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The effect of intermittent external negative pressure ventilation (ENPV) with the Emerson Pulmowrap ventilator upon leg cycle endurance time (ET), maximal transdiaphragmatic pressure (Pdimax), breathing pattern as expressed by the tension time index (TTdi), and sense of well being was studied in 16 patients with severe chronic airflow obstruction (CAO). The patients were randomized to 3 wk of in-hospital pulmonary rehabilitation (Group I, seven patients) or the same program plus ENPV (Group II, nine patients). Both groups were similar in terms of age (65 +/- 8 versus 61 +/- 13 yr), severity of CAO (FEV1 of 0.64 +/- 0.14 versus 0.59 +/- 0.18 L), and PaCO2 (44 +/- 9 versus 45 +/- 7 mm Hg). Blood theophylline levels and nutritional status were also similar in both groups. Baseline ET (2.9 +/- 0.6 versus 3.8 +/- 1.6 min) and Pdimax (45 +/- 15 versus 56 +/- 18 cm H2O) were decreased in both groups. Baseline TTdi was high but similar in both groups; at rest the values were 0.15 +/- 0.05 versus 0.16 +/- 0.04, and at end-exercise they were 0.17 +/- 0.06 versus 0.21 +/- 0.12. After treatment FEV1 and Pdimax remained unchanged, but the patients in both groups manifested clinical improvement and had a significant increase in mean ET (Group I from 2.9 to 6.9 and Group II from 3.8 to 6 min, p less than 0.01). TTdi decreased both at rest (0.14 +/- 0.07 versus 0.13 +/- 0.04) and at end-exercise (0.14 +/- 0.06 versus 0.15 +/- 0.09) with no difference between groups.(ABSTRACT TRUNCATED AT 250 WORDS)

When human and rat epidermis are exposed to 32P-orthophosphoric acid, labeled phosphate is incorporated into several proteins. The pattern of phosphorylation is identical whether the isotope is delivered in vivo or in vitro. The predominant phosphorylated proteins are insoluble in Tris-HCl buffer but soluble in SDS-beta-mercaptoethanol. They migrate in SDS-polyacrylamide gels with apparent molecular weights between 45,000 and 65,000. When analyzed by two-dimensional gel electrophoresis, the labeled phosphoproteins co-migrate with keratins isolated from human callus. Serine is the phosphate acceptor in these proteins. The pattern of phosphorylation of these SDS-beta-mercaptoethanol soluble epidermal proteins is not changed in basal cell carcinoma, icthyosis vulgaris, Kyrle's disease or Netherton's syndrome. The pattern is altered in psoriasis. Others have demonstrated that a 63,000 molecular weight protein is absent from active psoriatic lesions. We have found that a 63,000 molecular weight phosphoprotein is present in uninvolved skin but absent in the psoriatic plaques.

Mouse major urinary proteins (MUPs) are encoded by a family of about 35 to 40 highly conserved genes. In the preceding paper (K. Shahan, M. Gilmartin, and E. Derman, Mol. Cell. Biol. 7:1938-1946, 1987), we presented the sequences of the most abundant MUP mRNAs in the liver (MUP I, II, and III) and in the lachrymal (MUP IV) and submaxillary (MUP V) glands. We have shown that these five mRNAs are coded by five distinct genes, MUP I through V. In the present communication, we examine the expression of MUP genes in all of the six tissues in which MUP mRNAs are synthesized, the mammary, parotid, sublingual, lachrymal, and submaxillary glands and the liver. We show that gene MUP II is expressed in the liver and in the mammary gland, that gene MUP IV is expressed in the lachrymal and parotid glands, and that gene MUP V is expressed in the submaxillary, sublingual, and lachrymal and parotid glands, and that gene MUP V is expressed in the submaxillary, sublingual, and lachrymal glands. Furthermore, we present evidence that in addition to genes MUP I through V, another gene, MUP VI, is expressed in BALB/c mice in the parotid gland. The tissue-specific synthesis of MUP mRNAs is thus brought about by two major mechanisms: the expression, in different tissues, of different members of the family and the expression of a single gene at various levels in different tissues. When a particular MUP gene is expressed in several tissues, transcripts of this gene initiate at the same site and are spliced and polyadenylated in the same manner.