Molecular characterization and expression of DERL1 in bovine ovarian follicles and corpora lutea

Kalidou Ndiaye, Jacques G. Lussier, Joy Lee Pate

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

The endoplasmic reticulum (ER) is a major site of protein synthesis and facilitates the folding and assembly of newly synthesized proteins. Misfolded proteins are retrotranslocated across the ER membrane and destroyed at the proteasome. DERL1 is an important protein involved in the retrotranslocation and degradation of a subset of misfolded proteins from the ER. We characterized a 2617 bp cDNA from bovine granulosa cells that corresponded to bovine DERL1. Two transcripts of 3 and 2.6 kb were detected by Northern blot analysis, and showed variations in expression among tissues. During follicular development, DERL1 expression was greater in day 5 dominant follicles compared to small follicles, ovulatory follicles, or corpus luteum (CL). Within the CL, DERL1 mRNA expression was intermediate in midcycle, and lowest in late cycle as compared to early in the estrous cycle. Western blot analyses demonstrated the presence of DERL1 in the bovine CL at days 5, 11, and 18 of the estrous cycle. Co-immunoprecipitation using luteal tissues showed that DERL1 interacts with class I MHC but not with VIMP or p97 ATPase. The interaction between DERL1 and MHC I suggests that, in the CL, DERL1 may regulate the integrity of MHC I molecules that are transported to the ER membrane. Furthermore, the greater expression of DERL1 mRNA is associated with the active follicular development and early luteal stages, suggesting a role of DERL1 in tissue remodeling events and maintenance of function in reproductive tissues.

Original languageEnglish (US)
Article number94
JournalReproductive Biology and Endocrinology
Volume8
DOIs
StatePublished - Aug 3 2010

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Ovarian Follicle
Corpus Luteum
Endoplasmic Reticulum
Estrous Cycle
Proteins
Messenger RNA
Membranes
Granulosa Cells
Proteasome Endopeptidase Complex
Immunoprecipitation
Northern Blotting
Complementary DNA
Western Blotting
Maintenance

All Science Journal Classification (ASJC) codes

  • Reproductive Medicine
  • Endocrinology
  • Developmental Biology

Cite this

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title = "Molecular characterization and expression of DERL1 in bovine ovarian follicles and corpora lutea",
abstract = "The endoplasmic reticulum (ER) is a major site of protein synthesis and facilitates the folding and assembly of newly synthesized proteins. Misfolded proteins are retrotranslocated across the ER membrane and destroyed at the proteasome. DERL1 is an important protein involved in the retrotranslocation and degradation of a subset of misfolded proteins from the ER. We characterized a 2617 bp cDNA from bovine granulosa cells that corresponded to bovine DERL1. Two transcripts of 3 and 2.6 kb were detected by Northern blot analysis, and showed variations in expression among tissues. During follicular development, DERL1 expression was greater in day 5 dominant follicles compared to small follicles, ovulatory follicles, or corpus luteum (CL). Within the CL, DERL1 mRNA expression was intermediate in midcycle, and lowest in late cycle as compared to early in the estrous cycle. Western blot analyses demonstrated the presence of DERL1 in the bovine CL at days 5, 11, and 18 of the estrous cycle. Co-immunoprecipitation using luteal tissues showed that DERL1 interacts with class I MHC but not with VIMP or p97 ATPase. The interaction between DERL1 and MHC I suggests that, in the CL, DERL1 may regulate the integrity of MHC I molecules that are transported to the ER membrane. Furthermore, the greater expression of DERL1 mRNA is associated with the active follicular development and early luteal stages, suggesting a role of DERL1 in tissue remodeling events and maintenance of function in reproductive tissues.",
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Molecular characterization and expression of DERL1 in bovine ovarian follicles and corpora lutea. / Ndiaye, Kalidou; Lussier, Jacques G.; Pate, Joy Lee.

In: Reproductive Biology and Endocrinology, Vol. 8, 94, 03.08.2010.

Research output: Contribution to journalArticle

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