Matrix metalloproteinases and tissue inhibitors of metalloproteinases in ovarian function

McIntush, Eric W.; Smith, Michael F.

doi:10.1530/ror.0.0030023

Cited by 61 publications

(22 citation statements)

References 14 publications

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“…These results strongly suggested that Ca 2+ is necessary for the activity of gelatinolytic enzymes. On the other hand, most MMPs are testified as zinc-dependent endopeptidases (Mcintush and Smith 1998;Kubota et al 2003). However, in our present study, the enzymes in the presence of Zn 2+ only revealed very weak activity (Fig.…”

Section: Discussioncontrasting

confidence: 60%

“…The matrix metalloproteinases (MMPs) are a family of zinc-and calciumdependent endopeptidases that play central roles in degrading proteins of extracellular matrix (ECM) (McIntush and Smith 1998;Kubota et al 2003). Until now, more than 28 members of MMPs have been reported in vertebrates and they can be classified into four families: interstitial collagenase, stromelysin, membrane-type MMPs and gelatinase (Somerville et al 2003;Van Lint and Libert 2006).…”

Section: Introductionmentioning

confidence: 99%

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IDENTIFICATION AND CHARACTERIZATION OF MATRIX METALLOPROTEINASES FROM THE SARCOPLASMIC FRACTION OF COMMON CARP (CYPRINUS CARPIO) DARK MUSCLE

Cao

et al. 2009

Journal of Food Biochemistry

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Two gelatin hydrolyzing proteinases in the sarcoplasmic fraction of common carp muscle were detected using gelatin zymography. A comparative study shows that the gelatin hydrolyzing activity in dark muscle is obviously higher than that in white muscle. The enzymes can transform to their active forms after treated by aminophenylmercuric acetate, an activator of matrix metalloproteinases. Optimum pH and temperature of these enzymes were around 8.0 and 40C using gelatin as substrate. Metalloproteinase inhibitors (ethylenediaminetetraacetic acid and ethylene glycol‐bis (2‐aminoethylother)‐N, N, N′, N′‐tetraacetic acid) completely suppressed the activities and 1,10‐phenanthroline also showed great inhibitory effects. However, other proteinase inhibitors, such as soybean trypsin inhibitor, benzamidine, E‐64 and pepstatin A, did not show any effect. Metal ions Ca2 + and Zn2 + are essential for these gelatinolytic activities. All these facts indicate that these proteinases are matrix metalloproteinases. Furthermore, these enzymes hydrolyze collagen effectively and maybe thus proposed to be responsible for the tenderization of fish muscle during the postmortem stage.

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Section: Discussioncontrasting

confidence: 60%

Section: Introductionmentioning

confidence: 99%

IDENTIFICATION AND CHARACTERIZATION OF MATRIX METALLOPROTEINASES FROM THE SARCOPLASMIC FRACTION OF COMMON CARP (CYPRINUS CARPIO) DARK MUSCLE

Cao

et al. 2009

Journal of Food Biochemistry

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“…The expression of Timps has been detected in unfertilized oocytes, zygotes, cleavage stage embryos and blastocysts as well as in granulosa and theca cells [33]. The functional interactions between TIMPs and MMPs have been thoroughly investigated during folliculogenesis, whereas much less is known about the post-secretory mechanisms regulating the activity of TIMPs [34]. As a TIMP2 binding partner involved in the ubiquitin proteosome system, Fbxoo may regulate the post-secretory activity of Timp2 to modulate oocyte development in rainbow trout.…”

Section: Discussionmentioning

confidence: 99%

Cloning and characterization of a novel oocyte-specific gene encoding an F-Box protein in rainbow trout (Oncorhynchus mykiss)

Wang

Tripurani

Wanna

et al. 2013

Reprod Biol Endocrinol

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BackgroundOocyte-specific genes play critical roles in oogenesis, folliculogenesis and early embryonic development. The objectives of this study were to characterize the expression of a novel oocyte-specific gene encoding an F-box protein during ovarian development in rainbow trout, and identify its potential interacting partners in rainbow trout oocytes.MethodsThrough analysis of expressed sequence tags (ESTs) from a rainbow trout oocyte cDNA library, a novel transcript represented by ESTs only from the oocyte library was identified. The complete cDNA sequence for the novel gene (named fbxoo) was obtained by assembling sequences from an EST clone and a 5′RACE product. The expression and localization of fbxoo mRNA and protein in ovaries of different developmental stages were analyzed by quantitative real time PCR, immunoblotting, in situ hybridization and immunohistochemistry. Identification of Fbxoo binding proteins was performed by yeast two-hybrid screening.Resultsfbxoo mRNA is specifically expressed in mature oocytes as revealed by tissue distribution analysis. The fbxoo cDNA sequence is 1,996 bp in length containing an open reading frame, which encodes a predicted protein of 514 amino acids. The novel protein sequence does not match any known protein sequences in the NCBI database. However, a search of the Pfam protein database revealed that the protein contains an F-box motif at the N-terminus, indicating that Fbxoo is a new member of the F-box protein family. The expression of fbxoo mRNA and protein is high in ovaries at early pre-vitellogenesis stage, and both fbxoo mRNA and protein are predominantly expressed in early pre-vitellogenic oocytes. Several proteins including tissue inhibitor of metalloproteinase 2 (Timp2) were identified as potential Fbxoo protein binding partners.ConclusionsResults suggest that the novel oocyte-specific F-box protein may play an important role in early oocyte development by regulating other critical proteins involved in oogenesis in rainbow trout.

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“…Выяснено, что TIMP-1 регулируется уровнем ФСГ и трийодтиронина, и через этот фермент может осуществляться связь между щитовидной железой и яичником. Возможно, TIMP-1 играет роль в функционировании и регрессе желтого тела [27]. Показано, что повышенная экспрессия TIMP-1 наблюдается в очагах эндометриоза, и этот фактор может влиять на нарушения овуляции при этом заболевании [28].…”

Section: гены экспрессия которых происходит в клетках теки и стромыunclassified

Molecular mechanisms of folliculogenesis. From ovulation to the corpus luteum formation

Boyarsky¹,

Kachiani²

2018

Probl. reprod.

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Рассмотрены молекулярные процессы, происходящие в ооците и клетках гранулезы человеческого фолликула во время овуляции. Описаны закономерности возобновления мейоза в ооците, расширение и выход комплекса ооцит-кумулюс из фолликула, лютеинизация клеток гранулезы. Уточнен механизм овуляции на уровне группы нейронов кисспептин-нейрокинин-В-динорфин, находящихся в дугообразном ядре гипоталамуса.

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Matrix metalloproteinases and tissue inhibitors of metalloproteinases in ovarian function

Cited by 61 publications

References 14 publications

IDENTIFICATION AND CHARACTERIZATION OF MATRIX METALLOPROTEINASES FROM THE SARCOPLASMIC FRACTION OF COMMON CARP (CYPRINUS CARPIO) DARK MUSCLE

IDENTIFICATION AND CHARACTERIZATION OF MATRIX METALLOPROTEINASES FROM THE SARCOPLASMIC FRACTION OF COMMON CARP (CYPRINUS CARPIO) DARK MUSCLE

Cloning and characterization of a novel oocyte-specific gene encoding an F-Box protein in rainbow trout (Oncorhynchus mykiss)

Molecular mechanisms of folliculogenesis. From ovulation to the corpus luteum formation

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