The role of matrix metalloproteinase-2 in the culture media in embryo implantation rate in normogonadotrophic cases undergoing ICSI

Orief, Yasser; Alabd, Mohamed Mourad; Alkasar, Yasser Saad; Koritam, Amr Gamil; Deghedy, Akram

doi:10.1016/j.mefs.2012.11.001

Cited by 1 publication

(1 citation statement)

References 32 publications

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“…Furthermore, MMP 2 and MMP 9 have been shown to be expressed in multiple genital organs including the testicular, epididymal fluids and seminal plasma amongst mammals such as ram, boar, stallion, buffaloes and canine [13][14][15][16]. With regards to reproduction, MMP2 and MMP9 have been associated with ovulation [17] and implantation of the embryo [18]. These two proteins exhibit three gelatin binding fn2 domains at the catalytic site as compared two fn2 domain in BSP proteins and their homologs [19].…”

Section: Mmp 2 and Mmpmentioning

confidence: 99%

Gelatin Binding Proteins in Reproductive Physiology

Kumar¹,

Tinson²,

Mulligan³

et al. 2016

Indian J Microbiol

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In order to advance the assisted reproductive technologies used in animals and human beings, it is important to accumulate basic informations about underlying molecular mechanisms that shape the biological processes of reproduction. From within seminal plasma, proteins perform a wide variety of distinct functions that regulate major reproductive events such as fertilization. The ability of such proteins to bind and interact with different antagonistic ions and biomolecules such as polysaccharides, lipids, and other proteins present in the male and female reproductive tract define these capabilities. Over the last two decades, extensive work has been undertaken in an attempt to define the role of seminal plasma proteins, of which, Gelatin binding proteins (GBPs) represent a large family. GBPs comprise of known group of Bovine seminal plasma (BSP) protein family, matrix metallo proteinases (MMP 2 and MMP 9) and fibronectin, which have been widely studied. The presence of a type II repeat is a characteristic feature of GBPs, which is similar in structure to the fibronectin type II domain (fn2), which has ability to bind multiple ligands including gelatin, glycosaminoglycans, choline phospholipids, and lipoproteins. Two fn2 domains are present within the BSP protein family, while, three fn2 domains are found in gelatinases (MMP-2 and MMP9), and ELSPBP1 (Epididymosomes Transfer Epididymal Sperm Binding Protein 1) contains four long fn2 domains. For the most part BSP proteins are exclusively expressed in seminal vesicles although mBSPH1, mBSPH2 and hBSPH1 are all expressed in the epididymis. The expression of gelatinases has been demonstrated in several organs and tissues such as the prostate, testis, epididymis, ovary, human placenta, cervix and endometrial wall. This review intends to bring current updates on the role of GBPs in reproductive physiology to light, which may act as basis for future studies on GBPs.

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