Production of gelatinases and tissue inhibitors of matrix metalloproteinases by equine ovarian stromal cells In vitro.
Abstract: Matrix metalloproteinases (MMPs) and tissue inhibitors of MMPs (TIMPs) play very important roles in extracellular matrix (ECM) remodeling in ovarian follicle growth and ovulation. Equine follicles are embedded in cortex that is at the center of the ovary, and they must expand/emigrate to the fossa, the only site in the ovary for ovulation. Therefore, equine ovarian stromal cells (EOSC) are probably involved in ECM remodeling during follicle growth. This study examined whether cultured EOSC synthesize gelatinases and TIMPs, molecules essential for ECM remodeling in other systems. Results showed that cultured EOSC (passage 3-8) had a fibroblast-like morphology and were positive for alpha-smooth muscle actin and type I procollagen by immunostaining. Gelatinase A (MMP-2), gelatinase B (MMP-9), TIMP-1, and TIMP-2 were present in EOSC-conditioned medium, and TIMP-3 in ECM of EOSC. Transforming growth factor beta significantly stimulated the activity of gelatinases A and B and TIMP-1 in conditioned medium from EOSC (p < 0.05). Phorbol 12-myristate 13-acetate also significantly stimulated the activity of gelatinases A and B and TIMP-1 in conditioned medium and of TIMP-3 in ECM (p < 0.05). Our results suggest that EOSC produce important components of the ECM remodeling machinery and, therefore, may play a role in the ECM remodeling during follicle growth in this species.
Publication Date: 1998-12-22 PubMed ID: 9858479DOI: 10.1095/biolreprod60.1.1Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research studied the production of extracellular matrix (ECM) remodeling components like gelatinases and tissue inhibitors of matrix metalloproteinases (TIMPs) by equine ovarian stromal cells (EOSC). The study found that EOSCs produce these elements, suggesting they play a role in ECM remodeling during follicle growth in horses.
Objectives of the Study
- The study aimed to understand the role of ECM remodeling in ovarian follicle growth and ovulation in equine species.
- The researchers specifically looked at EOSCs and the production of certain components including, gelatinases (MMP-2 and MMP-9) and TIMPs (TIMP-1, TIMP-2, and TIMP-3) by these cells.
Methods and Findings
- The study involved the cultivation of EOSCs to examine the synthesis of gelatinases and TIMPs, known to be critical in ECM remodeling.
- By immunostaining, they found that EOSCs of passage 3-8 exhibited a fibroblast-like morphology and were positive for type I procollagen and alpha-smooth muscle actin.
- Gelatinases A and B, along with TIMPs, were found in EOSC-conditioned medium, while TIMP-3 was present in the ECM of EOSC.
- The researchers observed that transforming growth factor beta significantly stimulated the activity of gelatinases A and B as well as TIMP-1 in the EOSC-conditioned medium.
- Furthermore, the substance Phorbol 12-myristate 13-acetate also noticeably enhanced the activity of gelatinases A and B, TIMP-1 is in the conditioned medium, and TIMP-3 in the ECM.
Conclusions
- The findings of this research suggest that EOSCs are producers of essential components involved in the ECM remodeling process.
- Therefore, these cells may play a significant part in the ECM remodeling during follicle growth in horses.
- The outcomes imply potential avenues for further study and could have implications for understanding and potentially managing reproductive processes in equine species.
Cite This Article
APA
Song L, Porter DG, Coomber BL.
(1998).
Production of gelatinases and tissue inhibitors of matrix metalloproteinases by equine ovarian stromal cells In vitro.
Biol Reprod, 60(1), 1-7.
https://doi.org/10.1095/biolreprod60.1.1 Publication
Researcher Affiliations
- a Department of Biomedical Sciences, Ontario Veterinary College, University of Guelph, Guelph, Ontario, Canada N1G 2W1.
MeSH Terms
- Animals
- Cells, Cultured
- Collagenases / biosynthesis
- Culture Media, Conditioned
- Dose-Response Relationship, Drug
- Extracellular Matrix / metabolism
- Female
- Gelatinases / biosynthesis
- Horses / metabolism
- Matrix Metalloproteinase 2
- Matrix Metalloproteinase 9
- Metalloendopeptidases / biosynthesis
- Ovary / metabolism
- Stromal Cells / metabolism
- Tetradecanoylphorbol Acetate / administration & dosage
- Tetradecanoylphorbol Acetate / pharmacology
- Tissue Inhibitor of Metalloproteinase-1 / biosynthesis
- Tissue Inhibitor of Metalloproteinase-2 / biosynthesis
- Tissue Inhibitor of Metalloproteinases / biosynthesis
- Transforming Growth Factor beta / administration & dosage
- Transforming Growth Factor beta / pharmacology
Citations
This article has been cited 2 times.- Saraswati S, Block AS, Davidson MK, Rank RG, Mahadevan M, Diekman AB. Galectin-3 is a substrate for prostate specific antigen (PSA) in human seminal plasma. Prostate 2011 Feb 1;71(2):197-208.
- Starr AE, Dan T, Minhas K, Shewen PE, Coomber BL. Potential involvement of gelatinases and their inhibitors in Mannheimia haemolytica pneumonia in cattle. Infect Immun 2004 Aug;72(8):4393-400.
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