concanavalin-a and Cushing-Syndrome

concanavalin-a has been researched along with Cushing-Syndrome* in 2 studies

Other Studies

2 other study(ies) available for concanavalin-a and Cushing-Syndrome

ArticleYear
Lectin histochemistry in adrenocortical hyperplasia and neoplasms with emphasis on carcinoma.
    Archives of pathology & laboratory medicine, 1989, Volume: 113, Issue:1

    Lectin binding analysis of Con A, SBA, PNA, WGA, HPA, RCA-I, DBA, and UEA-I was performed in two cases of normal human adrenal gland, four cases of adrenocortical hyperplasia, six cases of adrenocortical adenoma, and seven cases of adrenocortical carcinoma to examine the differences of lectin binding properties. No lectins were bound specifically to adrenocortical cells. Binding of RCA-I was observed in some carcinoma cells focally but not in benign counterparts. With WGA and Con A, the cytoplasmic binding became apparent in the cells manifesting hypercorticism. In adrenocortical carcinoma, various WGA and Con A binding patterns were intermingled, but no specific patterns were identified. The focal nature of RCA-I binding, and no specific WGA and Con A binding properties in carcinoma, suggest that diagnosis of malignant neoplasm must still largely rely on clinical, hormonal, and structural criteria in adrenocortical neoplasms.

    Topics: Adenoma; Adolescent; Adrenal Cortex; Adrenal Cortex Neoplasms; Adult; Carcinoma; Child; Child, Preschool; Concanavalin A; Cushing Syndrome; Female; Histocytochemistry; Humans; Hyperplasia; Lectins; Male; Middle Aged; Plant Lectins; Wheat Germ Agglutinins

1989
Characterization of alkaline phosphatase in canine serum.
    Enzyme, 1987, Volume: 37, Issue:3

    On the basis of carbohydrate structure, normal dog serum contains three basic types of serum alkaline phosphatase (SAP) corresponding to (1) highly branched complex (non-concanavalin A-binding), (2) complex, or (3) high-mannose (both concanavalin A-binding) oligosaccharide structures. Subsequent binding experiments with monoclonal antibody to intestinal alkaline phosphatase (AP) and bromotetramisole inhibition studies clearly indicated the presence of intestinal-like SAP. Concanavalin A (Con-A) binding characteristics suggested the presence of a bone-like SAP. Con-A-binding and isoelectric focusing results revealed the presence of two (type Ib and IIb) major SAP isoenzymes thought to be of hepatic origin. SAP isoenzymes appear to be modified when compared to tissue AP, particularly in regard to molecular size and, in some cases, carbohydrate structure.

    Topics: Alkaline Phosphatase; Animals; Bone and Bones; Carbohydrates; Concanavalin A; Cushing Syndrome; Dogs; Intestines; Isoenzymes; Liver; Male

1987