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Biomedical subjects

A O Grubb

Publications and source records attributed to A O Grubb.

26 records · Page 2Linked to original sources
PubMed1977

Expression of protein HC on the plasma membrane of different human cell types.

The surface expression of a recently described plasma glycoprotein called human complex-forming glycoprotein, hetergeneous in charge (protein HC) on a number of different human cell types was investigated. By means of direct and indirect immunofluorescence, protein HC was shown to be associated with the surface of virtually all cells of the investigated normal cell types including erythrocytes, peripheral blood B and T lymphocytes, and the human fibroblast lines HE 81, HE 31, and WI 38. When transformed and malignant cell populations were studied, it was found that some populations (e.g., the T cell line Molt-4) carried protein HC on the surfaces of very few cells, whereas other cell populations (e.g., chronic lymphocytic leukemia lymphocytes) carried the protein on most cells. Malignant cell populations with intermediary percentages of protein HC-positive cells were also found. Protein HC on the cell surface of normal peripheral blood lymphocytes could be redistributed by incubation of the cells with anti-protein HC-antiserum at 37 degrees C, and this reaction could be inhibited by sodium azide.

Animals↗
PubMed1976

A complex-forming glycoprotein heterogeneous in charge and present in human plasma, urine, and cerebrospinal fluid.

A glycoprotein from the urine of one healthy individual was purified by ultrafiltration, ion-exchange chromatography, gel chromatography and immunosorption. The protein contained only one polypeptide chain with an approximate molecular weight of 31 000 and was associated with a brown colour which did not disappear even after total reduction and alkylation of the protein followed by dialysis in 6 M guanidine hydrochloride. The protein appeared homogeneous on sodium dodecyl sulphate-polyacrylamide electrophoresis and gel chromatography. It had only one N-terminal amino acid sequence, Gly-Pro, and gave only one precipitate with a polyvalent antiserum but was found to be very heterorgeneous on agarose gel electrophoresis and on isoelectric focusing. Desialylation of the protein failed to alter this heterogeneity. An electroimmunoassay system was designed to measure the amount of the protein in normal human plasma, urine, and cerebrospinal fluid where the mean concentrations were found to be about 100, 10 and 0.3 mg/l, respectively. The protein was found to occur in normal plasma and urine as free monomers and dimers and as complexes with IgA and albumin.

Amino Acid Sequence↗
PubMed1976

Immunofluorescent demonstration of the presence of protein HC on the surface of human lymphocytes.

Indirect immunofluorescence was used to demonstrate the presence of protein HC on the surface of a large percentage of normal human peripheral blood lymphocytes. Protein HC is a recently described charge heterogeneous, complex-forming glycoprotein normally present in human plasma, urine and cerebrospinal fluid. The synthesis of protein HC by lymphocytes was indicated by the removal of the glycoprotein from the cell surfaces on trypsinization of the cells followed by the reappearance of the protein on continued cultivation of the cells.

Cell Membrane↗
PubMed1975

Immunochemical evidence for a common variable region in three immunoglobulin classes in the same individual.

One IgG1(kappa), one IgM(kappa), and one IgA1(kappa) monoclonal (M)-component were purified from one human serum. Rabbit antisera were raised against the IgG and IgM M-components and were absorbed until specific for idiotypic determinants on these molecules. All three M-components gave reactions of immunological identity when tested by double radial immunodiffusion with either of the two idiotype-specific antisera. Both heavy and light chains were isolated from each of the three M-components and all preparations inhibited formation of idiotypic precipitates. None of these preparations formed precipitates with idiotype-specific antisera alone. When heavy or light chains of one M-component were hybridized with light or heavy chains from the other M-components the resultant molecules precipitated with anti-idiotypic serum. Hybrids with chains from polyclonal IgG were not precipitable with such antiserum. These results indicate that the variable region of the heavy chains of these M-components of three different immunoglobulin classes are closely similar, if not identical.

Aged↗
PubMedDate not supplied

Immunohistochemical characterization of the amyloid deposits and quantitation of pertinent cerebrospinal fluid proteins in hereditary cerebral hemorrhage with amyloidosis.

Cystatin C, a protein inhibitor of lysosomal cysteine proteinases, was demonstrated by immunohistochemical techniques to be present in the birefringent amyloid deposits of the small arteries in the cerebrum, cerebellum, and leptomeninges of 10 Icelandic individuals with hereditary cerebral hemorrhage with amyloidosis. Specimens from other organs were investigated in one of the patients, and amyloid angiopathy characterized by an immunoreactivity of cystatin C was found in a submandibular lymph node. No immunoreactivity of amyloid fibril protein AA, kappa or lambda immunoglobulin light chain, or prealbumin was observed. Significantly low cerebrospinal fluid concentrations of cystatin C were found in all 9 investigated individuals with hereditary cerebral hemorrhage with amyloidosis. The concentrations of beta 2-microglobulin, albumin, and IgG in the cerebrospinal fluid were within normal limits. Isoelectric focusing showed that cystatin C from the cerebrospinal fluid of 9 patients with hereditary cerebral hemorrhage with amyloidosis had an isoelectric point identical to that of normal individuals. This investigation demonstrates that hereditary cerebral hemorrhage with amyloidosis may be diagnosed by two laboratory methods: immunohistochemical investigation of cystatin C in brain tissue specimens and quantitation of cystatin C in cerebrospinal fluid.

Adult↗