Kedudukan Anak Akibat Batalnya Perkawinan Karena Hubungan Darah Menurut Hukum Positif

Penelitian ini dilakukan dengan tujuan untuk mengetahui bagaimana pengaturan hukum tentang Pembatalan Perkawinan karena hubungan darah menurut Hukum Positif Di Indonesia dan bagaimana kedudukan hukum anak yang lahir setelah pembatalan perkawinan menurut Hukum Positif di Indonesia. Dengan menggunakan metode penelitian yuridis normatif, maka dapat disimpulkan: 1. Pengaturan hukum mengenai pembatalan perkawinan di Indonesia masih beragam walaupun Undang-Undang perkawinan yaitu Undang-Undang Nomor 1 Tahun 1974 seringkali disebut unifikasi hukum perkawinan. Pembatalan perkawinan merupakan putusnya perkawinan disebabkan persyaratan perkawinan yang diatur dalam undang-undang dan larangan perkawinan tidak dipenuhi. 2. Status hukum anak yang lahir dalam perkawinan yang telah batal pada dasarnya merupakan anak yang sah sebagaimana diatur dalam Undang-Undang Nomor 1 Tahun 1974 dalam Pasal 28. Berdasarkan Putusan Mahkamah Konstitusi Nomor 46/PUU-VIII/2010 Tentang Pengujian pasal 2 ayat 2 dan pasal 43 ayat 1 Undang-Undang Perkawinan yaitu Undang-Undang Nomor 1 Tahun 1974 yang menyatakan bahwa pasal 43 ayat Undang-Undang Nomor 1 Tahun 1974 melanggar Undang-Undang Dasar Republik Indonesia pasal 28 B ayat 1 dan 2 dan pasal 28 D ayat 1

Wnt3a inhibits cell proliferation, but increases cell migration and contraction after 72 hour treatment.

<p>(A) Cell proliferation was measured after 72 hours of treatment with Wnt3a or vehicle. Wnt-treated cells grew at 77.4±4.5% the rate of vehicle treated cells (p<0.05). (B) Cells were treated for 72 hours with Wnt3a or vehicle, and then a scratch wound assay was performed to measure cell migration. Wnt-treated cells closed the scratch wound at a significantly faster rate than vehicle-treated cells, as measured 48 hours after injury (78.1±2.1% vs 61.9±3.8%, p<0.05). (C) Cells were treated for 72 hours with Wnt3a or vehicle and then a fibroblast-populated collagen lattice contraction assay was performed. Images of contracted gels taken at 24 hours are shown along with the quantified surface areas of contracted gels. Wnt3a treatment significantly increased the fibroblast-mediated contraction of collagen gels (16.1±0.6% vs 29.4±1.3% of initial surface area, p<0.05). (* denotes p<0.05)</p

Wnt3a increases TGF-β expression, SMAD2 phosphorylation and smooth muscle α-actin expression.

<p>(A) Representative Western blot of TGF-β expression in vehicle-treated and Wnt3a-treated fibroblasts after 72 hours. Densitometry showed TGF-β expression to be significantly increased after Wnt3a treatment (p<0.05). (B) Western blot of SMAD2 phosphorylation after 72 hours of vehicle or Wnt3a treatment. Densitometry showed Wnt3a significantly increased SMAD2 phosphorylation at 72 hours. (C) Western blot of smooth muscle α-actin expression in vehicle-treated or Wnt3a-treated cells. Wnt3a-treatment significantly increased the expression of smooth muscle α-actin expression in mouse fibroblasts, as measured by densitometry (p<0.05). (D) Confocal images of fibroblasts immunostained for smooth muscle α-actin (green) and nuclei (blue). Wnt3a-treated fibroblasts had clearly visible smooth muscle α-actin positive stress fibres while the vehicle-treated cells did not display expression of smooth muscle α-actin in their stress fibres. (Scale bar = 47.00 µm in D, * denotes p<0.05)</p

Wnt3a induces canonical Wnt signaling in mouse fibroblasts.

<p>Confocal images of fibroblasts treated for 24 hours with vehicle (top panels) or 250 ng/mL Wnt3a (bottom panels) and immunonstained for β-catenin (green) and nuclei (blue). Wnt3a treatment induced clear nuclear accumulation of β-catenin in murine fibroblasts (arrows). (B) TOPFlash reporter assay demonstrated Wnt3a significantly increased luciferase activity 5.3±1.6 fold after a 24 hour treatment (p<0.05). (C) Wnt3a treatment induced a 255±71 fold increase in the mRNA expression of axin2, a target of classical Wnt signaling (p<0.05). (Scale bar = 23.00 µm in A, * denotes p<0.05)</p

Wnt3a-induced change in cell phenotype is dependent on TGF-β expression.

<p>(A) Representative Western blots of vehicle- and Wnt3a-treated fibroblasts showing TGF-β expression, SMAD2 phosphorylation, and smooth muscle α-actin expression at 12, 24, 48, and 72 hours of treatment. (B) Graphical representation of the densitometry results for the blots in A shows, in a sequential manner, that TGF-β expression peaks between 12 and 24 hours, followed by SMAD2 phosphorylation peaking between 24 and 48 hours, which is then followed by smooth muscle α-actin expression peaking after 72 hours of treatment. (C) Western blot of SMAD2 phosphorylation in fibroblasts treated with or without Wnt3a and a TGF-β neutralizing antibody. Densitometry demonstrated the TGF-β neutralizing antibody significantly inhibited Wnt3a-induced SMAD2 phosphorylation (p<0.05). No change was seen in the vehicle-treated cells (p = 0.74). (D) Western blot of smooth muscle α-actin expression in fibroblasts treated with or without Wnt3a and the TGF-β neutralizing antibody. Densitometry confirmed TGF-β neutralization significantly inhibited the Wnt3a-induced smooth muscle α-actin expression (p<0.05). No change was seen in vehicle-treated cells (p = 0.71). (* denotes p<0.05)</p

Wnt3a induces a spindle-like morphology with increased stress fibre formation after 72 hours of treatment.

<p>(A) Light microscope images of mouse fibroblasts that had been treated for 72 hours with vehicle (left panel) or 250 ng/mL Wnt3a (right panel). Wnt3a treatment induced a spindle-like morphology in fibroblasts. (B) Confocal images of vehicle-treated (left panel) or Wnt3a-treated (right panel) fibroblasts immunostained for f-actin (red) and nuclei (blue) showing the increased formation and parallel organization of stress fibres following 72 hours Wnt3a treatment. (C) Low density culture of vehicle-treated (left panel) or Wnt3a-treated (right panel) fibroblasts highlights the increased formation of stress fibres seen after Wnt3a treatment. (Scale bars = 47.00 µm in B, 23.00 µm in C)</p

Increased decorin in plaques from granzyme B and perforin deficient apolipoprotein Eknockout mice.

<p>Representative images of aortic root sections fromapolipoprotein E knockout (ApoE KO), granzyme B (GzmB)/ApoE double knockout (DKO) and perforin (Prf1)/ApoE DKO mice stained for decorin. Decorin in the GzmB deficient animals was observed near the surface of the plaque in concentrated pockets (black arrowheads) while decorin in Prf1 deficient animals stained more diffusely throughout the plaque (white arrowheads). White scale bars = 50 µm, black scale bars = 500 µm.</p

Expression of granzyme A, T cells and macrophages in atherosclerotic plaques.

<p>Representative images of wild type (WT), apolipoprotein E knockout (ApoE KO), granzyme B (GzmB)/ApoE double knockout (DKO) and perforin(Prf1)/ApoE DKO mouse aortas stained for (A) granzyme A, (B) CD3 and (C) F4/80. Scale bars = 100 µm.</p

Granzyme B, but not perforin deficiency results in increased collagen content in atherosclerotic plaques.

<p>(A) Representative images of aortic root sections stained for collagen using picrosirius red and visualized under bright field or polarized light. Bright field images were used to define the area of plaque and collagen was quantified using the images taken under polarized light. Scale bars = 500 µm. (B) Compared to the high fat diet-fed apolipoprotein E knockout (ApoE KO) mice (n = 4), granzyme B (GzmB)/ApoE double knockout (DKO) mice (n = 6) exhibited increased collagen content in atherosclerotic plaques of the aortic root. Perforin (Prf1)/ApoE DKO mice (n = 5) on the other hand, showed no difference in collagen content compared to ApoE KO mice and significantly less collagen compared to GzmB/ApoE DKO mice. *P<0.05, ***P<0.005 (One-way ANOVA with bonferronipost test). Error bars represent SEM.</p

Versican increases N-cadherin expression.

<p>(A) Light microscopy shows no major change in cell morphology in versican-transfected fibroblasts at both sub-confluent and confluent densities. (B) Representative Western blot showing increased expression of N-cadherin in versican-transfected cells. (C) Confocal microscopy confirmed the increased N-cadherin expression in versican-transfected cells. (Scale bar = 12.00 μm).</p