Observation of Schlemm's canal and transluminal trabeculotomy using an ophthalmic endoscope: a case report.

BACKGROUND: Gonioscopy-assisted transluminal trabeculectomy is a novel and useful technique for ab interno trabeculotomy. However, gonioscopy-assisted transluminal trabeculectomy is difficult to perform in patients with corneal opacity or in patients with sequelae of cerebral infarction and cervical osteoarthritis with severe limitation of spinal mobility. This is because observing Schlemm's canal during surgery using gonioscopy is difficult. In this report, we introduce a new and beneficial surgical technique of transluminal trabeculotomy for these patients, using an ophthalmic endoscope for cases in which normal gonioscopy-assisted transluminal trabeculectomy is difficult. CASE PRESENTATION: Our patient was a 65-year-old Japanese man with cervical osteoarthritis with severe limitation of spinal mobility who showed primary open-angle glaucoma of the right eye. He had limited conversion of his head during surgery because of complications. Therefore, we performed transluminal trabeculotomy using an ophthalmic endoscope. Finally, ab interno trabeculotomy of 200 degrees was achieved by this method, and an average reduction in ocular pressure of 60% from baseline was achieved after surgery, with no major complications. CONCLUSIONS: This surgical technique may be useful as an alternative method for normal gonioscopy-assisted transluminal trabeculectomy in difficult cases.

A simple and easy method using rigid endoscope to detect iridocorneal and keratolenticular adhesions in peters' anomaly.

Peters' anomaly is characterized by a central corneal opacity with corresponding defects in the posterior stroma, Descemet's membrane, and endothelium. We present 2 cases that showed corneal opacity when examined by topical endoscopic imaging (TEI). Case 1 was a 20-day-old neonatal female who had a central corneal opacity in the left eye. TEI showed that the iris stroma was adhered toward the back of the opacified cornea. Case 2 was a 4-month-old male who had a bilateral corneal opacity. TEI revealed that both a keratolenticular adhesion and a surrounding iridocorneal adhesion were observed behind the area of corneal opacity. The patient was diagnosed as having Peters' anomaly with persistent fetal vasculature. This study demonstrates that TEI is a novel method capable of looking into an eye from only a small area of the clear cornea.

Cytochrome c oxidase contains an extra charged amino acid cluster in a new type of respiratory chain in the amino-acid-producing Gram-positive bacterium Corynebacterium glutamicum.

The membranes from Corynebacterium glutamicum cells contain a hydrophobic di-haem C protein as the cytochrome c subunit of the new type of cytochrome bc complex (complex III in the respiratory chain) encoded by the qcrCAB operon [Sone, N., Nagata, K., Kojima, H., Tajima, J., Kodera, Y., Kanamaru, T., Noguchi, S. & Sakamoto, J. (2001). Biochim Biophys Acta 1503, 279-290]. To characterize complex IV, cytochrome c oxidase and its structural genes were isolated. The oxidase is of the cytochrome aa(3) type, but mass spectrometry indicated that the haem is haem As, which contains a geranylgeranyl side-chain instead of a farnesyl group. The enzyme is a SoxM-type haem-copper oxidase composed of three subunits. Edman degradation and mass spectrometry suggested that the N-terminal signal sequence of subunit II is cleaved and that the new N-terminal cysteine residue is diacylglycerated, while neither subunit I nor subunit III is significantly modified. The genes for subunits II (ctaC) and III (ctaE) are located upstream of the qcrCAB operon, while that for subunit I (ctaD) is located separately. The oxidase showed low enzyme activity with extrinsic substrates such as cytochromes c from horse heart or yeast, and has the Cu(A)-binding motif in its subunit II. A prominent structural feature is the insertion of an extra charged amino acid cluster between the beta2 and beta4 strands in the substrate-binding domain of subunit II. The beta2-beta4 loop of this oxidase is about 30 residues longer than that of major cytochrome c oxidases from mitochondria and proteobacteria, and is rich in both acidic and basic residues. These findings suggest that the extra charged cluster may play a role in the interaction of the oxidase with the cytochrome c subunit of the new type of bc complex.