Search PubMed⌕ Search

Biomedical subjects

G Husby

Publications and source records attributed to G Husby.

At least 217 records · Page 12Linked to original sources
PubMed1983

Comparative studies of the high molecular weight amyloid fibril proteins and similar components from normal tissues.

Analysis of purified amyloid fibrils by gel filtration, polyacrylamide gel electrophoresis in SDS and 8 M urea, and immunodiffusion and immunoelectrophoresis showed that, in addition to the specific amyloid proteins AA and AL, the amyloid preparations all contain a high molecular weight complex. The latter protein complex contains fibronectin, a component which reacts with a non-AA specificity of an antiserum to degraded AA amyloid fibrils (termed the 'B' specificity), and a high molecular weight component excluded by a Sepharose 2BCL column. Similar components were found in aqueous extracts of normal tissues prepared by an identical procedure, and these form aggregates of different size in non-dissociating conditions. It is suggested that amyloid fibrils are complexes of a variety of macromolecules in addition to the specific proteins AA and AL.

Amyloid↗
PubMed1983

Studies on humoral immunity in pregnancy: immunoglobulins, alloantibodies and autoantibodies in healthy pregnant women and in pregnant women with rheumatoid disease.

Levels of immunoglobulins, alloantibodies and the presence of autoantibodies were prospectively studied during and after pregnancy in healthy women and in women suffering from rheumatoid arthritis (RA) and ankylosing spondylitis (AS). A decrease of IgG and IgA during pregnancy was found in all women while levels of IgM and alloantibodies remained stable. Multiparous women had higher levels of IgG during pregnancy when compared to primigravidae. No difference in the frequency of rheumatoid factor (RF) or antinuclear antibodies (ANA) was found when healthy pregnant women were compared to healthy non pregnant controls. None of the RF negative patients conversed to seropositivity during or after pregnancy. Decrease of ANA was correlated to remission of disease activity in the patients with RA.

ABO Blood-Group System↗
PubMed1983

Stimulation of murine macrophage cathepsin B by serum from patients with rheumatoid arthritis: an indicator of disease activity.

Cultures of non-elicited mouse peritoneal macrophages were used as a test system to study the effect of sera from patients with rheumatoid arthritis (RA) on intra-cellular cathepsin B activity of macrophages. Sequential sera obtained during and after pregnancy from six RA patients, and sera from six actively ill, non-pregnant RA patients were compared to six healthy female controls and 3rd trimester healthy women. Sera from actively ill RA patients (both pregnant and non-pregnant) caused macrophage cathepsin B levels significantly above normal controls, while intra-cellular activities of beta-glucuronidase and N-acetyl-glucosaminidase did not differ from the controls. A significant correlation between activity of RA and intracellular cathepsin B was found in pregnant patients. It is suggested that a factor (or factors) present in serum from patients with active RA causes a rise of intracellular cathepsin B in macrophages.

Acetylglucosaminidase↗
PubMed1982

Ankylosing spondylitis and motherhood.

The influence of pregnancy on the course of ankylosing spondylitis (AS) was evaluated for 87 pregnancies of 50 patients. Remission of AS was recorded in 18 pregnancies, exacerbation in 21, and no change in 48. A short flareup of AS was noticed postpartum in 45% of the patients. Postpartum anterior uveitis occurred frequently (20%). The first symptoms of AS were often (20%) related to pregnancy. AS had no harmful effect on pregnancy, the fetus, or the newborn. Twelve percent of the offspring who were 18 years old or older have developed definite ankylosing spondylitis.

Adult↗
PubMed1982

Plasma exchange in the treatment of severe, childhood onset systemic lupus erythematosus.

Plasma exchange was used in the treatment of a 10-year-old girl with acute systemic lupus erythematosus. The patient was in a life-threatening condition, and treatment with high dose corticosteroids did not control the disease. The patient's condition improved dramatically during the second day of plasma exchange therapy. It also appeared to have a long-lasting effect in combination with immunosuppressive drugs. This is, to our knowledge, the first report of plasma exchange in a child with systemic lupus erythematosus.

Child↗
PubMed1982

Immunohistochemical characterization of hepatic tissue lymphocyte subpopulations in liver disease.

Liver biopsies from 27 patients were studied by the indirect immunofluorescence and immunoperoxidase technique for relative distribution of B cells and T-cell subpopulations. T-cell subsets were defined for OKT4(+) (helper/inducer) and OKT8(+) (suppressor/cytotoxic) cells by using mouse hybridoma monoclonal antibodies. Patients with chronic active hepatitis and those with primary biliary cirrhosis showed marked relative increments in suppressor/cytotoxic OKT8(+) lymphocytes within hepatic lymphocytic infiltrates. Other patients with acute hepatitis or those with only reactive changes also showed a relative increment in OKT8(+) T lymphocytes within hepatic biopsy material. These findings suggest that tissue lymphocytic subpopulation increments in suppressor/cytotoxic T-cell subpopulations are commonly associated with hepatic lymphocytic infiltrates and may be related to disorders of immune regulation or expression in some of these disorders.

Adolescent↗
PubMed1982

Amyloid A in systemic amyloidosis associated with cancer.

Amyloid fibrils from two cases of cancer-associated, systemic amyloidosis with renal cell carcinoma and mesothelioma as the respective underlying disorders were studied. The immunochemical studies suggested strongly that amyloid A comprised a principal fibril component in both cases of cancer-associated amyloidosis. This was definitively proven by amino acid sequence analyses, which revealed structural homology between a purified subcomponent of the amyloid fibrils from both of the two cases of cancer-associated amyloidosis and previously sequenced amyloid A proteins. The chemical composition of the amyloid fibrils from systemic amyloidosis associated with cancer thus corresponded to that seen in amyloidosis reactive to inflammatory diseases and Hodgkin's disease. Amyloid proteins of immunoglobulin light chain type, which are found associated with myelomatosis, macroglobulinemia, and idiopathic (primary) amyloidosis, were not found in the two amyloid preparations. Renal cell carcinoma appears to be an effective stimulator of amyloid formation, while only one case of amyloidosis associated with mesothelioma has been reported previously.

Adolescent↗
PubMed1982

Characterization of amyloid related protein SAA complexed with serum lipoproteins (apoSAA).

The amyloid related protein SAA was isolated from the serum lipoproteins of three patients with connective tissue disease, one of them having amyloidosis, and from a pool of normal control sera. The bulk of SAA (apoSAA) was complexed to high density lipoprotein (HDL), but significant amounts of apoSAA were also detected in the other lipoprotein fractions. Electrofocusing revealed five-six subspecies of SAA which were distributed in similar proportions in HDL and LDL. Three of these SAA subspecies made up almost all of the apoSAA present in HDL and LDL in the sera from the patients as well as in the control. A small portion of SAA not complexed to lipoproteins was isolated corresponding to a molecular weight higher than 200,000. No particular 'amyloid prone' SAA was found in serum from the patient with amyloidosis.

Amino Acids↗
PubMed1982

Monoclonal hybridoma antibodies to human amyloid related protein SAA.

Problems concerning isolation and characterization of the amyloid related serum protein SAA in a pure form prompted us to make monoclonal antibodies to the protein. Protein SAA isolated by gel filtration under dissociating conditions was used for immunization of BALB/c mice, and spleen cells from a mouse producing high titred antiserum to SAA were fused with cells from the mouse plasmacytoma line P3U1. Antibody specificity to various preparations of protein SAA was tested using an indirect enzyme-linked immunosorbent assay. Monoclonal antibodies with specificity for SAA were obtained in addition to antibodies which reacted with both SAA and the related amyloid protein AA. Antibodies specific for one of the apoC proteins of the lipoprotein fraction were also produced showing that the SAA preparation used for immunization was contaminated with apoC proteins.

Amyloid↗
PubMed1981

The complete amino acid sequence of a prototype immunoglobulin-lambda light-chain-type amyloid-fibril protein AR.

The amino acid sequence of an amyloid-fibril protein of immunoglobulin light-chain type (AL) was elucidated. The sequence determination involved digesting the protein with trypsin, thermolysin and pepsin. The protein was found to consist of 154 amino acid residues and is thus missing about half of the constant region of a light chain. A certain heterogeneity in the length of the polypeptide was observed in the C-terminal region. The amino acid sequence from CDR (complementary-determining region) 1 and FR (framework region) 3 indicated an oligoclonal origin of the protein. By comparing the primary structure of protein AR with other lambda- and even kappa-chains, it was revealed that protein AR had an insertion of two residues of aspartic acid, namely residues 68 and 69, which has not been reported previously in light chains. The overall sequence homology in the variable region showed that protein AR is more similar to V lambda V than to the other subgroups [Kabat, Wu & Bilofsky (1979) Variable regions of Immunoglobulin Chains, Medical Computer Systems, Bolt, Beranek and Newman, Cambridge, MA].

Amino Acid Sequence↗
PubMed1981

Characterization of renal tissue lymphocytes in patients with interstitial nephritis.

Five patients with interstitial nephritis who presented with a variety of clinical profiles were studied with particular emphasis on documentation of the cellular types of potentially immunocompetent lymphocytes and mononuclear cells present within interstitial renal infiltrates. Immunohistologic studies coupled with conventional light and electron microscopic observations indicated that most mononuclear cells making up renal interstitial infiltrates were T cells. Some chronic inflammatory cell foci within renal interstitium were characterized by clusters of Ia antigen-positive T cells considered to be markers for activated lymphocytes. B cells were present in very small proportions (5 percent or less). The profile of immunocompetent cells present in lesions of interstitial nephritis suggests a major role for cell-mediated immunity in this disorder. Increase in tissue lymphocytes of the T gamma subclass with receptors for the Fc portion of immunoglobulin G (IgG) also suggests local activation of intrinsic suppressor cell mechanisms.

Adolescent↗
PubMed1981

Further structural and antigenic studies of light-chain amyloid proteins.

The major subunit protein of amyloid fibrils (758) isolated from a patient with systemic amyloidosis and studied by N-terminal amino acid sequence analysis was found to be almost identical to the sequence of a V lambda IV Bence-Jones protein and a previously described A lambda IV amyloid protein. The two A lambda IV amyloid proteins showed strong antigenic cross-reaction, appearing as antigenic identity in double immunodiffusion tests using anti-A lambda IV antiserum raised against one or the other of the two proteins. In addition, another new A lambda V amyloid fibril protein (R.S.) showed strong amino acid sequence homology and antigenic identity in double immunodiffusions with the prototype of the A lambda V subgroup (the AR protein). Finally, 20 primary or myeloma-associated amyloid proteins were characterized using antisera against the AA and several Ig light-chain-derived amyloid proteins.

Amino Acid Sequence↗
PubMed1981

Characterization of an amyloid fibril protein from localized amyloidosis of the skin as lambda immunoglobulin light chains of variable subgroup I (A lambda I).

Amyloid fibrils obtained from a case (Hud) of localized, tumorous amyloidosis of the skin were investigated by immunological and biochemical methods including amino acid sequence studies. Evidence was obtained that a lambda immunoglobulin light chain protein, A lambda I, and differently sized N terminal fragments (mol. wt 14,000 and 10,000) of the same protein comprised a major component of the fibrils. The chemical nature of this protein suggested that this case of cutaneous amyloidosis belonged to the idiopathic form of amyloidosis, probably as a special type of systemic, idiopathic amyloid disease.

Amino Acid Sequence↗
PubMed1981

Characterization of human amyloid-related protein SAA as a polymorphic protein: association with albumin and prealbumin in serum.

Human amyloid-related protein SAA has been prepared and purified by gel filtration, ion-exchange and affinity chromatography techniques. It was shown that SAA, even after extensive purification, is an electrophoretically heterogeneous protein. In addition, prealbumin and fragments of albumin were detected in the SAA preparation. Most of the SAA molecules and the fragments of albumin were present in a free form, but some SAA was also found to be complexed with albumin fragments.

Aged↗