Studies on the aetiology of coeliac disease: No evidence for lectin-like components in wheat gluten

Rühlmann, Jörg; Sinha, Pranav; Hansen, G.; Tauber, Rudolf; Köttgen, E.

doi:10.1016/0925-4439(93)90028-y

Cited by 11 publications

(4 citation statements)

References 40 publications

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“…O ur data of multiple binding site s do not support the hypothe sis of distinct re ceptors for food prote ins comparable to the e nzyme aminope ptidase N as a receptor for coronavirus (39) . Moreover, prote in± oligosaccharide inte ractions le ading to membrane attachme nt could be e xclude d be cause food prote in (27,40) . In our opinion, prote in± prote in inte ractions are responsible for food prote in attachme nt to BBM.…”

Section: Discussionmentioning

confidence: 99%

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Bolte¹,

Knauss²,

Metzdorf³

et al. 1998

Digestive Diseases and Sciences

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To investigate maturational changes of membrane food protein binding capacity, we studied binding characteristics of brush border membranes isolated from small intestines of newborn and adult rats. Binding of biotinylated gliadin peptides, cow's milk proteins (alpha-casein, beta-lactoglobulin, alpha-lactalbumin, bovine serum albumin) and lectins was assessed by a sensitive chemiluminescence blot assay. We found specific food protein binding with regard to saturation and inhibition. Maximal binding of most food proteins and several lectins to brush border membranes of newborn and adult rats was comparable, whereas binding of beta-lactoglobulin was substantially less. Common or adjoining binding sites for the different food proteins tested were indicated by corresponding membrane protein binding patterns and by inhibition properties of unrelated proteins. Compared to newborns, adult membrane vesicles as well as isolated membrane proteins showed higher binding capacities. Thus postnatal maturation of small intestinal brush border membranes correlated with increased food protein binding capacity.

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Section: Discussionmentioning

confidence: 99%

Untitled

Bolte¹,

Knauss²,

Metzdorf³

et al. 1998

Digestive Diseases and Sciences

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“…Finally, other cells, including intestinal stem cells [22] and Paneth cells (including their alpha-defensins), if altered by lectin binding activities, may provide a key role in linking the microbiome with celiac disease [23]. Previously, several investigators [24,25,26] hypothesized that gluten acts as a lectin, binding to specific oligosaccharide structures of the intestinal epithelial cell surface and causing cell toxicity, but this hypothesis has been considered to be controversial [20,27]. Some recent evidence has accumulated to show that gliadin and gluten peptides may behave like lectins with the ability to bind to high mannose-type glycoproteins in human serum as well as immature crypt cells in rat intestine [24,25].…”

Section: Celiac Disease and The Lectin Hypothesismentioning

confidence: 99%

Topographic Lectin Mapping of the Epithelial Cell Surface in Normal Intestine and Celiac Disease

Freeman¹

2019

IJCD

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The etiology and pathogenesis of celiac disease remains obscure but remains the focus of intense research investigation. It is generally believed to be an immune-mediated small intestinal mucosal disorder that can cause diarrhea, impaired nutrient assimilation and weight loss. A key component in this process occurs at the intestinal epithelial cell surface that is closely associated with the luminal intestinal microbiome. Here, epithelial membrane glycoproteins and glycolipids are present along with adsorbed molecules that permit interaction with the intestinal microbiome. In recent years, use of specific sugar residue seeking proteins, lectins, that can be found in the diet have been employed topographically to map the small intestinal cell surface and goblet cell secretory mucins to further elucidate the structure and function of this tissue. Evidence has accumulated to indicate that this microenvironment may be critically important in further understanding the etiology and pathogenesis of celiac disease and other sprue-like intestinal disorders.

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“…In CD, it was hypothesized that this binding to the brush border would initiate a series of toxic events, which indeed some investigators were able to show in vitro [31,32]. This hypothesis persisted throughout the 80s and only in the early 90s was it challenged and definitively put to rest [33] in the face of the rising fortune of the 'immunological theory' that was quickly gaining ground.…”

Section: Progress In Understanding the Pathogenesismentioning

confidence: 99%

Historical Perspective of Celiac Disease

Guandalini¹

2008

Frontiers in Celiac Disease

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Studies on the aetiology of coeliac disease: No evidence for lectin-like components in wheat gluten

Cited by 11 publications

References 40 publications

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Topographic Lectin Mapping of the Epithelial Cell Surface in Normal Intestine and Celiac Disease

Historical Perspective of Celiac Disease

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