Direct evidence that ganglioside is an integral component of the thyrotropin receptor

W. Kielczynski; L. C. Harrison; P. J. Leedman

doi:10.1073/pnas.88.5.1991

Direct evidence that ganglioside is an integral component of the thyrotropin receptor

W. Kielczynski, L. C. Harrison, P. J. Leedman

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

30 Citations (Scopus)

Abstract

Gangliosides were extracted from purified human and porcine thyrotropin (TSH) receptors (TSH-R) and were detected by probing with an ¹²⁵I-labeled sialic acid-specific lectin, Limax flavus agglutinin. Gangliosides copurified with human and porcine TSH-R migrated between monosialoganglioside GM1 and disialoganglioside GD1a. Ceramide glycanase digestion of the purified human TSH-R-associated glycolipid confirmed its ganglioside nature. It was resistant to Vibrio cholerae sialidase, which digests all gangliosides except GM1, but was sensitive to Arthrobacter ureafaciens sialidase, which digests all gangliosides including GM1. These findings indicate that the human TSH-R contains ganglioside that belongs to the galactosyl(β1 → 3)-N-acetylgalactosaminyl(β1 → 4)-[N-acetylneuraminyl(α2 → 3)]galactosyl(β1 → 4)glucosyl(β1 → 1)ceramide (GM1) family. Its intimate association with receptor protein role for ganglioside in the structure and function of the TSH-R.

Original language	English
Pages (from-to)	1991-1995
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	88
Issue number	5
DOIs	https://doi.org/10.1073/pnas.88.5.1991
Publication status	Published - 1991
Externally published	Yes

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10.1073/pnas.88.5.1991

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title = "Direct evidence that ganglioside is an integral component of the thyrotropin receptor",

abstract = "Gangliosides were extracted from purified human and porcine thyrotropin (TSH) receptors (TSH-R) and were detected by probing with an 125I-labeled sialic acid-specific lectin, Limax flavus agglutinin. Gangliosides copurified with human and porcine TSH-R migrated between monosialoganglioside GM1 and disialoganglioside GD1a. Ceramide glycanase digestion of the purified human TSH-R-associated glycolipid confirmed its ganglioside nature. It was resistant to Vibrio cholerae sialidase, which digests all gangliosides except GM1, but was sensitive to Arthrobacter ureafaciens sialidase, which digests all gangliosides including GM1. These findings indicate that the human TSH-R contains ganglioside that belongs to the galactosyl(β1 → 3)-N-acetylgalactosaminyl(β1 → 4)-[N-acetylneuraminyl(α2 → 3)]galactosyl(β1 → 4)glucosyl(β1 → 1)ceramide (GM1) family. Its intimate association with receptor protein role for ganglioside in the structure and function of the TSH-R.",

keywords = "ceramide glycanase, glycolipid, Limax flavus agglutinin, sialidases, thyroid-stimulating hormone",

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year = "1991",

doi = "10.1073/pnas.88.5.1991",

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AU - Kielczynski, W.

AU - Harrison, L. C.

AU - Leedman, P. J.

PY - 1991

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N2 - Gangliosides were extracted from purified human and porcine thyrotropin (TSH) receptors (TSH-R) and were detected by probing with an 125I-labeled sialic acid-specific lectin, Limax flavus agglutinin. Gangliosides copurified with human and porcine TSH-R migrated between monosialoganglioside GM1 and disialoganglioside GD1a. Ceramide glycanase digestion of the purified human TSH-R-associated glycolipid confirmed its ganglioside nature. It was resistant to Vibrio cholerae sialidase, which digests all gangliosides except GM1, but was sensitive to Arthrobacter ureafaciens sialidase, which digests all gangliosides including GM1. These findings indicate that the human TSH-R contains ganglioside that belongs to the galactosyl(β1 → 3)-N-acetylgalactosaminyl(β1 → 4)-[N-acetylneuraminyl(α2 → 3)]galactosyl(β1 → 4)glucosyl(β1 → 1)ceramide (GM1) family. Its intimate association with receptor protein role for ganglioside in the structure and function of the TSH-R.

AB - Gangliosides were extracted from purified human and porcine thyrotropin (TSH) receptors (TSH-R) and were detected by probing with an 125I-labeled sialic acid-specific lectin, Limax flavus agglutinin. Gangliosides copurified with human and porcine TSH-R migrated between monosialoganglioside GM1 and disialoganglioside GD1a. Ceramide glycanase digestion of the purified human TSH-R-associated glycolipid confirmed its ganglioside nature. It was resistant to Vibrio cholerae sialidase, which digests all gangliosides except GM1, but was sensitive to Arthrobacter ureafaciens sialidase, which digests all gangliosides including GM1. These findings indicate that the human TSH-R contains ganglioside that belongs to the galactosyl(β1 → 3)-N-acetylgalactosaminyl(β1 → 4)-[N-acetylneuraminyl(α2 → 3)]galactosyl(β1 → 4)glucosyl(β1 → 1)ceramide (GM1) family. Its intimate association with receptor protein role for ganglioside in the structure and function of the TSH-R.

KW - ceramide glycanase

KW - glycolipid

KW - Limax flavus agglutinin

KW - sialidases

KW - thyroid-stimulating hormone

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AN - SCOPUS:0026012158

SN - 0027-8424

VL - 88

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EP - 1995

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

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ER -

Direct evidence that ganglioside is an integral component of the thyrotropin receptor

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