Bronchoalveolar lavage in interstitial lung diseases: does the recovery rate affect the results?

BACKGROUND: Bronchoalveolar lavage (BAL) is an established diagnostic tool in interstitial lung diseases. BAL frequently yields findings of diagnostic value and at times even confirmatory diagnostic results. OBJECTIVES: The present study has been designed to investigate whether the recovery rate affects BAL results relative to the instilled volume. METHODS: Six hundred and eighteen patients with the following diagnoses were included into the study: 236 with sarcoidosis, 85 with idiopathic pulmonary fibrosis, 83 with cryptogenic organizing pneumonitis, 64 with connective tissue disease affecting the lungs, 54 with respiratory bronchiolitis with interstitial lung disease, 51 with extrinsic allergic alveolitis and 45 control patients. BAL was performed during flexible bronchoscopy with an irrigation volume of 100 ml 0.9% saline solution in 5 aliquots of 20 ml each. Only patients with a recovery of at least 30 ml were evaluated. Initially, the entire patient population was analysed, followed by an analysis within the different diagnostic groups and a comparison between patients with a high (>50 ml) and low (< or =50 ml) recovery rate. RESULTS: The recovery rate varied between the diagnostic groups (p < 0.001) and was negatively correlated with age (r = -0.21, p < 0.001) and smoking history (r = -0.11, p < 0.035). There were no correlations with inspiratory vital capacity (%pred.; p = 0.26) and forced expiratory volume in 1 s (%pred.; p = 0.15), but a positive correlation with the index (forced expiratory volume in 1 s/inspiratory vital capacity) x 100 (r = 0.23, p < 0.001). The cellular and non-cellular constituents of BAL were not affected by the recovery: cells/millilitre BAL (p = 0.71), relative proportion of macrophages (p = 0.92), lymphocytes (0 = 0.33), neutrophils (p = 0.14) and eosinophils (p = 0.11), albumin concentration (p = 0.13), and proportion of albumin in total protein (p = 0.06). The same applied for the lymphocyte surface markers CD4 (p = 0.72) and CD8 (p = 0.53). In the group with a high recovery rate, patients with sarcoidosis had a lower proportion of eosinophils (p = 0.04) and patients with cryptogenic organizing pneumonitis a higher concentration of albumin (p = 0.02) and lymphocytes (p = 0.007). Otherwise, no further differences were detected. CONCLUSIONS: The recovery rate hardly affected the cellular and non-cellular constituents of BAL at a lower limit of 30% of the instilled volume.

Morphologic changes of the anal sphincter musculature during and after temporary stool deviation.

BACKGROUND AND AIMS: Temporary stool deviation, using a stoma, is a well-known surgical principle to protect low colorectal or coloanal anastomoses. The purpose of this study was to evaluate any morphologic changes with regard to the anal sphincter muscles during and after temporary ileostomy. PATIENTS AND METHODS: Forty-four patients with rectal carcinomas were studied prospectively. All patients underwent low anterior resection. Reconstruction was performed using either a coloanal pouch or a straight end-to-end anastomosis. A protective stoma was fashioned in all 44 patients (ileostomy n=41; colostomy n=3). Stoma closure was carried out after a median of 85 days (41-330 days). Using a standard protocol, anal-sphincter thickness [m. puborectalis, external anal sphincter (EAS) and internal anal (IAS) sphincter] was assessed by means of endoanal ultrasonography preoperatively, at the time of stoma closure, and every 3 months thereafter for 1 year. RESULTS: The diameter of the puborectal muscle decreased from a median preoperative value of 6.3 mm to 5.7 mm at the time of stoma closure (P=0.03). After 3 months, 6.2 mm was measured. This value remained stable for the complete follow-up period. Similar results were recorded for the EAS. The IAS thickness remained stable throughout the study period, measuring between 2.1 mm and 2.4 mm. CONCLUSION: Temporary stool deviation does lead to morphologic changes of the anal sphincter. While the smooth muscle remains unchanged, the striated counterpart undergoes atrophic transformation. However, after passage reconstruction, i.e., stoma closure, a rapid regeneration of the voluntary muscles is observed.

Tryptophan glycoconjugates in food and human urine.

Evaluating the formation of tryptophan glycoconjugates other than well-established Amadori rearrangement products, HPLC-tandem MS (MS/MS) analysis of human urine collected from several healthy individuals proved the presence of one distinct tryptophan C-glycosyl compound [Horiuchi, Yonekawa, Iwahara, Kanno, Kurihara and Fujise (1994) J. Biochem. (Tokyo) 115, 362-366]. After isolation, unambiguous identification of this novel tryptophan metabolite as 2-(alpha-mannopyranosyl)-l-tryptophan was achieved by tandem MS combined with NMR spectroscopy including homonuclear COSY, heteronuclear multiple-bond connectivity and (1)H-detected heteronuclear multiple-quantum coherence experiments. Remarkably, a thorough evaluation of vicinal proton-proton coupling constants in different solvents and nuclear Overhauser effect experiments demonstrate the predominant axial orientation of the hydroxymethyl group of the hexopyranosyl residue. Likewise this spatial arrangement indicates that the respective alpha-anomeric C-mannosylhexopyranose is preferentially adopting a (1)C(4) conformation in acidic methanol. Whereas only one distinct tryptophan mannoconjugate could be observed in human urine, HPLC-MS/MS analysis of food samples for the first time led to the identification of numerous N(1)-(beta-d-hexopyranosyl)-l-tryptophan, 2-(beta-d-hexopyranosyl)-l-tryptophan and 1-(1,2,3,4,5-pentahyd- roxypent-1-yl)-1,2,3,4-tetrahydro-beta-carboline-3-carboxylic acid derivatives derived from the condensation of tryptophan with aldohexoses. Taking into consideration the significant differences between profiles and configurations of tryptophan glycoconjugates originating from dietary sources and human urine, C-2 mannosylation of tryptophan residues [de Beer, Vliegenthart, Loeffler and Hofsteenge (1995) Biochemistry 34, 11785-11789] represents a novel enzymic pathway in tryptophan metabolism in humans.