While Dysferlin and Myoferlin Are Coexpressed in the Human Placenta, Only Dysferlin Expression Is Responsive to Trophoblast Fusion in Model Systems1

Robinson, John M.; Ackerman, William E.; Behrendt, Nicholas; Vandré, Dale D.

doi:10.1095/biolreprod.108.074591

Cited by 32 publications

(39 citation statements)

References 32 publications

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“…As we have previously reported [3,22,23], in our preliminary proteomics analysis we identified dysferlin and myoferlin as novel components of the STB apical plasma membrane. Dysferlin has been shown to function as a plasma membrane repair protein in the sarcolemma of skeletal muscle, and participates in forming a “patch” for damaged muscle fibers [33, 34].…”

Section: Discussionsupporting

confidence: 58%

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A placental sub-proteome: The apical plasma membrane of the syncytiotrophoblast

et al. 2012

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As a highly vascularized tissue, the placenta mediates gas and solute exchange between maternal and fetal circulations. In the human placenta, the interface with maternal blood is a unique epithelial structure known as the syncytiotrophoblast. Previously we developed a colloidal-silica based method to generate highly enriched preparations of the apical plasma membrane of the syncytiotrophoblast. Using similar preparations, a proteomics assessment of this important sub-proteome has identified 340 proteins as part of this apical membrane fraction. The expression of 38 of these proteins was previously unknown in the human placental syncytiotrophoblast. Together with previous studies, the current proteomic database expands our knowledge of the proteome of the syncytiotrophoblast apical plasma membrane from normal placentas to include more than 500 proteins. This database is a valuable resource for future comparisons to diseased placentas. Additionally, this dataset provides a basis for further experimental studies of placenta and trophoblast function.

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Section: Discussionsupporting

confidence: 58%

“…Of particular relevance in the STB sub-proteome data set are proteins that are functionally classified as being involved in vesicular trafficking (Table 1). Among these proteins are dysferlin and myoferlin, whose expression was previously unknown in the placenta prior to the initiation of our proteomics analysis of the STB [22,23]. …”

Section: Resultsmentioning

confidence: 99%

A placental sub-proteome: The apical plasma membrane of the syncytiotrophoblast

et al. 2012

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“…While dysferlin and myoferlin are co-expressed in the human placenta, only dysferlin expression is positively correlated to cell fusion in trophoblastic cells (Robinson et al, 2009). In Drosophila melanogaster , only one ferlin gene, called misfire ( mfr ), has been found.…”

Section: Introductionmentioning

confidence: 99%

Dysferlin is essential for endocytosis in the sea star oocyte

Oulhen

Onorato

Ramos

et al. 2014

Developmental Biology

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Dysferlin is a calcium-binding transmembrane protein involved in membrane fusion and membrane repair. In humans, mutations in the dysferlin gene are associated with muscular dystrophy. In this study, we isolated plasma membrane-enriched fractions from full-grown immature oocytes of the sea star, and identified dysferlin by mass spectrometry analysis. The full-length dysferlin sequence is highly conserved between human and the sea star. We learned that in the sea star Patiria miniata, dysferlin RNA and protein are expressed from oogenesis to gastrulation. Interestingly, the protein is highly enriched in the plasma membrane of oocytes. Injection of a morpholino against dysferlin leads to a decrease of endocytosis in oocytes, and to a developmental arrest during gastrulation. These results suggest that dysferlin is critical for normal endocytosis during oogenesis and for embryogenesis in the sea star and that this animal may be a useful model for studying the relationship of dysferlin structure as it relates to its function.

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“…All chemiluminescent signals were collected within the linear response range of the CCD camera and analyzed using Quantity One software (Bio-Rad). The potential for cross-reactivity between the anti-DYSF and anti-MYOF antibodies was assessed in immunoblot assays [23, and unpublished observations], and was found to be negligible.…”

Section: Methodsmentioning

confidence: 99%

“…In mice and humans, mutations in DYSF result in certain muscular dystrophies and cardiomyopathy [11;16–19], while OTOF deficiency produces sensorineural deafness [20;21]. Given that DYSF and MYOF are co-expressed in placental trophoblast [22;23], it has been speculated that these proteins might also contribute to STB plasma membrane repair [24]. …”

Section: Introductionmentioning

confidence: 99%

Placental Dysferlin Expression is Reduced in Severe Preeclampsia

et al. 2009

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Dysferlin (DYSF) and myoferlin (MYOF), members of the ferlin family of membrane proteins, are co-expressed in human placental syncytiotrophoblast (STB). Although the role of these ferlin proteins in the placenta has yet to be established, it has been suggested that DYSF and MYOF may contribute to the stability of the apical STB plasma membrane. The release of STB-derived cellular debris increases in the setting of preeclampsia (PE), suggesting relative destabilization of the hemochorial interface. To test whether PE was associated with alterations in placental expression of DYSF and/ or MYOF, a cross-sectional study was performed using specimens of villous placenta collected form women with severe PE (n = 10) and normotensive controls (n = 10). DYSF and MYOF expression were examined using quantitative real-time RT-PCR, immunoblotting, and immunofluorescence labeling of tissue specimens. Placental DYSF expression was 57% lower at the mRNA level (p = 0.03) and 38% lower at the protein level (p = 0.026) in severe PE as compared to normotensive subjects. There were no differences in placental MYOF protein or mRNA expression between these groups. No appreciable changes in the distribution of DYSF or MYOF within placental villli were observed in PE relative to control specimens. We conclude that DYSF expression is reduced in severe PE relative to gestational age-matched controls. As DYSF has a role in membrane repair, these data suggest a role for DYSF in the stability of the apical STB plasma membrane and may account, at least in part, for the increased shedding of microparticles from this membrane in PE.

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While Dysferlin and Myoferlin Are Coexpressed in the Human Placenta, Only Dysferlin Expression Is Responsive to Trophoblast Fusion in Model Systems1

Cited by 32 publications

References 32 publications

A placental sub-proteome: The apical plasma membrane of the syncytiotrophoblast

A placental sub-proteome: The apical plasma membrane of the syncytiotrophoblast

Dysferlin is essential for endocytosis in the sea star oocyte

Placental Dysferlin Expression is Reduced in Severe Preeclampsia

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