Altered perlecan expression in placental development and gestational diabetes mellitus

Yang, Wei; Su, Ta‐Wei; Yang, Yuh Cheng; Chang, Suying; Chen, C.-Y.; Chen, C.-P.

doi:10.1016/j.placenta.2004.11.002

Cited by 29 publications

(22 citation statements)

References 28 publications

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“…Perlecan expression has been examined in developing human placentae (Rohde et al 1998;Yang et al 2005). As expected, it is found in all basal laminae of these structures; however, perlecan also accumulates in Nitabuch's membrane (Rohde et al 1998), an area of attachment at the maternalfetal interface placental villi and the decidua (Figure 1).…”

Section: Perlecan Expression In Embryo Implantation and Placentationmentioning

confidence: 65%

Perlecan a multifunctional extracellular proteoglycan scaffold

2007

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Perlecan is a large multidomain heparan sulfate proteoglycan of the extracellular matrix. Expression of this proteoglycan changes dynamically during embryo implantation and placentation. Perlecan is expressed by various cells of the embryo including trophectoderm and trophoblast as well as the maternal compartment, including basal lamina underlying uterine epithelia and endothelia and, most dynamically, in developing decidua. Perlecan supports various biological functions, including cell adhesion, growth factor binding, and modulation of apoptosis. Moreover, studies in other systems demonstrate that perlecan expression and activity can be controlled at many levels, including transcription, alternative splicing, and extracellular proteolysis. This review will discuss changes in perlecan expression that occur during embryo implantation and placentation. Furthermore, we propose a model in which perlecan represents an extracellular scaffold protein that supports complex, distinct functions in its full-length form or smaller forms generated by alternative mRNA splicing, extracellular proteolysis, or glycosidase action.

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Section: Perlecan Expression In Embryo Implantation and Placentationmentioning

confidence: 65%

Perlecan a multifunctional extracellular proteoglycan scaffold

2007

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“…If adequate supply is not available because of reduced oxygen delivery to the intervillous space as a result of the higher oxygen affinity of glycated hemoglobin (29), thickening of the placental basement membrane (30,31), and reduced utero-placental or fetoplacental blood flow (32,33), fetal hypoxemia will ensue (34). Hypoxia is a potent stimulator of hypoxia-sensitive transcription factors such as the hypoxia inducible factor (HIF) and will therefore lead to the stimulated expression and synthesis of a variety of molecules, some of which are key players, especially in angiogenesis (35,36).…”

Section: The Insulin Receptormentioning

confidence: 99%

The Human Placenta in Gestational Diabetes Mellitus

2007

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“…In contrast to the findings that hyperglycemia suppressed perlecan and HS synthesis in aortic and glomerular endothelial cells, high glucose concentration and osmotic pressure were found to enhance in vitro perlecan expression in cytotrophoblasts (59). The mechanism and significance for increased placental perlecan expression in gestational diabetes mellitus remain to be elucidated.…”

Section: Upregulation Of Perlecan In Villi Of Gestational Diabetes Mementioning

confidence: 69%

“…Placental villi in gestational diabetes mellitus express a higher level of perlecan and CS/DS than those in normal pregnancy (59). In contrast to the findings that hyperglycemia suppressed perlecan and HS synthesis in aortic and glomerular endothelial cells, high glucose concentration and osmotic pressure were found to enhance in vitro perlecan expression in cytotrophoblasts (59).…”

Section: Upregulation Of Perlecan In Villi Of Gestational Diabetes Mementioning

confidence: 69%

Diverse functions of uterine proteoglycans in human reproduction (Review)

Kitaya¹,

Tada²,

Hayashi³

et al. 2012

Mol Med Report

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Abstract. Proteoglycans (PGs) are a group of heavily glycosylated proteins that are present throughout the mammalian body and are involved in a wide variety of biological phenomena, including structural maintenance, tissue remodeling, molecular presentation, cell adhesion and signal transmission. Previous studies have revealed an increasing number of roles for PGs in human reproduction. Several PGs are currently utilized or regarded as biomarkers for the diagnosis of certain pathological uterine conditions associated with infertility and obstetrical complications. The aim of this review was to discuss the involvement of PGs in the human uterus in reproductive biology and pathophysiology. Contents1. Introduction 2. PGs in human endometrium 3. Close association between miscarriage and deficiency in thrombomodulin and syndecan-4 4. Syndecan-1 as a diagnostic biomarker for plasmacyte infiltrates in chronic endometritis 5. DSPGs mediate ectopic growth and development of endometriosis 6. PGs in human myometrium and cervix 7. Contribution of fibromodulin, versican and decorin to structural maintenance and growth of uterine fibroids 8. Low myometrial syndecan-3 expression in dystocia 9. PGs in human placenta 10. Amniotic fluid perlecan and agrin as potential biomarkers for premature rupture of fetal membranes 11. Preventive role of syndecan-1 against pre-eclampsia 12. Upregulation of perlecan in the villi of gestational diabetes mellitus 13. Elevated amniotic fluid lumican concentration in fetus with Turner syndrome 14. Conclusions IntroductionProteoglycans (PGs) are a group of macromolecules which consist of one core protein and one or more covalently attached sulfated glycosaminoglycan (GAG) side chain(s). The PG core proteins are encoded by distinct genes and contain multiple functional domains that bind to and modulate a wide range of molecules, including chemokines, cytokines, growth factors, extracellular matrix (ECM) proteins, coagulation factors and lipid-metabolizing enzymes. The localization of PGs is attributed to the molecular and structural characteristics of their core proteins. GAGs consist of diversely epimerized/sulfated unbranched polysaccharide chains composed of 1,4-linked repeated disaccharide units. According to the combination of disaccharides, the sulfated GAG side chains are classified as chondroitin sulfate (CS), dermatan sulfate (DS), heparan sulfate (HS) and keratan sulfate (KS). The sulfation status of the GAG side chains in PGs varies with tissue type, location and age, which provides PGs with organ-dependent properties in molecular weight, structure and function (1).PGs are classified into two distinct types by their location in tissues: i) cell surface PGs and ii) ECM PGs (Table I). The cell surface PGs include the syndecan and glypican families. Syndecans are a group of transmembrane HSPGs that interact with and regulate various soluble molecules. Glypicans are glycosylphosphatidylinositol-anchored HSPGs on the outer surface of the plasma membrane that regulate multiple intracellular sig...

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Altered perlecan expression in placental development and gestational diabetes mellitus

Cited by 29 publications

References 28 publications

Perlecan a multifunctional extracellular proteoglycan scaffold

Perlecan a multifunctional extracellular proteoglycan scaffold

The Human Placenta in Gestational Diabetes Mellitus

Diverse functions of uterine proteoglycans in human reproduction (Review)

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