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Objective Nasoalveolar molding (NAM) can optimize aesthetic outcomes in patients with cleft lip and palate (CLP), particularly in those with wider clefts. However, its impact on long-term postoperative sequelae such as midface hypoplasia (MFH) remains unclear. This study analyzed cephalometric data to evaluate NAM's effect on MFH in patients with complete unilateral CLP (UCLP).Design Systematic Review and Meta Analysis.Patients Included studies reported cephalometrics of patients ≥ 7 years old with repaired UCLP who underwent presurgical NAM versus no-NAM (control). Studies of bilateral cases or unoperated clefts were excluded.Main Outcome Measures Main outcomes were cephalometric angles (sella-nasion-A point (SNA), sella-nasion-B point (SNB), and A point-nasion-B point (ANB)) of patients treated with NAM vs. no-NAM.Results Of 2063 articles, three met inclusion criteria. Cephalometrics were reported for 171 patients (89 NAM, 82 no-NAM) at an average age of 8.5 ± 0.9 years. On pooled analysis, compared to the no-NAM cohort, the NAM cohort had insignificantly smaller SNA (78.8°±1.5° vs. 76.7°±1.5°, p = 0.169), SNB (75.5°±1.0° vs. 75.5°±1.0°, p = 0.954), and ANB (3.6°±1.4° vs. 1.23°±1.2°, p = 0.089) angles. Upon meta-analysis, compared to the no-NAM cohort, the NAM cohort had significantly smaller SNA (Mean Difference (MD) −1.96 [−3.31 to −0.61], p = 0.005) and ANB angles (MD −2.22 [−3.20 to −1.24], p < 0.001).Conclusion This meta-analysis revealed that patients with UCLP who underwent presurgical NAM had significantly smaller SNA and ANB angles, possibly indicating worse MFH. Before choosing NAM, clinicians should consider CLP severity, potential sagittal growth restrictions, and feasibility, particularly in low-resource settings.

1,25-Dihydroxyvitamin D3 inhibits the proliferation of the chronic myelogenous leukemia cell line RWLeu-4 but not the resistant variant, JMRD3. Although these cells exhibit no detectable differences in the vitamin D receptor, alterations in the interaction of nuclear extracts with the osteocalcin-1,25-dihydroxyvitamin D3-response element are noted. It is shown herein that the 1,25-dihydroxyvitamin D3 receptor binds to the osteocalcin-1,25-dihydroxyvitamin D3-response element along with activator protein-1 (AP-1) complexes and that the DNA binding activities of members of the Jun and Fos proto-oncogene families, which make up the AP-1 transcription factor, are differentially regulated by 1,25-dihydroxyvitamin D3. It is shown that JunD DNA binding activity is enhanced by 1,25-dihydroxyvitamin D3 during cell cycle arrest in the sensitive cells but is decreased in the resistant cells. These results suggest that the level of JunD DNA binding activity may be a critical factor in the regulation of proliferation.

Rat insulin-like growth factor I (IGF-I) cDNAs contain three alternative 5' untranslated sequences (termed class A, B, and C), which are associated with an identical coding region for the mature IGF-I peptide. A solution hybridization/RNase protection assay was used to simultaneously quantitate the relative abundance of IGF-I transcripts with the different 5' untranslated regions. In all the tissues studied, transcripts with the class C 5' untranslated region were most abundant. In contrast, both class A and B transcripts were tissue specific. Class A transcripts were present in moderate abundance in liver; in low abundance in kidney, lung, testes, and stomach; and were undetectable in muscle, heart, and brain; whereas class B transcripts were detected only in liver. These three classes of 5' untranslated region were also regulated independently by growth hormone. In liver, heart, kidney, and lung, growth hormone increased the abundance of class C transcripts 2- to 3-fold. In liver, growth hormone increased the abundance of the class A and B transcripts 6- to 7-fold. In lung and kidney, on the other hand, the abundance of class A transcripts was not affected by growth hormone. Thus, rat IGF-I gene transcripts contain one of three alternative 5' untranslated regions, which are expressed in a tissue-specific manner and are differentially regulated by growth hormone. Finally, cDNA probes unique to two of the three 5' untranslated regions hybridized to all three major species of IGF-I mRNA typically seen on RNA blots with a coding region probe.

The double-stranded RNA (dsRNA)-dependent protein kinase which catalyzes the phosphorylation of ribosome-associated protein P1 and the alpha subunit of eukaryotic protein synthesis initiation factor 2 (eIF-2) was purified and characterized from mouse fibroblast L929 cells treated with either natural or recombinant interferon and from untreated cells. The dsRNA-dependent P1/eIF-2 alpha kinase was purified at least 1,500-fold from interferon-treated cells; the kinase activity that catalyzed the phosphorylation of eIF-2 alpha copurified with protein P1. The yield of P1/eIF-2 alpha protein kinase activity obtained following purification from cells treated with interferon was about 5-10 times greater than the yield from an equivalent number of untreated cells. The purified protein kinase remained dsRNA dependent. When P1 kinase was activated by dsRNA, a major phosphopeptide designated Xds was phosphorylated; Xds was not phosphorylated from P1 which had not been activated by dsRNA. The apparent native molecular weight of the purified mouse L929 dsRNA-dependent kinase as determined by sedimentation analysis was about 62,000, comparable to the molecular weight of 67,000 determined for denatured L929 phosphoprotein P1 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The purified protein kinase was highly selective for the alpha subunit of protein synthesis initiation factor eIF-2 and endogenous protein P1. Kinase activity was dependent upon Mg2+, and the Km for ATP was determined to be 5 X 10(-6) M. Histones (H1, H2A-B, H3, and H4) and protein synthesis initiation factors other than eIF-2 (eIF-3, eIF-4A, eIF-4B, and eIF-5) were not substrates or were very poor substrates for the purified dsRNA-dependent protein kinase. N-Ethylmaleimide, ethylenediaminetetraacetic acid, AMP, pyrophosphate, spermine, spermidine, and high concentrations of potassium inhibited both P1 and eIF-2 alpha phosphorylation by the purified kinase, whereas ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid and phenanthroline did not significantly affect the phosphorylation of either protein P1 or eIF-2 alpha.