Soluble Human Intestinal Lactoferrin Receptor: Ca&lt;sup&gt;2+&lt;/sup&gt;-Dependent Binding to Sepharose-Based Matrices

Oshima, Yuta; Seki, Kazuhiko; Shibuya, Masataka; Naka, Yuki; Yokoyama, Tetsuji; Sato, Atsushi

doi:10.1248/bpb.b15-00643

Cited by 5 publications

(2 citation statements)

References 12 publications

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“…Ca 2+ dependent binding is observed for several other lectin–glycan interactions [59, 60]. The Ca 2+ dependence is also previously investigated for carbohydrate–carbohydrate interactions, where it is observed for some glycans [61], whereas in other studies no such dependence [62], or only a weak dependence, is reported [63].…”

Section: Discussionmentioning

confidence: 98%

Interactions between the breast cancer-associated MUC1 mucins and C-type lectin characterized by optical tweezers

et al. 2017

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Carbohydrate–protein interactions govern many crucial processes in biological systems including cell recognition events. We have used the sensitive force probe optical tweezers to quantify the interactions occurring between MGL lectins and MUC1 carrying the cancer-associated glycan antigens mucins Tn and STn. Unbinding forces of 7.6±1.1 pN and 7.1±1.1 pN were determined for the MUC1(Tn)—MGL and MUC1(STn)—MGL interactions, at a force loading rate of ~40 pN/s. The interaction strength increased with increasing force loading rate, to 27.1±4.4 and 36.9±3.6 pN at a force loading rate of ~ 310 pN/s. No interactions were detected between MGL and MUC1(ST), a glycoform of MUC1 also expressed by breast carcinoma cells. Interestingly, this glycan (ST) can be found on proteins expressed by normal cells, although in this case not on MUC1. Additionally, GalNAc decorated polyethylene glycol displayed similar rupture forces as observed for MUC1(Tn) and MUC1(STn) when forced to unbind from MGL, indicating that GalNAc is an essential group in these interactions. Since the STn glycan decoration is more frequently found on the surface of carcinomas than the Tn glycan, the binding of MUC1 carrying STn to MGL may be more physiologically relevant and may be in part responsible for some of the characteristics of STn expressing tumours.

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Section: Discussionmentioning

confidence: 98%

Interactions between the breast cancer-associated MUC1 mucins and C-type lectin characterized by optical tweezers

et al. 2017

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“…5) Moreover, bovine LF (bLF) has been shown to be taken up into 10 d-cultured Caco-2 cells, after which degraded bLF is released back into the culture medium. 6) Another study used spontaneously differentiated cell monolayers of 21 d-cultured Caco-2 as an in vitro model of the intestinal barrier 4) and showed, using a permeability assay, that LF transported across Caco-2 monolayers was more likely to be degraded, 7,8) which was inconsistent with in vivo events. 3) In this study, to confirm the earlier published results, we have reevaluated LF uptake and release by Caco-2 cells.…”

Section: Introductionmentioning

confidence: 99%

Cellular Uptake and Release of Intact Lactoferrin and Its Derivatives in an Intestinal Enterocyte Model of Caco-2 Cells

Matsuzaki

Nakamura

Nogita

et al. 2019

Biological & Pharmaceutical Bulletin

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An Intact form of lactoferrin (LF) is known to be absorbed from the small intestine and transported into the blood circulation. We reevaluated the cellular uptake and release of LF using an enterocyte model of human small intestinal cells derived from the Caco-2 cell line. In contrast to a previous report, we observed that intact bovine LF was taken up into seven and 21 d-cultured Caco-2 cells and successfully released back into the culture medium, even though the human intestinal LF receptor, intelectin-1, was not immunochemically detectable. Similar observations were made for human LF and its derivatives (the N-terminal half of LF designated N-lobe and Fc fusions). These observations regarding the uptake and release of intact LF in Caco-2 cells were consistent with in vivo observations. Therefore, we propose that the uptake and release of intact LF by Caco-2 cells should be assessed as a potential in vitro model of in vivo LF absorption in human intestines.

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Molecular properties and ligand specificity of zebrafish intelectin-2

Singrang

Sitthiyotha

Chomanee

et al. 2022

Fish & Shellfish Immunology

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Soluble Human Intestinal Lactoferrin Receptor: Ca<sup>2+</sup>-Dependent Binding to Sepharose-Based Matrices

Cited by 5 publications

References 12 publications

Interactions between the breast cancer-associated MUC1 mucins and C-type lectin characterized by optical tweezers

Interactions between the breast cancer-associated MUC1 mucins and C-type lectin characterized by optical tweezers

Cellular Uptake and Release of Intact Lactoferrin and Its Derivatives in an Intestinal Enterocyte Model of Caco-2 Cells

Molecular properties and ligand specificity of zebrafish intelectin-2

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