The identification of novel ovarian proteases through the use of genomic and bioinformatic methodologies

Kei Miyakoshi, Melinda J. Murphy, Richard R. Yeoman, Siddhartha Mitra, Christopher J. Dubay, Jon D. Hennebold

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

Proteolytic activities are essential for follicular growth, ovulation, as well as for luteal formation and regression. Using suppression subtractive hybridization (SSH), a novel mouse ovary-selective gene (termed protease serine 35, Prss35) was identified. Analysis of the mouse genome database using the Prss35 sequence led to the identification of a homologous protease (protease serine 23, Prss23). PRSS35 possesses general features that are characteristic of serine (Ser) proteases, but is unique in that the canonical Ser that defines this enzyme family is replaced by a threonine (Thr). In contrast, PRSS23 possesses the standard catalytic Ser typical for this family of proteases. As determined by real-time polymerase chain reaction (PCR), the Prss35 mRNA levels increased around the time of ovulation and remained elevated in the developing corpus luteum. Steroid ablation/replacement studies demonstrated progesterone-dependent regulation of Prss35 gene expression prior to follicle rupture. Prss35 gene expression was localized to the theca cells of pre-antral follicles, the theca and granulosa cells of pre-ovulatory and ovulatory follicles, as well as to the developing corpus luteum. In contrast, Prss23 mRNA levels decreased transiently after ovulation induction and again in the postovulatory period. Prss23 gene expression was noted primarily in the granulosa cells of the secondary/early antral follicles. PRSS35 and PRSS23 orthologs in the rat, human, rhesus macaque, chimpanzee, cattle, dog, and chicken were identified and found to be highly homologous to one another (75-99% homology). Collectively, these results suggest that the PRSS35 and PRSS23 genes have been conserved as critical ovarian proteases throughout the course of vertebrate evolution.

Original languageEnglish
Pages (from-to)823-835
Number of pages13
JournalBiology of Reproduction
Volume75
Issue number6
DOIs
Publication statusPublished - 2006 Dec
Externally publishedYes

Fingerprint

Serine Proteases
Computational Biology
Peptide Hydrolases
Theca Cells
Granulosa Cells
Corpus Luteum
Ovulation
Gene Expression
Serine
Luteolysis
Messenger RNA
Pan troglodytes
Ovulation Induction
Threonine
Macaca mulatta
Genes
Progesterone
Vertebrates
Real-Time Polymerase Chain Reaction
Rupture

Keywords

  • Corpus luteum
  • Follicle
  • Granulosa cell
  • Ovary
  • Theca cell

ASJC Scopus subject areas

  • Cell Biology
  • Developmental Biology
  • Embryology

Cite this

The identification of novel ovarian proteases through the use of genomic and bioinformatic methodologies. / Miyakoshi, Kei; Murphy, Melinda J.; Yeoman, Richard R.; Mitra, Siddhartha; Dubay, Christopher J.; Hennebold, Jon D.

In: Biology of Reproduction, Vol. 75, No. 6, 12.2006, p. 823-835.

Research output: Contribution to journalArticle

Miyakoshi, Kei ; Murphy, Melinda J. ; Yeoman, Richard R. ; Mitra, Siddhartha ; Dubay, Christopher J. ; Hennebold, Jon D. / The identification of novel ovarian proteases through the use of genomic and bioinformatic methodologies. In: Biology of Reproduction. 2006 ; Vol. 75, No. 6. pp. 823-835.
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abstract = "Proteolytic activities are essential for follicular growth, ovulation, as well as for luteal formation and regression. Using suppression subtractive hybridization (SSH), a novel mouse ovary-selective gene (termed protease serine 35, Prss35) was identified. Analysis of the mouse genome database using the Prss35 sequence led to the identification of a homologous protease (protease serine 23, Prss23). PRSS35 possesses general features that are characteristic of serine (Ser) proteases, but is unique in that the canonical Ser that defines this enzyme family is replaced by a threonine (Thr). In contrast, PRSS23 possesses the standard catalytic Ser typical for this family of proteases. As determined by real-time polymerase chain reaction (PCR), the Prss35 mRNA levels increased around the time of ovulation and remained elevated in the developing corpus luteum. Steroid ablation/replacement studies demonstrated progesterone-dependent regulation of Prss35 gene expression prior to follicle rupture. Prss35 gene expression was localized to the theca cells of pre-antral follicles, the theca and granulosa cells of pre-ovulatory and ovulatory follicles, as well as to the developing corpus luteum. In contrast, Prss23 mRNA levels decreased transiently after ovulation induction and again in the postovulatory period. Prss23 gene expression was noted primarily in the granulosa cells of the secondary/early antral follicles. PRSS35 and PRSS23 orthologs in the rat, human, rhesus macaque, chimpanzee, cattle, dog, and chicken were identified and found to be highly homologous to one another (75-99{\%} homology). Collectively, these results suggest that the PRSS35 and PRSS23 genes have been conserved as critical ovarian proteases throughout the course of vertebrate evolution.",
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