Transarterial Embolization of Renal Arteriovenous Malformations: Treatment Outcomes According to Angiographic Classification.

PURPOSE: To assess the different adjunctive catheter techniques required to achieve complete occlusion of renal arteriovenous malformations (rAVMs) of different angioarchitectural types. MATERIALS AND METHODS: Overall, data on 18 patients with rAVM (Type 1, n = 7; Type 2, n = 2; Type 3, n = 9; mean age, 53.8 years) who underwent 25 procedures between 2011 and 2022 were reviewed. The clinical presentations, endovascular techniques, arteriovenous malformation (AVM) occlusion rate, adverse events (including the incidence of renal infarction), and clinical symptoms and outcomes (including recurrence/increase of AVM) were analyzed according to the Cho-Do angioarchitectural classification. Posttreatment renal infarction was classified as no infarction, small infarction (<12.5%), medium infarction (12.5%-25%), and large infarction (>25%) using contrast-enhanced computed tomography or magnetic resonance imaging. RESULTS: Hematuria and heart failure were presenting symptoms in 10 and 2 patients, respectively. The embolic materials used were as follows: Type 1 rAVM, coils alone or with n-butyl-2-cyanoacrylate (nBCA); Type 2 rAVM, nBCA alone or with coils; and Type 3 rAVMs, nBCA alone. Fourteen patients underwent adjunctive catheter techniques, including flow control with a balloon catheter and multiple microcatheter placement, alone or in combination. Immediate postprocedural angiography revealed complete occlusion in 15 patients (83%) and marked regression of rAVM in 3 (17%). Small asymptomatic renal infarctions were observed in 6 patients with Type 3 rAVMs without any decrease in renal function. No major adverse events were observed. All symptomatic patients experienced symptom resolution. Recurrence/increase of rAVM was not observed during the mean 32-month follow-up period (range, 2-120 months). CONCLUSIONS: Transarterial embolization using adjunctive catheter techniques according to angioarchitectural types can be an effective treatment for rAVMs.

Subcentimeter large cell neuroendocrine carcinoma of the lung.

To our knowledge, no report exists of a subcentimeter size large cell neuroendocrine carcinoma (LCNEC) of the lung. A 75-year-old man participating in a low-dose CT screening program for lung cancer was found incidentally to have a partly-solid nodule in the right upper lung. After treatment with antibiotics, a repeat CT showed resolution of the nodule, but a new solid nodule measuring 9 x 9 mm was detected in the left lower lobe. The lesion showed marked enhancement on dynamic contrast-enhanced MRI. Video-assisted thoracic surgery and frozen section biopsy was suggestive of malignant lesion, resulting in extension of surgery to lobectomy with nodal dissection. The final diagnosis was stage IA-LCNEC. The estimated volume doubling time of the tumor was 30.1 days. These aggressive tumors may rarely have doubling times that overlap with benign processes.

SHEPHERD is the Arabidopsis GRP94 responsible for the formation of functional CLAVATA proteins.

The Arabidopsis shepherd (shd) mutant shows expanded shoot apical meristems (SAM) and floral meristems (FM), disorganized root apical meristems, and defects in pollen tube elongation. We have discovered that SHD encodes an ortholog of GRP94, an ER-resident HSP90-like protein. Since the shd phenotypes in SAM and FM are similar to those of the clavata (clv) mutants, we have explored the possibility that CLV complex members could be SHD targets. The SAM and FM morphology of shd clv double mutants are indistinguishable from those of clv single mutants, and the wuschel (wus) mutation is completely epistatic to the shd mutation, indicating that SHD and CLV act in the same genetic pathway to suppress WUS function. Moreover, the effects of CLV3 overexpression that result in the elimination of SAM activity were abolished in the shd mutant, indicating that CLV function is dependent on SHD function. Therefore, we conclude that the SHD protein is required for the correct folding and/or complex formation of CLV proteins.