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Biomedical subjects

G Husby

Publications and source records attributed to G Husby.

At least 235 records · Page 13Linked to original sources
PubMed1980

A chemical classification of amyloid. Correlation with different clinical types of amyloidosis.

Results of recent research have made it possible to classify amyloidosis by means of the chemical and antigenic characteristics of the amyloid fibrils. The chemical classification of amyloid correlates quite well with the various clinical types of amyloidosis. Monoclonal immunoglobulins constitute a major part of primary amyloid fibrils, while amyloid protein AA plays a similar role in secondary amyloidosis. In addition, structural properties of amyloid fibril proteins derived from medullary carcinoma of the thyroid and from senile cardiac amyloidosis respectively, have been shown to be unique for these clinical types of localized amyloidosis. A protein identical or similar to prealbumin appears to constitute an amyloid fibril subunit in familial amyloidotic polyneuropathy. However, the mechanisms by which the various amyloid precursor proteins are converted to fibrils and deposited in the tissues are still not clear.

Amyloid↗
PubMed1980

An unusually large (83 amino acid residues) amyloid fibril protein AA from a patient with Waldenström's macroglobulinaemia and amyloidosis.

The amino acid sequence studies of a human amyloid fibril protein AA derived from a patient with Waldenström's macroglobulinaemia revealed 83 residues. This protein AA was larger than but otherwise very similar to other human AA proteins studied by complete sequencing. Two amino acids were found both in position 52 (Val/Ala) and in position 53 (Trp/Arg), strongly suggesting a polymorphism of AA proteins. Immunologic studies showed the antigenic determinant(s) reacting with antiprotein AA to be located between positions 25 and 76 of the third cyanogen bromide cleavage fragment of the protein.

Amino Acid Sequence↗
PubMed1980

The primary structure of amyloid fibril protein AA in endotoxin-induced amyloidosis of the mink.

Two AA proteins were isolated from the same amyloid fibril preparation from the liver of a mink, in which amyloidosis had been induced by injections with endotoxin. The two proteins were of different size, one containing 53 amino acid residues and the other 64 residues. The amino acid sequence was otherwise found to be identical. Both proteins revealed pyrrolidone carboxylic acid as the N-terminal amino acid. Sequence homologies with protein AA from other species were very striking. However, no antigenic cross-reaction was seen between mink protein AA and antisera to protein AA from human, mouse or rabbit sources.

Amino Acid Sequence↗
PubMed1980

Immunocytological studies of lymph nodes in rheumatoid arthritis and malignant lymphoma.

Lymph nodes obtained from 9 patients with active rheumatoid arthritis were stained by immunological techniques permitting identification of B and T cell areas within the nodes. The lymph nodes were also compared with those obtained from patients with lymphoma. The rheumatoid lymph nodes showed prominent B cell staining in the follicular centres by the EAC and fluoresceinated immunoglobulin techniques. Interfollicular areas were intensely stained with anti-theta globulin. In contrast, lymphoma nodes stained less intensely with fluoresceinated immunoglobulins but stained like benign nodes with EAC. The difference in staining may reflect the degree of disorganisation of the neoplastic follicle and/or the different sensitivity of these 2 methods in the detection of B cells. The differences in staining are helpful in distinguishing the benign changes associated with chronic inflammation from neoplastic B cell proliferative changes seen in lymph nodes.

Arthritis, Rheumatoid↗
PubMed1980

T-lymphocyte subpopulations in peripheral blood and tissues of cancer patients.

Patients with cancer often show impaired immune functions; however, the basis of this suppression is still not understood. In several experimental systems, human T-cells with receptors for Fc of immunoglobulin G may function as suppressors, and those with receptors for Fc of immunoglobulin M may function as helpers. Peripheral blood as well as tumor tissue infiltrates were examined for proportions and numbers of T gamma, T mu, or Ia-positive T-cells. Forty-five untreated patients with solid tumors and 24 patients with lymphomas were studied. An increase in the percentage of peripheral blood T gamma cells (p < 0.001) and a decrease in T mu cells (p < 0.0005) were recorded in all tumor patients when compared with 30 normal controls. Percentages and absolute numbers of peripheral blood Ia-positive T-cells were decreased (p < 0.001 and < 0.00001) in solid-tumor patients; by contrast, the proportion of peripheral blood Ia-positive T-cells was elevated (p < 0.005) in lymphoma subjects. Studies of cancer tissues from 46 untreated patients using immunofluorescence and mouse hybridoma antibody specific for T-cells showed that tumor lymphocytic infiltrates were composed mainly of T-cells. Double staining with fluorescein-conjugated specific anti-T gamma and Ia-positive T-cells within solid-tumor lymphoid infiltrates. A comparison of peripheral blood and tumor lymphocyte T-cell profiles revealed that, in some patients, low proportions of Ia-positive T-cells in blood were paralleled by a high percentage of such cells in tumor lymphoid infiltrates.

Antigens, Surface↗
PubMed1979

The amyloid P-component (protein AP): an integral part of the amyloid substance?

The P-component of amyloid (protein AP) appears to be present in all types of amyloid substance regardless of the clinical category of amyloidosis or the chemical class of the amyloid fibril. The role of protein AP in the formation of amyloid substance has not been established. In a patient with primary amyloidosis, significant amounts of protein AP were found closely associated with the amyloid fibril proteins and was released from the latter only after dissociation and reduction of the amyloid fibril preparation. EDTA seemed to be very effective in releasing protein AP, and it is thought that the close association between the amyloid fibrils and protein AP is calcium-dependent. The very close association between the amyloid fibrils and protein AP suggests that the latter is an integral part of the amyloid substance.

Amino Acid Sequence↗
PubMed1979

Immunologic and gastrointestinal abnormalities in dermatitis herpetiformis.

Eighty patients with untreated dermatitis herpetiformis (DH) were studied. The final diagnosis was made after completion of immunofluorescence (IF) studies of the skin, iodine provocation tests and gastrointestinal investigations. IgA deposits in the skin and the HLA-DRw3 B-cell alloantigen can be demonstrated in nearly all cases of DH. Positive iodine provocation test and gastrointestinal abnormalities are present in about 78% of the cases. For diagnostic purposes tissue typing and intestinal biopsy is of value in addition to IF studies of the skin.

Adolescent↗
PubMed1979

Occurrence of immunoglobulins and complement in the skin of patients undergoing topical treatment of mycosis fungoides.

Deposits of immunoglobulins (IgG, IgA and IgM) and complement were occasionally found in lesional skin of mycosis fungoides patients. However, after complete remission of the skin lesions, deposits of immunoglobulins and complement were found, corresponding to previous infiltrates or tumours, in about half of the patients. These deposits appeared as globular bodies in the upper part of the dermis closely connected with the basement membrane.

Complement System Proteins↗
PubMed1978

Probable endometrial carcinoma of the prostate, crossed renal ectopia and dermatomyositis in a 32-year-old man.

An unusual type of prostatic carcinoma associated with crossed renal ectopia and dermatomyositis is reported in a young man. Infiltration by an epithelial tumor filled the enlarged prostate with soft papillary masses. Cystoprostatectomy and removal of a single large pelvic lymph node metastasis were done. Histologically, the tumor resembled endometrial carcinoma and may have arisen from paramesonephric tissue in the prostate. Large amounts of immunoglobulins were found in the tumor tissue. The patient has survived for more than 5 years, although a slow growing urethral recurrence has been noted.

Adenocarcinoma↗
PubMed1978

Human lymphocyte subpopulations defined by double surface markers.

Subpopulations of human peripheral blood lymphocytes were studied with single and double surface marker assays. The markers employed were as follows: (1) Fc receptor, using EA, mean 21.4%; (2) C3 receptor, using Zy-C3, mean 14.6%; (3) Slg, using a fluoresceinated F(ab')2 anti-F(ab')2 mean 8.9%; and (4) T lymphocytes forming E-rosette, mean 69.3%. The proportions of lymphocytes with any given surface marker which also have another surface marker were as follows: (1) EA + Slg/EA = 0.14, (2) EA + Zy-C3/EA = 0.22, (3) Slg + Zy-C3/Slg = 0.83, (4) Zy-C3 + E-rosette/E-rosette = 0.02, (5) EA + E-rosette/E-rosette = 0.06, (6) Slg + E-rosette/E-rosette = 0. The relative percentages of cells which were Slg+EA-, EA+Slg-, and EA+Zy-C3- were confirmed by EA rosette depletion via gradient centrifugation. On the basis of these observations, calculations were made of the theoretical numbers of lymphocytes with triple markers (EA+Slg+Zy-C3+ = 3.0%) and lymphocytes with only a single surface marker (EA+ only = 12.5%, Zy-C3+ only = 1.5%, Slg+ only = 1.5%). Finally a schematic representation of the multiple subpopulations of lymphocytes with various surface markers is presented.

B-Lymphocytes↗
PubMed1978

Senile cardiac amyloid: demonstration of a unique fibril protein in tissue sections.

Antisera were raised against degrading amyloid fibrils isolated from the heart of a patient with senile cardiac amyloidosis (SCA), and from a medullary carcinoma of the thyroid (MCT). The antisera were absorbed and used in indirect immunofluorescence to identify an amyloid fibril protein (ASCA) in heart tissue from patients with senile cardiac amyloidosis and to identify the amyloid fibril protein (AMCT) found in association with medullary carcinomas of the thyroid. Absorbed anti-ASCA antiserum did not react with normal tissue such as heart, liver, spleen, and striated muscle, or with amyloid tissue known to contain amyloid fibril proteins AA, AlambdaI, AlambdaIV, AlambdaV, AMCT or with pancreatic tissue containing islet amyloid deposits. The reactions with senile amyloid he,rt tissue could be blocked completely by degraded amyloid fibrils extracted from senile amyloid heart tissue or by amyloid fibril protein ASCA isolated from such fibrils. The anti-AMCT antiserum showed a similar specific reaction restricted to amyloid associated with MCT. In addition, antisera specific for amyloid fibril proteins AA, AlambdaI, AlambdaIV, and AlambdaV failed to react with senile cardiac amyloid, pancreatic islet amyloid, or medullary thyroid amyloid.

Aged↗