[Study on surgical treatment for lung cancer associated with giant bullous disease].

Five patients of primary lung cancer with giant bullous disease underwent surgery from April 1985 to December 1995. All patients were male and heavy smokers, and the median age was 50 years. The location of the tumor was in the right upper lobe in four patients and in the left upper lobe in the other. Three patients were treated by lobectomy and two by sleeve lobectomy. Histological examination showed large cell carcinoma in four patients and poorly-differentiated adenocarcinoma in the other. The pathological stage was I in three. IIIA in one, and IV in the other. Two of three in stage I have survived for more than 6 years postopertively without recurrence, and the other died of brain metastasis. The stage IIIA case and the IV case died 3 years and one year postoperatively, respectively. The clinical features of lung cancer associated with giant bullous disease was discussed by reviewing 33 patients reported in Japan, including our patients. In 13 patients, lung cancer and bullous disease were diagnosed simultaneously (group A), and in 20 patients, bullous disease were diagnosed prior to the appearance of an abnormal shadow due to lung cancer (group B). The patients in group B had a tendency to be diagnosed at an earlier stage of lung cancer than the patients in group A. In the patients of stage I, the 5-year survival rate was 78.6%, however, in the patients of more than stage IIIA, 3-year survival rate was 26.5% and the 5-year survival rate was 0%. Significant differences in the survival curves were demonstrated between the cases with stage I and the cases with more than stage IIIA. In conclusion, in order to improve the prognosis of lung cancer with giant bullous disease, it is considered to be important to detect giant bulla prior to lung cancer, and when a case of bullous disease is found, periodical follow-up must be done to find early stage lung cancer.

5'-S-(2-aminoethyl)-N6-(4-nitrobenzyl)-5'-thioadenosine (SAENTA), a novel ligand with high affinity for polypeptides associated with nucleoside transport. Partial purification of the nitrobenzylthioinosine-binding protein of pig erythrocytes by affinity chromatography.

Derivatives of N6-(4-aminobenzyl)adenosine (substituted at the aminobenzyl group) and 5'-linked derivatives of N6-(4-nitrobenzyl)adenosine (NBAdo) were evaluated as inhibitors of site-specific binding of [3H]nitrobenzylthioinosine (NBMPR) to pig erythrocyte membranes. Potent inhibitors were SAENTA [5'-S-(2-aminoethyl)-N6-(4-nitrobenzyl)-5'-thioadenosine] and acetyl-SAENTA (the 2-acetamidoethyl derivative of SAENTA). SAENTA was coupled to derivatized agarose-gel beads (Affi-Gel 10) to form an affinity matrix for chromatographic purification of NBMPR-binding polypeptides, which in pig erythrocytes are part of, or are associated with, the equilibrative nucleoside transporter. When pig erythrocyte membranes were solubilized with octyl glucoside (n-octyl beta-D-glucopyranoside) and applied to SAENTA-Affi-Gel 10 (SAENTA-AG10), polypeptides that migrated as a broad band on SDS/PAGE with an apparent molecular mass of 58-60 kDa were selectively retained by the affinity gel. These polypeptides were identified as components of the nucleoside transporter of pig erythrocytes by reactivity with a monoclonal antibody (mAb 11C4) that recognizes the NBMPR-binding protein of pig erythrocytes. Retention of the immunoreactive polypeptides by SAENTA-AG10 was blocked by NBAdo. The immunoreactive polypeptides were released from SAENTA-AG10 by elution under denaturing conditions with 1% SDS or by elution with detergent solutions containing competitive ligands (NBAdo or NBMPR). A 72-fold enrichment of the immunoreactive polypeptides was achieved by a single passage of solubilized, protein-depleted membranes through a column of SAENTA-AG10, followed by elution with detergent solutions containing NBAdo. These results demonstrate that polypeptide components of NBMPR-sensitive nucleoside-transport systems may be partly purified by affinity chromatography using gel media bearing SAENTA groups.

Conformational study of the basic proline-rich polypeptides from human parotid saliva.

The conformational study of two basic proline-rich polypeptides from human parotid saliva, P--D and P--E of known primary structures, was performed by CD and 1H--n.m.r. spectra measurements. These polypeptides contain consecutive sequences of five prolyl residues in their amino acid sequences. The troughs in CD spectra of P--D and P--E were found at 202 and 201 nm, respectively. These wavelengths were different from the value of 206 nm of poly-L-proline form II conformation. In spite of this, the existence of poly-L-proline form II conformation was suggested in the structure of P--D, because the trough for a fragmental peptide of P--D containing five consecutive prolyl residues was found at 204 nm. No remarkable change was detected in CD and 1H--n.m.r. spectra of P--D and P--E in the range of pH 3.0-11.0. The result suggests that no folding of polypeptide which might be affected by ionic interaction exists in its structure.

Conformational study of the salivary proline-rich polypeptides.

The conformational study of three proline-rich polypeptides of human whole saliva, with known primary structures, was performed by CD and 1H-n.m.r. spectra measurements. All these polypeptides contained more than four consecutive prolyl residues in their amino acid sequences. The occurrence of the poly-L-proline form II conformation in their structures was demonstrated with two of these polypeptides. The continuous prolyl residues in the third was suggested to take the same structure as the others.

Retarding effect of dodecyl alcohol on polyacrylamide gel electrophoresis of SDS micelles and SDS-protein polypeptide complexes.

Micelles of sodium dodecyl sulfate (SDS) are significantly retarded by the addition of a small amount of dodecyl alcohol to a sample solution in SDS-polyacrylamide gel electrophoresis. The phenomenon can be ascribed to the decrease in charge density due to the incorporation of dodecyl alcohol into SDS micelles. The effect is extended to SDS-protein polypeptide complexes when the amount of SDS micelles is insufficient to accomodate the dodecyl alcohol. A similar effect is likely to occur when SDS-polyacrylamide gel electrophoresis is applied to a sample containing lipophilic materials.