New Surgical Approach for Mandibular Anterior Root Coverage by Modified Tunnel Technique With Simultaneous Frenuloplasty: Technical Description and 5-Year Recall Case Report.

INTRODUCTION: Root coverage of gingival recessions in the anterior mandible has limited predictability. Mandibular incisors often offers a thin phenotype, a lack of keratinized tissue and moreover a shallow vestibule with high labial frenum attachment. These conditions induce tensions on the surgical site in conventional coronally advanced flap (CAF) procedures and may compromise the complete root coverage. The purpose of this case report is to present a novel surgical technique for deep labial recessions on mandibular incisors, based on a modified tunnel technique with subepithelial connective tissue graft (CTG) in combination with simultaneous frenuloplasty. CASE PRESENTATION: A 20-year-old female patient was referred to the office for treatment of an isolated RT1 in Cairo classification buccal recession on #24 with a shallow vestibule. The design of the recipient site consisted of a full-thickness modified tunnel preparation extending 4 mm bilaterally to the recession and beyond the crestal bone. A CTG was harvested from the palate and properly adapted to the root surface. The graft and flap were secured with single-interrupted sutures and double-crossed sutures to achieve complete root coverage. Frenuloplasty was then performed with a single incision in the bottom of the vestibule and careful sectioning of frenum fibers to release vestibular tensions. Complete root coverage was maintained at 5 years with completely satisfactory esthetic outcomes. CONCLUSION: Treatment of single deep mandibular anterior recessions with a combined tunneled CTG approach in addition to frenuloplasty appears to lead to complete long-term root coverage in one surgery with lasting esthetics results.

Ghrelin uses the GHS-R1a/Gi/cAMP pathway and induces differentiation only in mature osteoblasts. This ghrelin pathway is impaired in AIS patients.

We have examined the Acylated Ghrelin (AG)/Gi pathway in different human osteoblastic cell lines. We have found that: 1) AG induces differentiation/mineralization only in mature osteoblasts; 2) the expression of GHS-R1a increases up to the mature cell stage, 3) the action is mediated via the GHS-R/Gi/cAMP pathway only in mature osteoblasts, and 4) osteoblastic cells from adolescent idiopathic scoliosis (AIS) are resistant to the AG/Gi/cAMP pathway. Altogether, these results suggested that AG uses the GHS-R1a/Gi/cAMP pathway to induce differentiation in mature osteoblasts only. This pathway is impaired in AIS osteoblasts. Understanding AG-specific pathways involved in normal and pathological osteoblasts may be useful for developing new treatments for pathologies such as AIS or osteoporosis.

SHIP2 regulates epithelial cell polarity through its lipid product, which binds to Dlg1, a pathway subverted by hepatitis C virus core protein.

The main targets of hepatitis C virus (HCV) are hepatocytes, the highly polarized cells of the liver, and all the steps of its life cycle are tightly dependent on host lipid metabolism. The interplay between polarity and lipid metabolism in HCV infection has been poorly investigated. Signaling lipids, such as phosphoinositides (PIs), play a vital role in polarity, which depends on the distribution and expression of PI kinases and PI phosphatases. In this study, we report that HCV core protein, expressed in Huh7 and Madin-Darby canine kidney (MDCK) cells, disrupts apicobasal polarity. This is associated with decreased expression of the polarity protein Dlg1 and the PI phosphatase SHIP2, which converts phosphatidylinositol 3,4,5-trisphosphate into phosphatidylinositol 4,5-bisphosphate (PtdIns(3,4)P2). SHIP2 is mainly localized at the basolateral membrane of polarized MDCK cells. In addition, PtdIns(3,4)P2 is able to bind to Dlg1. SHIP2 small interfering RNA or its catalytically dead mutant disrupts apicobasal polarity, similar to HCV core. In core-expressing cells, RhoA activity is inhibited, whereas Rac1 is activated. Of interest, SHIP2 expression rescues polarity, RhoA activation, and restricted core level in MDCK cells. We conclude that SHIP2 is an important regulator of polarity, which is subverted by HCV in epithelial cells. It is suggested that SHIP2 could be a promising target for anti-HCV treatment.