Functional glycosylation of human podoplanin: Glycan structure of platelet aggregation-inducing factor

Mika Kato Kaneko; Yukinari Kato; Akihiko Kameyama; Hiromi Ito; Atsushi Kuno; Jun Hirabayashi; Tomomi Kubota; Koh Amano; Yasunori Chiba; Yasushi Hasegawa; Isoji Sasagawa; Kazuhiko Mishima; Hisashi Narimatsu

doi:10.1016/j.febslet.2006.12.044

Functional glycosylation of human podoplanin: Glycan structure of platelet aggregation-inducing factor

Mika Kato Kaneko, Yukinari Kato, Akihiko Kameyama, Hiromi Ito, Atsushi Kuno, Jun Hirabayashi, Tomomi Kubota, Koh Amano, Yasunori Chiba, Yasushi Hasegawa, Isoji Sasagawa, Kazuhiko Mishima, Hisashi Narimatsu

Department of Surgery (General and Gastroenterological Surgery)

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

92 Citations (Scopus)

Abstract

Podoplanin (Aggrus) is a mucin-type sialoglycoprotein that plays a key role in tumor cell-induced platelet aggregation. Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity. Endogenous or recombinant human podoplanin were purified, and total glycosylation profiles were surveyed by lectin microarray. Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAcα2-3Galβl-3(NeuAcα2-6)GalNAcαl-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52. Sialic acid-deficient podoplanin recovered its activity after additional sialylation. These results indicated that the sialylated Corel at Thr52 is critical for podoplanin-induced platelet aggregation.

Original language	English
Pages (from-to)	331-336
Number of pages	6
Journal	FEBS Letters
Volume	581
Issue number	2
DOIs	https://doi.org/10.1016/j.febslet.2006.12.044
Publication status	Published - 2007 Jan 23

Keywords

Disialyl-T
Disialyl-corel
Platelet aggregation
Podoplanin

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2006.12.044

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@article{3c6b0d2c9d96460a9e34e09321a111f4,

title = "Functional glycosylation of human podoplanin: Glycan structure of platelet aggregation-inducing factor",

abstract = "Podoplanin (Aggrus) is a mucin-type sialoglycoprotein that plays a key role in tumor cell-induced platelet aggregation. Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity. Endogenous or recombinant human podoplanin were purified, and total glycosylation profiles were surveyed by lectin microarray. Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAcα2-3Galβl-3(NeuAcα2-6)GalNAcαl-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52. Sialic acid-deficient podoplanin recovered its activity after additional sialylation. These results indicated that the sialylated Corel at Thr52 is critical for podoplanin-induced platelet aggregation.",

keywords = "Disialyl-T, Disialyl-corel, Platelet aggregation, Podoplanin",

author = "Kaneko, {Mika Kato} and Yukinari Kato and Akihiko Kameyama and Hiromi Ito and Atsushi Kuno and Jun Hirabayashi and Tomomi Kubota and Koh Amano and Yasunori Chiba and Yasushi Hasegawa and Isoji Sasagawa and Kazuhiko Mishima and Hisashi Narimatsu",

note = "Funding Information: We thank Ms. Kahori Tachibana, Ms. Sanae Furukawa, Ms. Kozue Hagiwara, Ms. Yuki Tsunoda, and Mr. Noboru Uchiyama for their technical assistance. We are very grateful to Drs. Webster K Cavenee, Naoya Fujita, and Takashi Tsuruo for their generous donation of materials. This work was performed as a part of the Medical Glycomics Project supported by NEDO (New Energy and Industrial Technology Development Organization). This study was supported in part by a grant for Research Fellowships from the Japanese Society for the Promotion of Science (Y. Kato), by Kanae Foundation for Life and Socio-medical Science (Y. Kato), and by the Osaka Cancer Research Foundation (Y. Kato).",

year = "2007",

month = jan,

day = "23",

doi = "10.1016/j.febslet.2006.12.044",

language = "English",

volume = "581",

pages = "331--336",

journal = "FEBS Letters",

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TY - JOUR

T1 - Functional glycosylation of human podoplanin

T2 - Glycan structure of platelet aggregation-inducing factor

AU - Kaneko, Mika Kato

AU - Kato, Yukinari

AU - Kameyama, Akihiko

AU - Ito, Hiromi

AU - Kuno, Atsushi

AU - Hirabayashi, Jun

AU - Kubota, Tomomi

AU - Amano, Koh

AU - Chiba, Yasunori

AU - Hasegawa, Yasushi

AU - Sasagawa, Isoji

AU - Mishima, Kazuhiko

AU - Narimatsu, Hisashi

N1 - Funding Information: We thank Ms. Kahori Tachibana, Ms. Sanae Furukawa, Ms. Kozue Hagiwara, Ms. Yuki Tsunoda, and Mr. Noboru Uchiyama for their technical assistance. We are very grateful to Drs. Webster K Cavenee, Naoya Fujita, and Takashi Tsuruo for their generous donation of materials. This work was performed as a part of the Medical Glycomics Project supported by NEDO (New Energy and Industrial Technology Development Organization). This study was supported in part by a grant for Research Fellowships from the Japanese Society for the Promotion of Science (Y. Kato), by Kanae Foundation for Life and Socio-medical Science (Y. Kato), and by the Osaka Cancer Research Foundation (Y. Kato).

PY - 2007/1/23

Y1 - 2007/1/23

N2 - Podoplanin (Aggrus) is a mucin-type sialoglycoprotein that plays a key role in tumor cell-induced platelet aggregation. Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity. Endogenous or recombinant human podoplanin were purified, and total glycosylation profiles were surveyed by lectin microarray. Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAcα2-3Galβl-3(NeuAcα2-6)GalNAcαl-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52. Sialic acid-deficient podoplanin recovered its activity after additional sialylation. These results indicated that the sialylated Corel at Thr52 is critical for podoplanin-induced platelet aggregation.

AB - Podoplanin (Aggrus) is a mucin-type sialoglycoprotein that plays a key role in tumor cell-induced platelet aggregation. Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity. Endogenous or recombinant human podoplanin were purified, and total glycosylation profiles were surveyed by lectin microarray. Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAcα2-3Galβl-3(NeuAcα2-6)GalNAcαl-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52. Sialic acid-deficient podoplanin recovered its activity after additional sialylation. These results indicated that the sialylated Corel at Thr52 is critical for podoplanin-induced platelet aggregation.

KW - Disialyl-T

KW - Disialyl-corel

KW - Platelet aggregation

KW - Podoplanin

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U2 - 10.1016/j.febslet.2006.12.044

DO - 10.1016/j.febslet.2006.12.044

M3 - Article

C2 - 17222411

AN - SCOPUS:33846257761

SN - 0014-5793

VL - 581

SP - 331

EP - 336

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

Functional glycosylation of human podoplanin: Glycan structure of platelet aggregation-inducing factor

Abstract

Keywords

ASJC Scopus subject areas

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