The addition of radiotherapy tended to decrease the rate of local failure (P =.13), but did not significantly improve survival (P =.73), because of the high rate of distant metastatic disease.
Abstract. Mucopolysaccharidosis VII was diagnosed in a domestic shorthair cat from California. The cat was small and had multiple abnormalities, including a small body disproportionate to the size of the skull, angular deformities of the ribs, abnormally short forelimbs, luxating patellas, generalized epiphyseal dysplasia involving the vertebrae and long bones, cuboidal vertebrae, pectus excavatum, subluxation of both hips, osteosclerosis of the tentorium cerebelli and left petrous temporal bone, tracheal hypoplasia, and corneal clouding. -Glucuronidase activity was markedly decreased in peripheral blood leukocytes. The cat died at 21 months of age, and a complete necropsy was performed. Tissues were examined by light and transmission electron microscopy. Large clear, round vacuoles representing distended lysosomes were present in many epithelial and connective tissue cells, including fibrocytes, chondrocytes, smooth muscle cells, hepatocytes, astrocytes, and macrophages.
In many lipid systems, the activity of protein kinase C (PKC) exhibits a peak followed by a decline as the mol % of one component is increased. In these systems, an increase in one lipid component is always at the expense of another or accompanied by a change in total lipid concentration. Here we report that in saturated phosphatidylserine (PS)/phosphatidylcholine (PC)/diacylglycerol (DAG) mixtures, increasing PS or DAG at the expense of PC revealed an optimal mol % PS, dependent on mol % DAG, with higher mol % PS diminishing activity. The decrease at high mol % PS is probably not attributable simply to more gel-phase lipid due to the higher melting temperature of saturated PS versus PC because a similar peak in activity occurred in unsaturated lipid systems. Increasing the total lipid concentration at suboptimal mol % PS provided the same activity as higher mol % PS at lower total lipid concentration. However, at optimal mol % PS, activity increased and then decreased as a function of total lipid concentration. PKC autophosphorylation also exhibited an optimum as a function of mol % PS, and increasing the PKC concentration increased the mol % PS at which activity decreased, both for autophosphorylation and for heterologous phosphorylation. Formation of two-dimensional crystals of PKC on lipid monolayers also exhibited a peak as a function of mol % PS, and the unit cell size of the crystals formed shifts from 50 ؋ 50 Å at low mol % PS to 75 ؋ 75 Å at higher PS. Collectively, these data suggest the existence of optimal lipid compositions for PKC activation, with increased quantity of these domains serving to dilute out enzyme-substrate aggregates and/or enzyme-enzyme aggregates on the lipid surface.Protein kinase C (PKC) 1 (1), which constitutes a family of structurally related kinases, is defined by the phospholipid dependence of its activity, with all isozymes activated by acidic phospholipids, preferably phosphatidylserine (PS), and all but PKC and PKC/ further stimulated by diacylglycerols (DAG) or phorbol esters. The originally identified ␣, , and ␥ family members also require calcium binding to the C2 domain, which is distinct in these isozymes (for reviews, see Refs. 2-4). Although the role of some lipid components is becoming better defined, variable results in different systems leave many questions unanswered.Structural analyses of DAG and phorbol ester analogues (5-7) and analysis of PKC deletions and mutations argue for specific phorbol ester and DAG binding to the Cys-rich, zinccontaining C1 domain (8 -11). X-ray fluorescence (12), NMR (13), and x-ray crystallography (14) have revealed the structure of this domain. Binding of phorbol ester does not alter the conformation, but helps to present a hydrophobic surface on the domain that could facilitate insertion into the membrane to a depth of 7-8 Å (14). The two versions of the C1 domain, C1A and C1B, present in most PKC isozymes have structural differences (reviewed in Ref. 15) that may account for greatly differing affinities of fluorescent phorbol e...
Objective: To evaluate the expression of cyclooxygenase (COX) and lipoxygenase (LO) enzymes in nasal polyp specimens from aspirin-sensitive (AS) and aspirintolerant (AT) patients.Design: Immunohistochemical staining of archived tissue.Subjects: Specimens from 26 patients (11 AS and 15 AT) with nasal polyps were analyzed; specimens from 4 patients were used as controls.Interventions: Immunohistochemical techniques were used to evaluate the expression of the enzymes COX-1, COX-2, 5-LO, 12-LO, and 15-LO in nasal polyp tissue specimens from AS and AT patients. The results were compared with those of a control group of patients without a history of nasal polyposis or rhinosinusitis.Results: Characteristic staining patterns of epithelium and submucosal glands were noted for each enzyme. Statistically significant (PϽ.05) differences in staining of co-
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