2001 Fiscal Year Final Research Report Summary
Involvement of UDP-GlcNAc biosynthesis in sexual dysfunctions caused by endocrine disrupting chemicals
| Project/Area Number |
11670348
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Hygiene
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| Research Institution | Yokohama City University |
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Principal Investigator |
OKABE Toshiko Yokohama City University, School of Medicine, Lecturer, 医学部, 講師 (20152564)
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| Co-Investigator(Kenkyū-buntansha) |
MATSUI Mitsuaki Yokohama City University, School of Medicine, Research Assciate, 医学部, 助手 (00285115)
KASHIMA Yuji Yokohama City University, School of Medicine, Research Associate, 医学部, 助手 (50233705)
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| Project Period (FY) |
1999 – 2001
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| Keywords | male infertility / UDP-Ν-acetylglucosamine / UAP1 / AgX1 / anti-sperm antibody / GlcNAc kinase / GlcNAc-phosphate deacetyiase / NAG cluster |
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| Research Abstract |
In human and animals, male sexual dysfunctions had been reported recently. It is suggested that the reason for this phenomenon was thought to be the effects of endocrine disrupting chemicals on sex hormone receptors. Human N-acetylglucosamine-1-phosphate uridyltransferase (UAP1) is expressed in testis and sperm tail, especially outer dense fiber and thought to play important function in sexual function. In this study, we found that the antibody against UAP1 was detected more frequently in sperm plasma with impaired sperm motility. Because the primary structure of UAP1 showed the partial homology with several sperm surface proteins, the antibody against UAP1 might prevent the function of UAP1 as well as other sperm surface proteins, and cause the inhibition of various sperm function.
Furthermore, GNA1 and AGM1, which encode glucosamine-6-phosphate acetyltransferase and phosphoacetylglucosamine mutase, respectively, and are involved in eukaryotic UDP-GlcNAc biosynthesis as well as UAP1 had been cloned and characterized. Furthermore the enzymes for catabolism of N-acetylglucosamine (GlcNAc) such as GlcNAc kinase and GlcNAc-phosphate deacetylase were identified and characterized.
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