Characterization of a novel cell-surface protein expressed on human sperm

Ruey Bing Yang, Heng Kien Au, Chii Ruey Tzeng, Ming T. Tsai, Ping Wu, Yu Chih Wu, Thai Y. Ling, Yen H. Huang

研究成果: 雜誌貢獻文章

8 引文 (Scopus)

摘要

BACKGROUND: Precise sperm-oocyte interaction is a critical event for successful fertilization. However, the identity of molecules involved in this process in humans remains largely unknown. This report describes the identification and characterization of a novel cell-surface protein and its potential role in human sperm-oocyte interaction. METHODS: AND RESULTSWe previously identified an orphan guanylyl cyclase receptor (mouse GC-G) highly enriched in mouse testis and involved in sperm activation. By using a comparative genomic approach, we found the homologue gene in human (hGC-G) composed of 21 exons, spanning a minimum of 48 kb on chromosome 10q25. Real-time RT-PCR analysis revealed hGC-G mRNA selectively expressed in testis but with low or no expression in all other tissues examined. Compared with mGC-G, the hGC-G transcript contains three 1-bp deletions and two in-frame termination codons, which results in a short putative receptor-like polypeptide. Western blot analysis with an anti-hGC-G-specific antibody confirmed the protein expression of hGC-G in human sperm lysate. Flow cytometry and confocal immunofluorescence analysis demonstrated the localization of hGC-G protein on the acrosome cap and equatorial segment of mature human sperm. In addition, an integrin-binding Arg-Gly-Asp (RGD) motif was found in the extracellular domain of hGC-G. Pre-incubation of the hGC-G RGD peptide with zona pellucida-free oocytes greatly decreased the binding of human sperm to hamster oocytes, which suggests a role for hGC-G role in sperm-oocyte interaction. CONCLUSION: ShGC-G is a novel surface protein on human sperm and potentially mediates sperm-oocyte interaction through its RGD-containing motif.

原文英語
頁(從 - 到)42-51
頁數10
期刊Human Reproduction
25
發行號1
DOIs
出版狀態已發佈 - 一月 2010

指紋

Spermatozoa
Membrane Proteins
Sperm-Ovum Interactions
Oocytes
Testis
Guanylate Cyclase-Coupled Receptors
Zona Pellucida
Acrosome
Orphaned Children
Terminator Codon
GTP-Binding Proteins
Fertilization
Integrins
Cricetinae
Fluorescent Antibody Technique
Real-Time Polymerase Chain Reaction
Exons
Flow Cytometry
Chromosomes
Western Blotting

ASJC Scopus subject areas

  • Obstetrics and Gynaecology
  • Rehabilitation
  • Reproductive Medicine

引用此文

Characterization of a novel cell-surface protein expressed on human sperm. / Yang, Ruey Bing; Au, Heng Kien; Tzeng, Chii Ruey; Tsai, Ming T.; Wu, Ping; Wu, Yu Chih; Ling, Thai Y.; Huang, Yen H.

於: Human Reproduction, 卷 25, 編號 1, 01.2010, p. 42-51.

研究成果: 雜誌貢獻文章

Yang, Ruey Bing ; Au, Heng Kien ; Tzeng, Chii Ruey ; Tsai, Ming T. ; Wu, Ping ; Wu, Yu Chih ; Ling, Thai Y. ; Huang, Yen H. / Characterization of a novel cell-surface protein expressed on human sperm. 於: Human Reproduction. 2010 ; 卷 25, 編號 1. 頁 42-51.
@article{a5edf20aaac54fce93272f645f14969e,
title = "Characterization of a novel cell-surface protein expressed on human sperm",
abstract = "BACKGROUND: Precise sperm-oocyte interaction is a critical event for successful fertilization. However, the identity of molecules involved in this process in humans remains largely unknown. This report describes the identification and characterization of a novel cell-surface protein and its potential role in human sperm-oocyte interaction. METHODS: AND RESULTSWe previously identified an orphan guanylyl cyclase receptor (mouse GC-G) highly enriched in mouse testis and involved in sperm activation. By using a comparative genomic approach, we found the homologue gene in human (hGC-G) composed of 21 exons, spanning a minimum of 48 kb on chromosome 10q25. Real-time RT-PCR analysis revealed hGC-G mRNA selectively expressed in testis but with low or no expression in all other tissues examined. Compared with mGC-G, the hGC-G transcript contains three 1-bp deletions and two in-frame termination codons, which results in a short putative receptor-like polypeptide. Western blot analysis with an anti-hGC-G-specific antibody confirmed the protein expression of hGC-G in human sperm lysate. Flow cytometry and confocal immunofluorescence analysis demonstrated the localization of hGC-G protein on the acrosome cap and equatorial segment of mature human sperm. In addition, an integrin-binding Arg-Gly-Asp (RGD) motif was found in the extracellular domain of hGC-G. Pre-incubation of the hGC-G RGD peptide with zona pellucida-free oocytes greatly decreased the binding of human sperm to hamster oocytes, which suggests a role for hGC-G role in sperm-oocyte interaction. CONCLUSION: ShGC-G is a novel surface protein on human sperm and potentially mediates sperm-oocyte interaction through its RGD-containing motif.",
keywords = "Cell-surface protein, Gamete interaction, Human sperm, Integrin, RGD motif",
author = "Yang, {Ruey Bing} and Au, {Heng Kien} and Tzeng, {Chii Ruey} and Tsai, {Ming T.} and Ping Wu and Wu, {Yu Chih} and Ling, {Thai Y.} and Huang, {Yen H.}",
year = "2010",
month = "1",
doi = "10.1093/humrep/dep359",
language = "English",
volume = "25",
pages = "42--51",
journal = "Human Reproduction",
issn = "0268-1161",
publisher = "Oxford University Press",
number = "1",

}

TY - JOUR

T1 - Characterization of a novel cell-surface protein expressed on human sperm

AU - Yang, Ruey Bing

AU - Au, Heng Kien

AU - Tzeng, Chii Ruey

AU - Tsai, Ming T.

AU - Wu, Ping

AU - Wu, Yu Chih

AU - Ling, Thai Y.

AU - Huang, Yen H.

PY - 2010/1

Y1 - 2010/1

N2 - BACKGROUND: Precise sperm-oocyte interaction is a critical event for successful fertilization. However, the identity of molecules involved in this process in humans remains largely unknown. This report describes the identification and characterization of a novel cell-surface protein and its potential role in human sperm-oocyte interaction. METHODS: AND RESULTSWe previously identified an orphan guanylyl cyclase receptor (mouse GC-G) highly enriched in mouse testis and involved in sperm activation. By using a comparative genomic approach, we found the homologue gene in human (hGC-G) composed of 21 exons, spanning a minimum of 48 kb on chromosome 10q25. Real-time RT-PCR analysis revealed hGC-G mRNA selectively expressed in testis but with low or no expression in all other tissues examined. Compared with mGC-G, the hGC-G transcript contains three 1-bp deletions and two in-frame termination codons, which results in a short putative receptor-like polypeptide. Western blot analysis with an anti-hGC-G-specific antibody confirmed the protein expression of hGC-G in human sperm lysate. Flow cytometry and confocal immunofluorescence analysis demonstrated the localization of hGC-G protein on the acrosome cap and equatorial segment of mature human sperm. In addition, an integrin-binding Arg-Gly-Asp (RGD) motif was found in the extracellular domain of hGC-G. Pre-incubation of the hGC-G RGD peptide with zona pellucida-free oocytes greatly decreased the binding of human sperm to hamster oocytes, which suggests a role for hGC-G role in sperm-oocyte interaction. CONCLUSION: ShGC-G is a novel surface protein on human sperm and potentially mediates sperm-oocyte interaction through its RGD-containing motif.

AB - BACKGROUND: Precise sperm-oocyte interaction is a critical event for successful fertilization. However, the identity of molecules involved in this process in humans remains largely unknown. This report describes the identification and characterization of a novel cell-surface protein and its potential role in human sperm-oocyte interaction. METHODS: AND RESULTSWe previously identified an orphan guanylyl cyclase receptor (mouse GC-G) highly enriched in mouse testis and involved in sperm activation. By using a comparative genomic approach, we found the homologue gene in human (hGC-G) composed of 21 exons, spanning a minimum of 48 kb on chromosome 10q25. Real-time RT-PCR analysis revealed hGC-G mRNA selectively expressed in testis but with low or no expression in all other tissues examined. Compared with mGC-G, the hGC-G transcript contains three 1-bp deletions and two in-frame termination codons, which results in a short putative receptor-like polypeptide. Western blot analysis with an anti-hGC-G-specific antibody confirmed the protein expression of hGC-G in human sperm lysate. Flow cytometry and confocal immunofluorescence analysis demonstrated the localization of hGC-G protein on the acrosome cap and equatorial segment of mature human sperm. In addition, an integrin-binding Arg-Gly-Asp (RGD) motif was found in the extracellular domain of hGC-G. Pre-incubation of the hGC-G RGD peptide with zona pellucida-free oocytes greatly decreased the binding of human sperm to hamster oocytes, which suggests a role for hGC-G role in sperm-oocyte interaction. CONCLUSION: ShGC-G is a novel surface protein on human sperm and potentially mediates sperm-oocyte interaction through its RGD-containing motif.

KW - Cell-surface protein

KW - Gamete interaction

KW - Human sperm

KW - Integrin

KW - RGD motif

UR - http://www.scopus.com/inward/record.url?scp=72849144943&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=72849144943&partnerID=8YFLogxK

U2 - 10.1093/humrep/dep359

DO - 10.1093/humrep/dep359

M3 - Article

C2 - 19828552

AN - SCOPUS:72849144943

VL - 25

SP - 42

EP - 51

JO - Human Reproduction

JF - Human Reproduction

SN - 0268-1161

IS - 1

ER -