Semenogelin, a coagulum macromolecule monitoring factor involved in the first step of fertilization: A prospective review

Int J Biol Macromol. 2022 Jun 1;209(Pt A):951-962. doi: 10.1016/j.ijbiomac.2022.04.079. Epub 2022 Apr 18.

Abstract

Human male infertility affects approximately 1/10 couples worldwide, and its prevalence is found more in developed countries. Along with sperm cells, the secretions of the prostate, seminal vesicle and epididymis plays a major role in proper fertilization. Many studies have proven the functions of seminal vesicle secretions, especially semenogelin protein, as an optimiser for fertilization. Semenogelin provides the structural components for coagulum formation after ejaculation. It binds with eppin and is found to have major functions like motility of sperm, transporting the sperm safely in the immune rich female reproductive tract until the sperm cells reach the egg intact. The capacitation process is essential for proper fertilization and semenogelin involved in mediating capacitation in time. Also, it has control of events towards the first step in the fertilization process. It is a Zn ions binding protein, and Zn ions act as a cofactor that helps in the proper motility of sperm cells. Therefore, any imbalance in protein that automatically affect sperm physiology and fertility status. This review sheds a comprehensive and critical view on the significant functions of semenogelin in fertilization. This review can open up advanced proteomics research on semenogelin towards unravelling molecular mechanisms in fertilization.

Keywords: Capacitation; Human male infertility; Hyper viscosity; Semenogelin; Seminal plasma; Sperm cells.

Publication types

  • Review

MeSH terms

  • Female
  • Fertilization
  • Humans
  • Infertility, Male* / metabolism
  • Male
  • Prospective Studies
  • Proteins / metabolism
  • Seminal Vesicle Secretory Proteins* / chemistry
  • Seminal Vesicle Secretory Proteins* / metabolism
  • Spermatozoa / metabolism

Substances

  • Proteins
  • Seminal Vesicle Secretory Proteins