Native and/or asialo-Tamm-Horsfall glycoproteins Sd(a+) are important receptors for Triticum vulgaris (wheat germ) agglutinin and for three toxic lectins (abrin-a, ricin and mistletoe toxic lectin-I)

Albert M. Wu; Winifred M. Watkins; Chie Pein Chen; Shuh Chyung Song; Lu Ping Chow; Jung Yaw Lin

doi:10.1016/0014-5793(95)00862-4

Native and/or asialo-Tamm-Horsfall glycoproteins Sd(a⁺) are important receptors for Triticum vulgaris (wheat germ) agglutinin and for three toxic lectins (abrin-a, ricin and mistletoe toxic lectin-I)

Albert M. Wu^*, Winifred M. Watkins, Chie Pein Chen, Shuh Chyung Song, Lu Ping Chow, Jung Yaw Lin

^*Corresponding author for this work

Department of Molecular Biology

Research output: Contribution to journal › Journal Article › peer-review

19 Scopus citations

Abstract

The binding properties of human Tamm-Horsfall Sd(a⁺) urinary glycoprotein (THGP) and asialo-THGP with Triticum vulgaris agglutinin(WGA) and three toxic lectins (abrin-a, ricin, and Mistletoe toxic lectin-I) were investigated by quantitative precipitin and precipitin inhibition assays. Both glycoproteins reacted strongly with abrin-a, precipitating over 80% of the lectin nitrogen tested. THGP also bound well to mistletoe toxic lectin-I and precipitated 86% of this lectin added, while the precipitability of its asialo product decreased by 28%. The native glycoprotein completely precipitated the WGA added, but its reactivity was reduced dramatically after desialylation. On the contrary, the poor reactivity of THGP with ricin increased substantially after removal of sialic acid and completely precipitated the lectin added. The glycoprotein-lectin interactions were inhibited by one or several of the following haptens, p-NO₂-phenylαGalNAc, p-NO₂-phenylβGalNAc, Galβ1→4GlcNAc, Galβ1→4Glc, GlcNAcβ1→4GlcNAc, and/or GlcNAc. From the above results, it is concluded that native and/or asialo Tamm-Horsfall glycoproteins serve as important receptors for these three toxic lectins and for WGA.

Original language	English
Pages (from-to)	32-34
Number of pages	3
Journal	FEBS Letters
Volume	371
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(95)00862-4
State	Published - 28 08 1995

Keywords

Lectin reactivity of abrin-a
ML-I
Native
asialo-Tamm-Horsfall glycoproteins
ricin
wheat germ

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10.1016/0014-5793(95)00862-4

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@article{17053f2a36754217bc363ab77481afee,

title = "Native and/or asialo-Tamm-Horsfall glycoproteins Sd(a+) are important receptors for Triticum vulgaris (wheat germ) agglutinin and for three toxic lectins (abrin-a, ricin and mistletoe toxic lectin-I)",

abstract = "The binding properties of human Tamm-Horsfall Sd(a+) urinary glycoprotein (THGP) and asialo-THGP with Triticum vulgaris agglutinin(WGA) and three toxic lectins (abrin-a, ricin, and Mistletoe toxic lectin-I) were investigated by quantitative precipitin and precipitin inhibition assays. Both glycoproteins reacted strongly with abrin-a, precipitating over 80% of the lectin nitrogen tested. THGP also bound well to mistletoe toxic lectin-I and precipitated 86% of this lectin added, while the precipitability of its asialo product decreased by 28%. The native glycoprotein completely precipitated the WGA added, but its reactivity was reduced dramatically after desialylation. On the contrary, the poor reactivity of THGP with ricin increased substantially after removal of sialic acid and completely precipitated the lectin added. The glycoprotein-lectin interactions were inhibited by one or several of the following haptens, p-NO2-phenylαGalNAc, p-NO2-phenylβGalNAc, Galβ1→4GlcNAc, Galβ1→4Glc, GlcNAcβ1→4GlcNAc, and/or GlcNAc. From the above results, it is concluded that native and/or asialo Tamm-Horsfall glycoproteins serve as important receptors for these three toxic lectins and for WGA.",

keywords = "Lectin reactivity of abrin-a, ML-I, Native, asialo-Tamm-Horsfall glycoproteins, ricin, wheat germ",

author = "Wu, {Albert M.} and Watkins, {Winifred M.} and Chen, {Chie Pein} and Song, {Shuh Chyung} and Chow, {Lu Ping} and Lin, {Jung Yaw}",

year = "1995",

month = aug,

day = "28",

doi = "10.1016/0014-5793(95)00862-4",

language = "英语",

volume = "371",

pages = "32--34",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc",

number = "1",

}

Native and/or asialo-Tamm-Horsfall glycoproteins Sd(a⁺) are important receptors for Triticum vulgaris (wheat germ) agglutinin and for three toxic lectins (abrin-a, ricin and mistletoe toxic lectin-I). / Wu, Albert M.; Watkins, Winifred M.; Chen, Chie Pein et al.
In: FEBS Letters, Vol. 371, No. 1, 28.08.1995, p. 32-34.

Research output: Contribution to journal › Journal Article › peer-review

TY - JOUR

T1 - Native and/or asialo-Tamm-Horsfall glycoproteins Sd(a+) are important receptors for Triticum vulgaris (wheat germ) agglutinin and for three toxic lectins (abrin-a, ricin and mistletoe toxic lectin-I)

AU - Wu, Albert M.

AU - Watkins, Winifred M.

AU - Chen, Chie Pein

AU - Song, Shuh Chyung

AU - Chow, Lu Ping

AU - Lin, Jung Yaw

PY - 1995/8/28

Y1 - 1995/8/28

N2 - The binding properties of human Tamm-Horsfall Sd(a+) urinary glycoprotein (THGP) and asialo-THGP with Triticum vulgaris agglutinin(WGA) and three toxic lectins (abrin-a, ricin, and Mistletoe toxic lectin-I) were investigated by quantitative precipitin and precipitin inhibition assays. Both glycoproteins reacted strongly with abrin-a, precipitating over 80% of the lectin nitrogen tested. THGP also bound well to mistletoe toxic lectin-I and precipitated 86% of this lectin added, while the precipitability of its asialo product decreased by 28%. The native glycoprotein completely precipitated the WGA added, but its reactivity was reduced dramatically after desialylation. On the contrary, the poor reactivity of THGP with ricin increased substantially after removal of sialic acid and completely precipitated the lectin added. The glycoprotein-lectin interactions were inhibited by one or several of the following haptens, p-NO2-phenylαGalNAc, p-NO2-phenylβGalNAc, Galβ1→4GlcNAc, Galβ1→4Glc, GlcNAcβ1→4GlcNAc, and/or GlcNAc. From the above results, it is concluded that native and/or asialo Tamm-Horsfall glycoproteins serve as important receptors for these three toxic lectins and for WGA.

AB - The binding properties of human Tamm-Horsfall Sd(a+) urinary glycoprotein (THGP) and asialo-THGP with Triticum vulgaris agglutinin(WGA) and three toxic lectins (abrin-a, ricin, and Mistletoe toxic lectin-I) were investigated by quantitative precipitin and precipitin inhibition assays. Both glycoproteins reacted strongly with abrin-a, precipitating over 80% of the lectin nitrogen tested. THGP also bound well to mistletoe toxic lectin-I and precipitated 86% of this lectin added, while the precipitability of its asialo product decreased by 28%. The native glycoprotein completely precipitated the WGA added, but its reactivity was reduced dramatically after desialylation. On the contrary, the poor reactivity of THGP with ricin increased substantially after removal of sialic acid and completely precipitated the lectin added. The glycoprotein-lectin interactions were inhibited by one or several of the following haptens, p-NO2-phenylαGalNAc, p-NO2-phenylβGalNAc, Galβ1→4GlcNAc, Galβ1→4Glc, GlcNAcβ1→4GlcNAc, and/or GlcNAc. From the above results, it is concluded that native and/or asialo Tamm-Horsfall glycoproteins serve as important receptors for these three toxic lectins and for WGA.

KW - Lectin reactivity of abrin-a

KW - ML-I

KW - Native

KW - asialo-Tamm-Horsfall glycoproteins

KW - ricin

KW - wheat germ

UR - http://www.scopus.com/inward/record.url?scp=0029116351&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(95)00862-4

DO - 10.1016/0014-5793(95)00862-4

M3 - 文章

C2 - 7664879

AN - SCOPUS:0029116351

SN - 0014-5793

VL - 371

SP - 32

EP - 34

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

Native and/or asialo-Tamm-Horsfall glycoproteins Sd(a⁺) are important receptors for Triticum vulgaris (wheat germ) agglutinin and for three toxic lectins (abrin-a, ricin and mistletoe toxic lectin-I)

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