Search PubMed⌕ Search

Biomedical subjects

J Sarles

Publications and source records attributed to J Sarles.

65 records · Page 4Linked to original sources
PubMed1985

Aminopeptidase N- and human blood group A-antigenicity along the digestive tract and associated glands in the rabbit.

The cellular localization of an aminopeptidase N homologous to the brush-border intestinal enzyme and that of human blood group A-substances were investigated using the immunofluorescence technique on thin frozen sections (200 nm) of the digestive tract and associated glands of A+ and A- rabbits. Aminopeptidase N was found to be a common specific marker of both the apical region of plasma membrane of acinar cells in submaxillary and parotid glands and pancreas and the brush border of jejunum and colon absorbing cells. In hepatocytes, the enzyme was localized in the sinusoidal domains. Soluble A-substances were present in mucus secretory granules of intestinal goblet cells and those of stomach and gall bladder mucous cells. In contrast, the mucous acini of sublingual and submaxillary glands were devoid of A-antigenicity. The columnar cells of striated ducts of these glands exhibited A-antigenicity. Soluble A-substances were also found in zymogen granules of parotid and pancreas acinar cells and those of stomach chief cells. Moreover, in all cells secreting A-substances, and in the non-secreting absorbing intestinal cells, the glycoproteins of the plasma membrane bore A-determinants. Aminopeptidase N was one of the membrane-bound glycoproteins that bore A-determinants in cells that expressed A-antigenicity.

ABO Blood-Group System↗
PubMed1984

Cellular localization of class I (HLA-A, B, C) and class II (HLA-DR and DQ) MHC antigens on the epithelial cells of normal human jejunum.

HLA class I and class II (HLA-DR (human I-E equivalent) and DQ (human I-A equivalent] antigens were localized by immunofluorescence technique on thin frozen sections of normal human jejunum using a panel of monomorphic monoclonal antibodies. HLA class I (A, B and C) and HLA-DR molecules were found in the basolateral membrane of enterocytes; HLA-DR were also detected in a patchy distribution in the apical part of enterocytes; HLA-DQ molecules (the human equivalent of the murine I-A molecular subset) were not detected on normal enterocytes. All three molecules were detected on the membrane of lymphocytes and monocytes present in the lamina propria.

Cell Membrane↗
PubMedDate not supplied

Subcellular localization of class I (A,B,C) and class II (DR and DQ) MHC antigens in jejunal epithelium of children with coeliac disease.

Thin frozen sections of 11 jejunal biopsies from 10 children at different stages of coeliac disease were stained by immunofluorescence technique using a panel of anti-HLA class I (A, B, C) and anti-HLA class II (DR and DQ) monoclonal antibodies. On the epithelium of flattened mucosa, in contrast with control sections, the intensity of the labeling on the basolateral membranes with both anti-class I and class II DR antibodies decreased strongly from the bottom to the upper part of the crypts, and no bright patchy staining was observed on the apical part of enterocytes with anti-HLA DR antibodies. Numerous cells with large granules expressing class I and class II DR antigens were found in the epithelium of the small intestine. Children with a fully recovered mucosa expressed MHC antigens identical to those previously observed in normal epithelium. On the other hand, children with intermediate mucosal lesions showed the presence of MHC antigens in varying degrees. The results of this report indicate that immunological mechanisms may play a prominent role in coeliac disease.

Celiac Disease↗
PubMedDate not supplied

Human gastric lipase: ontogeny and variations in children.

The aim of this study was to investigate the precise origin of the acid pre-duodenal lipase during human development and to evaluate its possible changes, at the tissue level, in children with gastritis or pancreatic insufficiency. Human gastric lipase appears around the 11th week of gestation and increases slowly during pre- and postnatal development. It is localized in the fundus of the stomach without any lingual localization. Human gastric lipase reaches its adult level in the third month of life, and does not vary in relation to pancreatic insufficiency. It is only rarely impaired during gastritis.

Adolescent↗
PubMedDate not supplied

[Wilson disease, IgA glomerulonephritis and vascular purpura: an incidental association?].

BACKGROUND: IgA nephropathy may occur in adults with alcoholic cirrhosis. It has also been reported in children with alpha-1-antitrypsin deficiency. A case of IgA nephropathy associated with cirrhosis due to Wilson's disease is reported. CASE REPORT: A 10 year-old girl, was admitted for cirrhosis. She had suffered from ascitis and hematuria since the age of 6 years and vascular purpura since the age of 9 yr 6 mo. At admission, she had atrophic liver cirrhosis, ascitis splenomegaly and petechiae on her legs. There was microcytic anemia due to iron deficiency. The Coombs test was positive. There were hypoalbuminemia (2 g/dl) and polyclonal hyperglobulinemia (IgA 750 mg/dl, IgG 1670 mg/dl and IgM 250 mg/dl). Her serum concentrations of complement factors were normal and no immune complexes were detected in serum. She also showed biological changes due to kidney failure, hematuria and proteinuria. A liver biopsy showed micronodular cirrhosis with numerous plasma cells containing IgA. The search for an etiology showed ceruloplasmin levels of 5 mg/dl, elevated urinary copper excretion (> 150 micrograms/day) and above normal liver copper (255 micrograms/g dry weight); Kayser-Fleischer ring was also seen. The renal biopsy showed membranoproliferative glomerulonephritis, and immunofluorescent microscopy revealed C3 and IgA in the mesangial and subendothelial regions. The patient was given spironolactone and furosemide followed by triethylenetetramine dihydrochloride. CONCLUSIONS: The IgA nephropathy, vascular purpura and elevated serum IgA levels could be due to the liver changes. If so, they should be improved by a liver transplant, although our patient would be a better candidate for combined liver and kidney transplantation.

Child↗