Anticoagulant Dermatan Sulfate Proteoglycan (Decorin) in the Term Human Placenta

Delorme, Michael A.; Xu, Li; Berry, Leslie R.; Mitchell, Lesley; Andrew, Maureen

doi:10.1016/s0049-3848(98)00035-8

Cited by 48 publications

(25 citation statements)

References 18 publications

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“…Delorme et al reported that thrombin generation is increased during normal pregnancy and that a greater proportion of thrombin molecules form a complex with HCII in plasma in pregnant woman than in nonpregnant women (34). It has also been reported that HCII levels are significantly decreased in women with severe preeclampsia (35).…”

Section: Discussionmentioning

confidence: 99%

Strain-dependent embryonic lethality and exaggerated vascular remodeling in heparin cofactor II–deficient mice

Aihara¹,

Azuma²,

Akiyama³

et al. 2007

J. Clin. Invest.

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atherosclerosis. However, the in vivo effects and the molecular mechanism underlying the action of HCII during vascular remodeling remain elusive. To clarify the role of HCII in vascular remodeling, we generated HCII-deficient mice by gene targeting. In contrast to a previous report, HCII -/-mice were embryonically lethal. In HCII +/-mice, prominent intimal hyperplasia with increased cellular proliferation was observed after tube cuff and wire vascular injury. The number of protease-activated receptor-1-positive (PAR-1-positive) cells was increased in the thickened vascular wall of HCII +/-mice, suggesting enhanced thrombin action in this region. Cuff injury also increased the expression levels of inflammatory cytokines and chemokines in the vascular wall of HCII +/-mice. The intimal hyperplasia in HCII +/-mice with vascular injury was abrogated by human HCII supplementation. Furthermore, HCII deficiency caused acceleration of aortic plaque formation with increased PAR-1 expression and oxidative stress in apoE-KO mice. These results demonstrate that HCII protects against thrombin-induced remodeling of an injured vascular wall by inhibiting thrombin action and suggest that HCII is potentially therapeutic against atherosclerosis without causing coagulatory disturbance.

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Section: Discussionmentioning

confidence: 99%

Strain-dependent embryonic lethality and exaggerated vascular remodeling in heparin cofactor II–deficient mice

Aihara¹,

Azuma²,

Akiyama³

et al. 2007

J. Clin. Invest.

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“…In addition, disruption of the mouse sulfotransferase gene, sult1e1 , leads to placental thrombosis and spontaneous fetal loss (Tong et al, 2005). Sulfate is also required in the placental trophoblast cells for the synthesis of proteoglycans, including heparan sulfate, dermatan sulfate and chondroitin sulfate, which prevent blood coagulation in the intervillous space, protect the fetus from the maternal immune system, and enable the implantation of the fetus in the uterine epithelium (Delorme et al, 1998;Slater and Murphy, 1999;Achur et al, 2000;Genbacev et al, 2003). Taken together, these findings highlight the essential role of sulfate during fetal development, and suggest that NaS2 may play an important role in maintaining placental sulfate levels for fetal development.…”

Section: Discussionmentioning

confidence: 99%

Molecular cloning and characterization of the mouse Na+ sulfate cotransporter gene (Slc13a4): structure and expression

et al. 2006

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Sulfate is an essential ion required for numerous functions in mammalian physiology. Due to its hydrophilic nature, cells require sulfate transporters on their plasma membranes to allow entry of sulfate into cells. In this study, we identified a new mouse Na + -sulfate cotransporter (mNaS2), characterized its tissue distribution and determined its cDNA and gene ( Slc13a4 ) structures. mNaS2 mRNA was expressed in placenta, brain, lung, eye, heart, testis, thymus and liver. The mouse NaS2 cDNA spans 3384 nucleotides and its open frame encodes a protein of 624 amino acids. Slc13a4 maps to mouse chromosome 6B1 and contains 16 exons, spanning over 40 kb in length. Its 5'-flanking region contains CAAT-and GC-box motifs and a number of putative transcription factor binding sites, including GATA-1, MTF-1, STAT6 and HNF4 consensus sequences. This is the first study to define the tissue distribution of mNaS2 and resolve its cDNA and gene structures, which will allow us to investigate mNaS2 gene expression in vivo and determine its role in mammalian physiology.

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“…We identified decorin as one of the major SP-D-binding proteins present in amniotic fluid (Figs. 1 and 9) by its Nterminal sequence (33) and molecular weight on SDS-PAGE (55,56).…”

Section: Interaction Between Different Domains Of Sp-d Andmentioning

confidence: 99%

Identification and Characterization of a Novel Interaction between Pulmonary Surfactant Protein D and Decorin

Nadesalingam

Bernal

Dodds

et al. 2003

Journal of Biological Chemistry

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Surfactant-associated protein D (SP-D) is a collectin Surfactant protein D (SP-D),1 a C-type lectin, is present in pulmonary surfactant and several other mucosal surfaces (1). Recent studies show that SP-D modulates multiple functions: innate immunity (2, 3), allergic response (4), expression of matrix metalloproteases (5, 6), alveolar wall remodeling-emphysema, fibrosis, and lipid and macrophage homeostasis (7-9). Taken together, these results indicate that SP-D regulates pathway(s) that involve matrix-related proteins. However, the SP-D-binding proteins, which may participate in this pathway, are not known.In the lung, pulmonary type II cells express and secrete SP-D into the alveolar environment (1, 10). SP-D expression is developmentally regulated, and its concentration increases in amniotic fluid during the last few weeks of pregnancy (10). In adult lungs, the concentration of SP-D varies significantly during allergic and pathological conditions, and therapeutic lung washings and amniotic fluid are routinely used for the purification of SP-D (11-13). Purified SP-D is a glycoprotein and is composed of a short interchain disulfide bond-forming N-terminal domain, a collagen-like region with Gly-X-Y repeats (where X represents any amino acid and Y is often hydroxyproline or hydroxylysine), a hydrophobic neck region, and a Cterminal globular carbohydrate recognition domain (CRD) (14 -16). Three CRDs are held together by protein-protein interactions at the hydrophobic neck region (17). The collagenlike region folds into a ϳ45-nm-long triple helix, and the chains are tethered at the end via the N-terminal segment. Trimeric SP-D subunits (3 ϫ 43 kDa) further assemble as higher order oligomers via interactions at the collagen-like and N-terminal domains. Dodecameric SP-D are X-shaped ϳ100-nm-long molecules (516 kDa), whereas higher order multimers appear as "fuzzy balls" (16,18). CRDs of SP-D can interact with glycoproteins (19), carbohydrates (20 -22), and lipids (23) present on microbial surfaces, phosphatidylinositol component of pulmonary surfactant lipid (24), and receptors/binding proteins such as CD14 (25) and gp-340 (26). N-terminal (27) and collagen-like (14) regions of SP-D are glycosylated and are implicated in structural organization and receptor binding. The N-terminal domain is important for disulfide-dependent oligomerization (28), and X-like structural assembly (29). Microfibril-associated protein 4, a fibrinogen-like domain-containing protein with lectin activity, binds to the collagen-like region of SP-D (30); however, its biological function is not clearly established.

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Anticoagulant Dermatan Sulfate Proteoglycan (Decorin) in the Term Human Placenta

Cited by 48 publications

References 18 publications

Strain-dependent embryonic lethality and exaggerated vascular remodeling in heparin cofactor II–deficient mice

Strain-dependent embryonic lethality and exaggerated vascular remodeling in heparin cofactor II–deficient mice

Molecular cloning and characterization of the mouse Na+ sulfate cotransporter gene (Slc13a4): structure and expression

Identification and Characterization of a Novel Interaction between Pulmonary Surfactant Protein D and Decorin

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