PubMed Health⌕ Search

Biomedical subjects

G Husby

Publications and source records attributed to G Husby.

At least 19 recordsLinked to original sources
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↗
PubMed1977

Direct immunochemical detection of prostaglandin-E and cyclic nucleotides in human malignant tumors.

Immunofluorescent localization of prostaglandin-E (PGE), cyclic AMP (CAMP), and cyclic GMP (cGMP) was studied in tumor tissues from 40 patients with a variety of solid tumors. Representative normal tissues served as controls. Rabbit antisera specific for PGE or the cyclic nucleotides were used, and the reactions observed were correlated with the degree and type of lymphocytic reaction at the tumor margins. Strong PGE immunofluorescence was detected in tumor cells in 27 of 42 malignancies; by contrast nine of 13 normal tissues showed weak PGE reactions, cAMP was detected in 30 of the 42 malignancies; cGMP was noted in only seven of the 42 malignant tissues and in none of the normal tissues studied. The most common malignant tumor profile (17/42) was that of positive PGE and cAMP and negative cGMP staining. Tumors showing strong staining with anti-PGE or cAMP demonstrated a distinct trend towards heavier lymphocytic infiltration with a predominance of T cells at their margins, although this association did not reach statistical significance in the present material.

B-Lymphocytes↗
PubMed1977

Immunohistochemical localization of prostaglandin E in rheumatoid synovial tissues.

Synovial tissues removed at synovectomy from patients with active rheumatoid arthritis (RA) or osteoarthritis (OA) were examined for prostaglandin E (PGE) by immunohistochemical techniques using rabbit antisera specific for PGE. Marked increments of PGE were noted in RA synovia in comparison to OA, with staining concentrated in synovial lining cells, interstitial inflammatory cells, and endothelial cells of blood vessels. A correlation was noted between the degree of synovial lymphocytic infiltrate and the intensity of PGE staining. These studies provide initial cellular localization of PGE in such tissues.

Arthritis, Rheumatoid↗
PubMed1977

Identification and characterization of different amyloid fibril proteins in tissue sections.

Antisera specific for 4 different classes of amyloid fibril proteins, amyloid protein AA and the immunoglobulin light-chain amyloid proteins AlambdaI, AlambdaIV, and AlambdaV, were used to identify these proteins directly in tissue sections from 25 patients with amyloidosis. The specificity of these reactions was established by blocking experiments with purified amyloid fibril proteins and Bence Jones proteins of known variable subgroups. Protein AA was detected in 17 patients, including all 13 with secondary amyloidosis, 2 with primary amyloidosis and 2 with Waldenström's macroglobulinemia. Immunoglobulin light-chain proteins AlambdaI, AlambdaIV, and AlambdaV were in 3, 1, and 2 patients, respectively, all of whom had primary or myeloma/macroglobulinemia-associated amyloidosis. Antiserum specific for the amyloid-related serum protein SAA reacted with the same tissues as anti-AA and had the same pattern of staining in tissue sections.

Amyloid↗
PubMed1977

Identification in human placentae of antigenic activity related to the amyloid serum protein SAA.

Antigenic activity related to the amyloid serum protein SAA was observed in indirect immunofluorescence studies on human placental tissue. Positive staining with anti-SAA antisera was localized to the cytoplasm of cells scattered within the mesenchymal stroma, thought to be fibroblasts, and to foetal stem vessel endothelium and some individual fibrillar structures in villous stroma and perivascular tissue. This immunofluorescent staining was specifically inhibited by protein SAA. In contrast, no immunofluorescent staining was achieved using antisera to the amyloid protein AA. Absorption and immunodiffusion studies have further suggested that anti-SAA antisera may recognize in human placentae only a very limited number of the antigenic determinants present in protein SAA but not in the smaller protein AA. The results support previous observations that protein SAA-like antigenic material can be found in normal human tissue.

Amyloid↗