A putative collagen structure from macrophage scavenger receptors binds to a wade range of ligands. In order to elucidate the ligand's binding mode, this collagen structure was constructed using short peptides. This was accomplished by the reaction of a tri-bromoacetylated branched peptide with a purified unprotected 25-residue peptide, which contained Cys, 4 repeats of the triplet, Gly-Pro-Hyp, and 12 residues from the bovine macrophage scavenger receptor (residues 332 to 343). The three identical 25-residue peptides are linked at the N-terminus. CD and NMR spectra of the N-terminus cross-linked tripeptide show that it forms a collagen structure below 10°C and an extended structure at high temperature with a midpoint of 20°C.
This study demonstrated that the presence of extracellular and intracellular mucin, signet-ring cells, small nucleoli, fine granular to vesicular chromatin, and nuclear groove in cytological samples may be a diagnostic clue for ALK-rearranged lung cancer.
ROS1-rearranged lung adenocarcinoma has been recently identified. We report a case of ROS1-rearranged lung adenocarcinoma with special emphasis on cytological findings. Here, we report a case of young woman with ROS1-rearranged lung adenocarcinoma diagnosed by cytology and discuss the clinical, cytological, and molecular findings. Cytologically, the tumor consisted of small tight clusters of cells with high nuclear/cytoplasmic ratio. Nuclei were enlarged and small nucleoli were occasionally observed. Signet-ring cells were focally identified. Neoplastic cells were positive for ROS1 immunocytochemistry. Subsequently, the translocation of ROS1 gene was confirmed in a histological specimen. In conclusion, the specific histology of adenocarcinoma on cytological materials should promote testing for ROS1 immunohistochemistry. Immunocytochemical detection of ROS1 protein helps identify patients suitable for molecular targeted therapy.
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