OBJECTIVETo discuss the primary experience and possibility of direct transsphenoidal pituitary adenoma resection under endoscopic assistance.

METHODSFrom March 2000 to March 2001, 22 patients with pituitary adenoma were treated by direct transsphenoidal pituitary adenoma surgery under endoscope. During direct transsphenoidal approach, no incision of the nasal mucosa was made without the dissection of the nasal septum and median nasal conchae. Under endoscopic assistance, the anterior wall of the sphnoidal sinus and sellae base was opened directly and adenoma resection was performed.

RESULTSAll the patients were followed up for 1 approximately 12 months. The increased hormone level in 17 patients were decreased to normal postoperatively. By postoperative MRI detection, adenomas in 15 patients were removed completely, but part of the adenomas were left in the carvernous sinuses in 7 patients. Temporary diabetes insipidus was observed in 4 patients.

CONCLUSIONSThe direct transsphenoidal approach in pituitary adenoma resection under endoscopic assistance is time saving, and safe, with good exposure of operative field. The injury to the patient and postoperative reaction are less. The effects were satisfactory without severe complications.

Adenoma ; surgery ; Adult ; Aged ; Endoscopy ; Female ; Humans ; Male ; Middle Aged ; Pituitary Neoplasms ; surgery

Proximity labeling catalyzed by promiscuous enzymes,such as APEX2,has emerged as a powerful approach to characterize multiprotein complexes and protein-protein interactions.How-ever,current methods depend on the expression of exogenous fusion proteins and cannot be applied to identify proteins surrounding post-translationally modified proteins.To address this limitation,we developed a new method to label proximal proteins of interest by antibody-mediated protein A-ascorbate peroxidase 2(pA-APEX2)labeling(AMAPEX).In this method,a modified protein is bound in situ by a specific antibody,which then tethers a pA-APEX2 fusion protein.Activation of APEX2 labels the nearby proteins with biotin;the biotinylated proteins are then purified using streptavidin beads and identified by mass spectrometry.We demonstrated the utility of this approach by profiling the proximal proteins of histone modifications including H3K27me3,H3K9me3,H3K4me3,H4K5ac,and H4K12ac,as well as verifying the co-localization of these iden-tified proteins with bait proteins by published ChIP-seq analysis and nucleosome immunoprecipi-tation.Overall,AMAPEX is an efficient method to identify proteins that are proximal to modified histones.