Dordrecht – 1962, De Bilt) was a Dutch paediatrician who was the first to develop the gluten-free diet and to show that in coeliac disease some types of flour cause relapse.[1]
From 1922 until 1929 Willem Dicke studied medicine in Leiden, then specialized in paediatry in Juliana Children's Hospital in Hague from 1929 until 1933. In 1936, being just 31 years old, he became the medical director of the hospital. In the 1940s and 1950s he went on to develop the gluten-free diet, changing the way of treatment and destinies of children sick with coeliac disease. In 1957 he was appointed a professor of Utrecht University and became a medical director of Wilhelmina Children's Hospital.
Netherlands' Society of Gastroenterology had instituted in his honor a decoration to reward the pioneering research in the field, and Willem was the first to receive the gold Dicke Medal.[2]


  1. van Berge-Henegouwen G, Mulder C (1993). "Pioneer in the gluten free diet: Willem-Karel Dicke 1905–1962, over 50 years of gluten free diet". Gut 34 (11): 1473–5. doi:10.1136/gut.34.11.1473. PMC 1374403. PMID 8244125.
  2. Stoop, J.W. (September 1991). "Willem Karel Dicke: 1905–1962". European Journal of Pediatrics 150 (11): 751. doi:10.1007/BF02026703. ISSN 0340-6199. OCLC 42895341.

W.K. Dicke havaitsi vuonna 1950, että keliakiaa triggeröi vehnäproteiinin syöminen. joillain yksilöillä

Wheat and its close relatives, rye and barley
Since the discovery by W. K. Dicke in 1950 that wheat was a key environmental factor that triggered celiac disease in susceptible individuals, the relationship of the disease to ingestion of wheat gluten proteins has become an essential part of the definition. By and large, if wheat doesn’t trigger enteropathy (or at least, changes in the mucosa that presage enteropathy), it isn’t celiac disease. Most reviews of celiac disease tend to avoid the question of toxicity, or lack thereof, in grains, seeds, or foods other than wheat—possibly because studies are lacking or inadequate. This may be reasonable from a scientific standpoint, but patients, dietitians, and primary care physicians would like something more. Only wheat and, in recent years, oats have been extensively studied with modern approaches (such as measurement of intraepithelial lymphocyte infiltration and cytokine production) for their toxicity in celiac disease—with wheat obviously being toxic, whereas evidence for the lack of toxicity of oats has now become quite strong (see below). Rye and barley have many identical or nearly identical storage proteins to those in wheat. Although testing is rather minimal, these strong protein sequence similarities, combined with the experience of celiac patients over many years with these grains and what scientific investigations have been carried out, are supportive of some degree of toxicity for these grains in celiac disease. It is very difficult to quantify the toxicity of any given grain, but I think it is at least possible that the lack of a-type gliadins (one of the most studied fractions in wheat) in rye and barley results in lesser toxicity for these two grains in comparison with wheat, as does the generally lower protein percentages of rye and barley grain.

Gluteenin koostumus lektiinit ja proteiinit


Milloin gluteeni keksittiin? Milloin sen rakenne selvitettiin?

On edistytty suuresti 1990 luvulta lähtien gluteenin rakenteen selvittämisessä. Nyyisin voidaan molekyylirakenne piirtää kaavana.

Philos Trans R Soc Lond B Biol Sci. Feb 28, 2002; 357(1418): 133–142.
PMCID: PMC1692935

The structure and properties of gluten: an elastic protein from wheat grain.


The wheat gluten proteins correspond to the major storage proteins that are deposited in the starchy endosperm cells of the developing grain. These form a continuous proteinaceous matrix in the cells of the mature dry grain and are brought together to form a continuous viscoelastic network when flour is mixed with water to form dough. These viscoelastic properties underpin the utilization of wheat to give bread and other processed foods. One group of gluten proteins, the HMM subunits of glutenin, is particularly important in conferring high levels of elasticity (i.e. dough strength). These proteins are present in HMM polymers that are stabilized by disulphide bonds and are considered to form the 'elastic backbone' of gluten. However, the glutamine-rich repetitive sequences that comprise the central parts of the HMM subunits also form extensive arrays of interchain hydrogen bonds that may contribute to the elastic properties via a 'loop and train' mechanism. Genetic engineering can be used to manipulate the amount and composition of the HMM subunits, leading to either increased dough strength or to more drastic changes in gluten structure and properties.

Full Text

The Full Text of this article is available as a PDF (793K).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Barro F, Rooke L, Békés F, Gras P, Tatham AS, Fido R, Lazzeri PA, Shewry PR, Barceló P. Transformation of wheat with high molecular weight subunit genes results in improved functional properties. Nat Biotechnol. 1997 Nov;15(12):1295–1299. [PubMed]
  • Belton PS, Colquhoun IJ, Grant A, Wellner N, Field JM, Shewry PR, Tatham AS. FTIR and NMR studies on the hydration of a high-M(r) subunit of glutenin. Int J Biol Macromol. 1995 Apr;17(2):74–80. [PubMed]
  • Field JM, Shewry PR, Miflin BJ. Solubilisation and characterisation of wheat gluten proteins: correlations between the amount of aggregated proteins and baking quality. J Sci Food Agric. 1983 Apr;34(4):370–377. [PubMed]
  • Field JM, Tatham AS, Shewry PR. The structure of a high-Mr subunit of durum-wheat (Triticum durum) gluten. Biochem J. 1987 Oct 1;247(1):215–221. [PMC free article] [PubMed]
  • Gilbert SM, Wellner N, Belton PS, Greenfield JA, Siligardi G, Shewry PR, Tatham AS. Expression and characterisation of a highly repetitive peptide derived from a wheat seed storage protein. Biochim Biophys Acta. 2000 Jun 15;1479(1-2):135–146. [PubMed]
  • Keck B, Köhler P, Wieser H. Disulphide bonds in wheat gluten: cystine peptides derived from gluten proteins following peptic and thermolytic digestion. Z Lebensm Unters Forsch. 1995 Jun;200(6):432–439. [PubMed]
  • Köhler P, Belitz HD, Wieser H. Disulphide bonds in wheat gluten: isolation of a cystine peptide from glutenin. Z Lebensm Unters Forsch. 1991 Mar;192(3):234–239. [PubMed]
  • Köhler P, Belitz HD, Wieser H. Disulphide bonds in wheat gluten: further cystine peptides from high molecular weight (HMW) and low molecular weight (LMW) subunits of glutenin and from gamma-gliadins. Z Lebensm Unters Forsch. 1993 Mar;196(3):239–247. [PubMed]
  • Miles MJ, Carr HJ, McMaster TC, I'Anson KJ, Belton PS, Morris VJ, Field JM, Shewry PR, Tatham AS. Scanning tunneling microscopy of a wheat seed storage protein reveals details of an unusual supersecondary structure. Proc Natl Acad Sci U S A. 1991 Jan 1;88(1):68–71. [PMC free article] [PubMed]
  • Napier JA, Richard G, Turner MF, Shewry PR. Trafficking of wheat gluten proteins in transgenic tobacco plants: gamma-gliadin does not contain an endoplasmic reticulum-retention signal. Planta. 1997 Dec;203(4):488–494. [PubMed]
  • Popineau Y, Deshayes G, Lefebvre J, Fido R, Tatham AS, Shewry PR. Prolamin aggregation, gluten viscoelasticity, and mixing properties of transgenic wheat lines expressing 1Ax and 1Dx high molecular weight glutenin subunit transgenes. J Agric Food Chem. 2001 Jan;49(1):395–401. [PubMed]
  • Shwry PR, Tatham AS, Barro F, Barcelo P, Lazzeri P. Biotechnology of breadmaking: unraveling and manipulating the multi-protein gluten complex. Biotechnology (N Y) 1995 Nov;13(11):1185–1190. [PubMed]
  • Tao HP, Adalsteins AE, Kasarda DD. Intermolecular disulfide bonds link specific high-molecular-weight glutenin subunits in wheat endosperm. Biochim Biophys Acta. 1992 Sep 4;1159(1):13–21. [PubMed]
  • Urry DW. Entropic elastic processes in protein mechanisms. I. Elastic structure due to an inverse temperature transition and elasticity due to internal chain dynamics. J Protein Chem. 1988 Feb;7(1):1–34. [PubMed]
  • Van Dijk AA, De Boef E, Bekkers A, Van Wijk LL, Van Swieten E, Hamer RJ, Robillard GT. Structure characterization of the central repetitive domain of high molecular weight gluten proteins. II. Characterization in solution and in the dry state. Protein Sci. 1997 Mar;6(3):649–656. [PMC free article] [PubMed]
  • Van Dijk AA, Van Wijk LL, Van Vliet A, Haris P, Van Swieten E, Tesser GI, Robillard GT. Structure characterization of the central repetitive domain of high molecular weight gluten proteins. I. Model studies using cyclic and linear peptides. Protein Sci. 1997 Mar;6(3):637–648. [PMC free article] [PubMed]
  • Wellner N, Belton PS, Tatham AS. Fourier transform IR spectroscopic study of hydration-induced structure changes in the solid state of omega-gliadins. Biochem J. 1996 Nov 1;319(Pt 3):741–747. [PMC free article] [PubMed]