Identification and characterization of superoxide dismutase in silkworm seminal fluid

Sumiharu Nagaoka, Kohji Yamamoto

Research output: Contribution to journalArticle

Abstract

Long-term exposure of human sperm cells to reactive oxygen species (ROS) can cause decreased motility and viability, as well as DNA fragmentation. An antioxidant defense system, called a preventive antioxidant system, is therefore needed to maintain low ROS concentrations in sperm and seminal plasma. Superoxide dismutase (SOD, EC 1.15.1.1), one of the most important antioxidant enzymes, catalyzes the conversion of superoxide radical (O2 -) to hydrogen peroxide (H2O2) and molecular oxygen (O2). In this report, we documented a high SOD activity level in the reproductive organs of the male silkmoth (Bombyx mori, L.), particularly in the glandula lacteola, and found that about 90% of the SOD activity was transferred to females by ejaculation and maintained. We characterized three cDNAs from the adult male reproductive system: a soluble cytoplasmic copper/ zinc SOD (Cu/Zn SOD, SOD1) and two extracellular forms of copper/zinc SOD (EC-SOD, SOD3). The levels of transcription and protein accumulation of Bombyx SOD1 indicated that it is abundantly present in the extracellular fluid of the male glandula lacteola, which transfers to the female during ejaculation. Furthermore, it was observed that some of the transferred SOD1 exists in the sperm fraction stored in the mating female’s bursa copulatrix. Our present results demonstrate the origins of seminal SOD activities and suggest that SOD might be a potential source and function of antioxidants in semen and also may control the amount of extracellular ROS involved in sperm quality maintenance.

Original languageEnglish
Pages (from-to)39-47
Number of pages9
JournalJournal of Insect Biotechnology and Sericology
Volume88
Issue number2
DOIs
Publication statusPublished - Jan 1 2019

Fingerprint

Bombyx
silkworms
Antioxidants
Superoxide Dismutase
Spermatozoa
superoxide dismutase
Reactive Oxygen Species
Ejaculation
Fluids
Semen
Oxygen
Zinc
Copper
Molecular oxygen
Extracellular Fluid
DNA Fragmentation
Transcription
Hydrogen peroxide
Superoxides
reactive oxygen species

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Applied Microbiology and Biotechnology
  • Business, Management and Accounting(all)
  • Agricultural and Biological Sciences(all)
  • Insect Science
  • Industrial and Manufacturing Engineering

Cite this

Identification and characterization of superoxide dismutase in silkworm seminal fluid. / Nagaoka, Sumiharu; Yamamoto, Kohji.

In: Journal of Insect Biotechnology and Sericology, Vol. 88, No. 2, 01.01.2019, p. 39-47.

Research output: Contribution to journalArticle

@article{34ffe496afa64a83bafd38a08ddc4565,
title = "Identification and characterization of superoxide dismutase in silkworm seminal fluid",
abstract = "Long-term exposure of human sperm cells to reactive oxygen species (ROS) can cause decreased motility and viability, as well as DNA fragmentation. An antioxidant defense system, called a preventive antioxidant system, is therefore needed to maintain low ROS concentrations in sperm and seminal plasma. Superoxide dismutase (SOD, EC 1.15.1.1), one of the most important antioxidant enzymes, catalyzes the conversion of superoxide radical (O2 -) to hydrogen peroxide (H2O2) and molecular oxygen (O2). In this report, we documented a high SOD activity level in the reproductive organs of the male silkmoth (Bombyx mori, L.), particularly in the glandula lacteola, and found that about 90{\%} of the SOD activity was transferred to females by ejaculation and maintained. We characterized three cDNAs from the adult male reproductive system: a soluble cytoplasmic copper/ zinc SOD (Cu/Zn SOD, SOD1) and two extracellular forms of copper/zinc SOD (EC-SOD, SOD3). The levels of transcription and protein accumulation of Bombyx SOD1 indicated that it is abundantly present in the extracellular fluid of the male glandula lacteola, which transfers to the female during ejaculation. Furthermore, it was observed that some of the transferred SOD1 exists in the sperm fraction stored in the mating female’s bursa copulatrix. Our present results demonstrate the origins of seminal SOD activities and suggest that SOD might be a potential source and function of antioxidants in semen and also may control the amount of extracellular ROS involved in sperm quality maintenance.",
author = "Sumiharu Nagaoka and Kohji Yamamoto",
year = "2019",
month = "1",
day = "1",
doi = "10.11416/jibs.88.2_039",
language = "English",
volume = "88",
pages = "39--47",
journal = "Journal of Insect Biotechnology and Sericology",
issn = "1346-8073",
publisher = "Japanese Society of Sericultural Sciences",
number = "2",

}

TY - JOUR

T1 - Identification and characterization of superoxide dismutase in silkworm seminal fluid

AU - Nagaoka, Sumiharu

AU - Yamamoto, Kohji

PY - 2019/1/1

Y1 - 2019/1/1

N2 - Long-term exposure of human sperm cells to reactive oxygen species (ROS) can cause decreased motility and viability, as well as DNA fragmentation. An antioxidant defense system, called a preventive antioxidant system, is therefore needed to maintain low ROS concentrations in sperm and seminal plasma. Superoxide dismutase (SOD, EC 1.15.1.1), one of the most important antioxidant enzymes, catalyzes the conversion of superoxide radical (O2 -) to hydrogen peroxide (H2O2) and molecular oxygen (O2). In this report, we documented a high SOD activity level in the reproductive organs of the male silkmoth (Bombyx mori, L.), particularly in the glandula lacteola, and found that about 90% of the SOD activity was transferred to females by ejaculation and maintained. We characterized three cDNAs from the adult male reproductive system: a soluble cytoplasmic copper/ zinc SOD (Cu/Zn SOD, SOD1) and two extracellular forms of copper/zinc SOD (EC-SOD, SOD3). The levels of transcription and protein accumulation of Bombyx SOD1 indicated that it is abundantly present in the extracellular fluid of the male glandula lacteola, which transfers to the female during ejaculation. Furthermore, it was observed that some of the transferred SOD1 exists in the sperm fraction stored in the mating female’s bursa copulatrix. Our present results demonstrate the origins of seminal SOD activities and suggest that SOD might be a potential source and function of antioxidants in semen and also may control the amount of extracellular ROS involved in sperm quality maintenance.

AB - Long-term exposure of human sperm cells to reactive oxygen species (ROS) can cause decreased motility and viability, as well as DNA fragmentation. An antioxidant defense system, called a preventive antioxidant system, is therefore needed to maintain low ROS concentrations in sperm and seminal plasma. Superoxide dismutase (SOD, EC 1.15.1.1), one of the most important antioxidant enzymes, catalyzes the conversion of superoxide radical (O2 -) to hydrogen peroxide (H2O2) and molecular oxygen (O2). In this report, we documented a high SOD activity level in the reproductive organs of the male silkmoth (Bombyx mori, L.), particularly in the glandula lacteola, and found that about 90% of the SOD activity was transferred to females by ejaculation and maintained. We characterized three cDNAs from the adult male reproductive system: a soluble cytoplasmic copper/ zinc SOD (Cu/Zn SOD, SOD1) and two extracellular forms of copper/zinc SOD (EC-SOD, SOD3). The levels of transcription and protein accumulation of Bombyx SOD1 indicated that it is abundantly present in the extracellular fluid of the male glandula lacteola, which transfers to the female during ejaculation. Furthermore, it was observed that some of the transferred SOD1 exists in the sperm fraction stored in the mating female’s bursa copulatrix. Our present results demonstrate the origins of seminal SOD activities and suggest that SOD might be a potential source and function of antioxidants in semen and also may control the amount of extracellular ROS involved in sperm quality maintenance.

UR - http://www.scopus.com/inward/record.url?scp=85073286409&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85073286409&partnerID=8YFLogxK

U2 - 10.11416/jibs.88.2_039

DO - 10.11416/jibs.88.2_039

M3 - Article

AN - SCOPUS:85073286409

VL - 88

SP - 39

EP - 47

JO - Journal of Insect Biotechnology and Sericology

JF - Journal of Insect Biotechnology and Sericology

SN - 1346-8073

IS - 2

ER -