The Multiple Rhomboid Vector Suture-Our Experience of Two Years with a Modified Suspension Approach for SMAS Plication Facelifts.

Purse string sutures in superficial musculoaponeurotic system (SMAS) plication facelifts may cause technique-related problems, such as soft tissue deformities, dimpling, and bulkiness inside and between the independent sutures. Therefore, the authors have developed a new approach named the multiple rhomboid vector (MRV) suture. A total of 103 patients (89 female, 14 male patients; median age: 57 years) received a primary rhytidectomy with the MRV SMAS plication suture in our clinic (2015-2017). Intraoperative time to perform the suture per side was recorded. Postoperative complications and dimpling and bulkiness of subcutaneous tissues were judged by three independent surgeons from 1 (= none) to 4 (= extreme) after 1 week, 1, 3, 6, and 12 months. A standardized survey, the FACE-Q questionnaire, was performed to evaluate postoperative patient satisfaction. Mean time to perform the suture was 5:14 minutes per side (minimum: 3:20 minutes, maximum: 5:53 minutes; standard deviation: 0:51 minutes). During the follow-up period, four complications were detected (two cases of temporary neurapraxia of the marginal branch of the mandibular nerve {n = 2 [1.9%]} and two cases of retroauricular hematoma {n = 2 [1.9%]}). Postoperative dimpling or bulkiness of subcutaneous tissues was judged as absent. Overall patient satisfaction rate, after the surgery was performed, was measured as "very high." The MRV suture offers a combined horizontal and vertical suspension approach, which effectively addresses the different vectors of age-related facial soft tissue descent with complication rates equal to other surgical lifting techniques. Apart from that, it may help reduce the possibility of contour irregularities, whereby it must be noted that a thorough preoperative assessment together with the patient and surgical planning is crucial to ensure realistic expectations of the surgical outcome.

Gαi2- and Gαi3-specific regulation of voltage-dependent L-type calcium channels in cardiomyocytes.

BACKGROUND: Two pertussis toxin sensitive G(i) proteins, G(i2) and G(i3), are expressed in cardiomyocytes and upregulated in heart failure. It has been proposed that the highly homologous G(i) isoforms are functionally distinct. To test for isoform-specific functions of G(i) proteins, we examined their role in the regulation of cardiac L-type voltage-dependent calcium channels (L-VDCC). METHODS: Ventricular tissues and isolated myocytes were obtained from mice with targeted deletion of either Gα(i2) (Gα(i2) (-/-)) or Gα(i3) (Gα(i3) (-/-)). mRNA levels of Gα(i/o) isoforms and L-VDCC subunits were quantified by real-time PCR. Gα(i) and Ca(v)α(1) protein levels as well as protein kinase B/Akt and extracellular signal-regulated kinases 1/2 (ERK1/2) phosphorylation levels were assessed by immunoblot analysis. L-VDCC function was assessed by whole-cell and single-channel current recordings. RESULTS: In cardiac tissue from Gα(i2) (-/-) mice, Gα(i3) mRNA and protein expression was upregulated to 187 ± 21% and 567 ± 59%, respectively. In Gα(i3) (-/-) mouse hearts, Gα(i2) mRNA (127 ± 5%) and protein (131 ± 10%) levels were slightly enhanced. Interestingly, L-VDCC current density in cardiomyocytes from Gα(i2) (-/-) mice was lowered (-7.9 ± 0.6 pA/pF, n = 11, p<0.05) compared to wild-type cells (-10.7 ± 0.5 pA/pF, n = 22), whereas it was increased in myocytes from Gα(i3) (-/-) mice (-14.3 ± 0.8 pA/pF, n = 14, p<0.05). Steady-state inactivation was shifted to negative potentials, and recovery kinetics slowed in the absence of Gα(i2) (but not of Gα(i3)) and following treatment with pertussis toxin in Gα(i3) (-/-). The pore forming Ca(v)α(1) protein level was unchanged in all mouse models analyzed, similar to mRNA levels of Ca(v)α(1) and Ca(v)ß(2) subunits. Interestingly, at the cellular signalling level, phosphorylation assays revealed abolished carbachol-triggered activation of ERK1/2 in mice lacking Gα(i2). CONCLUSION: Our data provide novel evidence for an isoform-specific modulation of L-VDCC by Gα(i) proteins. In particular, loss of Gα(i2) is reflected by alterations in channel kinetics and likely involves an impairment of the ERK1/2 signalling pathway.