Pancreatic and Gastric Plasmacytoma Presenting with Obstructive Jaundice, Diagnosed with Endoscopic Ultrasound-Guided Fine Needle Aspiration

Pancreatic plasmacytoma is a rare disorder which may present with obstructive jaundice. Only eighteen cases have been reported in the English language literature. We present the first case of pancreatic plasmacytoma and gastric plasmacytoma diagnosed with endoscopic ultrasound-guided fine needle aspiration (EUS-FNA). A 75-year-old male with a known history of multiple myeloma presented with obstructive jaundice and a pancreatic mass. A concomitant gastric mass due to gastric plasmacytoma was seen. The diagnosis was established via EUS-FNA of the pancreatic mass. Pancreatic plasmacytoma should be suspected in patients with a history of myeloma. EUS-FNA is a safe and effective modality in the diagnosis of pancreatic plasmacytoma. Radiation therapy should be the first-line of therapy in treating pancreatic plasmacytomas

PECAM-Independent Thioglycollate Peritonitis Is Associated With a Locus on Murine Chromosome 2

Background: Previous studies have demonstrated that knockout or inhibition of Platelet/Endothelial Cell Adhesion Molecule (PECAM, CD31) in a number of murine strains results in impaired inflammatory responses, but that no such phenotype is seen in the C57BL/6 (B6) murine background. Methodology/Principal Findings: We have undertaken a quantitative trait locus (QTL) mapping effort between FVB/n (FVB) and B6 mice deficient for PECAM to identify the gene or genes responsible for this unique feature of B6 mice. We have identified a locus on murine chromosome 2 at approximately 35.8 Mb that is strongly associated (LOD score = 9.0) with inflammatory responses in the absence of PECAM. Conclusions/Significance: These data potentiate further study of the diapedesis machinery, as well as potential identification of new components of this machinery. As such, this study is an important step to better understanding the processes of inflammation

A cytokine-neutralizing antibody as a structural mimetic of 2 receptor interactions

TGF-β isoforms are key modulators of a broad range of biological pathways and increasingly are exploited as therapeutic targets. Here, we describe the crystal structures of a pan-TGF-β neutralizing antibody, GC-1008, alone and in complex with TGF-β3. The antibody is currently in clinical evaluation for idiopathic pulmonary fibrosis, melanoma, and renal cell cancer. GC-1008 recognizes an asymmetric binding interface across the TGF-β homodimer with high affinity. Whereas both cognate receptors, TGF-β-receptor types I and II, are required to recognize all 3 TGF-β isoforms, GC-1008 has been engineered to bind with high affinity to TGF-β1, 2, and 3 via a single interaction surface. Comparison with existing structures and models of TGF-β interaction with its receptors suggests that the antibody binds to a similar epitope to the 2 receptors together and is therefore a structurally different but functionally identical mimic of the binding mode of both receptors