Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: UNIPROT:Q9UE34 (fibrinogen)
30,244 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Actinomyces pyogenes, an important pathogen of the bovine udder, was mainly characterized by production of the enzymes protease and neuraminidase. Both enzymes could be isolated and further analyzed. In addition A. pyogenes demonstrated lectin-like surface structures which caused hemagglutination reactions of neuraminidase treated erythrocytes. Further surface antigens of A. pyogenes which characteristically cross reacted with antisera against group polysaccharide antigens of streptococci of serological group G allowed an additional serological identification of this species. A. pyogenes further demonstrated binding properties for the plasma proteins alpha 2-macroglobulin, haptoglobin and fibrinogen and bacteriocin-like activities which caused growth inhibition of micrococci and staphylococci.
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PMID:[The possible pathogenic factors of Actinomyces pyogenes. A review]. 218 3

In a study of 25 giant cell arteritis patients, whose diagnoses were made by temporal artery biopsy, the authors compared the evolution of the erythrocyte sedimentation rate (ESR) with those of the acute phase proteins (APP): fibrinogen (F), C reactive protein (CRP), orosomucoid (O), haptoglobin (H) and alpha 2-globulins (alpha 2-G), before, during and after corticotherapy; 165 laboratory analyses were made. Prior to treatment, ESR was increased in 96% of the patients, O and H in 100%, F and CRP in 96% and alpha 2-G in 92%. CRP showed the greatest mean increase (21x). Statistically significant positive correlations were found between ESR and alpha 2-G, F, CRP and O. No significant relationship was observed between APP and the occurrence of ophthalmological complications or the length of treatment. The CRP level returned to normal within the first week of steroid therapy for 76% of the patients, before ESR, F and O. During the withdrawal phase of corticotherapy, an ESR greater than 30 mm almost always corresponded to an inflammatory syndrome and an ESR of less than 15 mm to its absence (kappa coefficient = 0.64, p less than 0.001); however, an ESR between 15 and 30 mm did not enable us to draw a conclusion as to the absence or presence of such a syndrome. After terminating steroid therapy, the relationship between ESR and an inflammatory syndrome was weaker (kappa coefficient = 0.57, p less than 0.02).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Inflammation proteins in Horton's disease. Prospective study of 25 patients]. 224 Sep 43

Two group G streptococcal cultures (G 10187, G 11122) with surface antigen T4 possess surface receptors for human haptoglobin (Hp). G 10187 additionally interacted with immunoglobulin G and albumin, G 11122 with fibrinogen and fibronectin. Binding of 125I-Hp 2-1 was time-dependent, saturable, reversible in the presence of unlabelled Hp and could be inhibited by unlabelled human-Hp 2-1, -Hp 2-2, -Hp 1-1, Hp-hemoglobin complexes and by Hp preparations from pigs, horses and rabbits. The Hp binding sites could be destroyed by heat treatment (95 degrees C) and by proteolytic treatment of the bacteria. Hp binding sites were solubilized from group G streptococcal surface by heat treatment of the bacteria at acid pH and subsequently isolated by affinity chromatography on Hp 2-1 sepharose. SDS-PAGE and Western blotting of the Hp binding proteins revealed numerous protein bands with 125I-Hp 2-1 binding activity. Specific antibodies against G streptococcal binding proteins prepared in chickens inhibited binding of 125I-Hp to group G and group A streptococci, but not to Actinomyces pyogenes.
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PMID:Characterization of haptoglobin-binding properties of streptococci of serological group G. 226 Oct 66

All 25 cultures of Actinomyces pyogenes tested in the present study bound 125I-labelled human alpha 2-macroglobulin with a mean binding of 65.6%. Thirteen cultures also bound 125I-labelled human haptoglobin with a mean of 51.5%. None interacted with fibrinogen, fibronectin, immunoglobulin G, or albumin. Twenty-eight cultures representing other species of actinomycetaceae did not show any interaction with alpha 2-macroglobulin, haptoglobin, and other plasma proteins tested. The binding of alpha 2-macroglobulin and haptoglobin to A. pyogenes was saturable and could be completely inhibited by the respective unlabelled plasma proteins. The binding of alpha 2-macroglobulin could not be inhibited by unlabelled haptoglobin. On the other hand, alpha 2-macroglobulin blocked the binding of haptoglobin, possibly by steric hindrance. Treatment of the bacteria with trypsin reduced their binding activities for alpha 2-macroglobulin and haptoglobin indicating the protein nature of the binding sites. Exposure to heat (1 h, 80 degrees C) significantly diminished the binding activity for haptoglobin, but not that for alpha 2-macroglobulin. The binding of alpha 2-macroglobulin and haptoglobin could be an important feature in the classification of A. pyogenes among the members of actinomycetaceae.
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PMID:Binding of alpha 2-macroglobulin and haptoglobin to Actinomyces pyogenes. 241 71

Interleukin-1 (IL-1) is secreted by macrophages, macrophage-like cells (e.g. Langerhans cells) and by astrocytes, keratinocytes, fibroblasts or natural killer cells. IL-1 is directly involved in the activation of helper T lymphocytes. However, it has been shown that IL-1 also induces release of collagenase and prostaglandins by fibroblasts. Furthermore, injections of IL-1 into animals are followed by fever, leukocytosis, increased serum concentrations of fibrinogen, serum amyloid A and haptoglobin, and decreased levels of iron and zinc. IL-1 has been extracted from experimental granuloma and from tissues of animals with endotoxinemia. Synovial fluids from patients with osteoarthritis contain significant amounts of IL-1. All in all, IL-1 may be ultimately involved in the development of fever and fibrosis, in the destruction of joints and the activation of T lymphocytes during inflammatory processes.
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PMID:[Interleukin 1]. 241 45

The synthesis of plasma proteins directed by mRNA from human brain tissues was studied by combining in vitro or in ovo translation of mRNAs with crossed immunoelectrophoresis of the mRNA-directed labeled polypeptides, followed by autoradiography of the washed plates. Poly(A)-containing mRNA was prepared from different developmental stages of fetal and postnatal human brain and also from primary glioblastomas and meningiomas. Several plasma protein-like polypeptides were identified in the autoradiographs by their migration coordinates in the two-dimensional gels, compared with immunoprecipitates formed by mature, unlabeled, stainable proteins. These included polypeptides migrating like Gc globulin, haptoglobin, fibrinogen, alpha-fetoprotein, transferrin, cholinesterase, and alpha 2-macroglobulin; other, yet unidentified plasma proteins, were also observed. In general, the synthesis of these plasma proteins appeared to be more pronounced in fetal and neoplastic brain tissues than in postnatal tissues. However, clear immunoprecipitates for some of these plasma proteins could also be detected in products directed by mRNA from particular regions of mature, normal brains, indicating that some synthesis of plasma proteins takes place in the human brain even as late as 40 years of age. mRNAs for several proteins were also identified in samples of neoplastic brain. mRNA for transferrin was identified in normal fetal and adult brain but not in either the glioblastomas or meningiomas studied. Microinjected Xenopus oocytes, in which post-translational processing occurs as well, were also used to translate fetal brain mRNA. Several plasma proteins could be detected in the translation products which were induced and stored in the oocytes. These included hemopexin, which could not be detected in the in vitro system. Others, such as cholinesterase, were found to be secreted by the oocytes. These findings indicate that different cell types in the human brain may produce and either store or secrete particular plasma proteins at defined stages in their development.
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PMID:Synthesis of plasma proteins in fetal, adult, and neoplastic human brain tissue. 242 74

Protein extracted from 24 human aortic intimas (6-33 years old) with 9 M urea mixture, were studied after separation by two-dimensional gel electrophoresis (2-DE) and silver staining. The protein composition of normal intima in 4 cases, each without any gross changes in the thoracic aorta, displayed similarity. In each 2-DE protein pattern of these intimas about 150 polypeptide spots were detectable/mg of wet tissue. Major and medium polypeptides were described by relative molecular weight Mr in kilodaltons (kDa) and relative charge Cr. Major proteins found were actin (P44-18; Mr = 44 kDa; Cr = -18), tropomyosin-like proteins (P34-29, P35-28.5, P36-31) and two glycoproteins (G35-21, G35-23.5). Several new major and medium extracellular proteins were demonstrated in fibro-fatty lesions as well as in the lesion-free intimas adjacent to lesion in 3 cases. Many of these proteins appeared to originate from plasma: albumin, IgG, alpha 1-antitrypsin, transferrin, haptoglobin beta-chain, apo A-I, apo A-II, fibrinogen beta-chain, alpha 2-HS glycoprotein and alpha 1-antichymotrypsin. Visual comparison of intimal protein patterns from 17 different cases with varying degree of fatty streaks in the thoracic aorta, showed variability in 2 polypeptides P32-17.8 and P32-19.8 as well as 4 plasma proteins albumin, alpha 1-antitrypsin, transferrin and apo A-I. This study suggests that changes in protein composition may occur in the human aortic intima during the initial histological stages of atherogenesis providing potentially useful markers for their identification and pathophysiological evaluation.
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PMID:Human aortic intima protein composition during initial stages of atherogenesis. 242 64

All 11 streptococcal cultures of serological group A possessing antigen T4 bound human 125I-labelled haptoglobin (hp) and fibronectin (fbn). Most of these cultures also interacted with alpha 2-macroglobulin (alpha 2m), immunoglobulin G (IgG) and fibrinogen (fib), none with albumin. The binding of the labelled hp could be completely inhibited by unlabelled hp. It was not significantly affected by the other plasma proteins, except alpha 2m. Trypsinization of the streptococci reduced their binding activities for hp, fbn, fib and alpha 2m, but not for IgG. Extraction with guanidine hydrochloride removed non-covalently bound substances from the streptococci without loss in binding-activity for hp.
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PMID:Binding of human haptoglobin to streptococci of serological group A. 242 72

Inflammation can be considered as a reactional process towards an injury of any etiology. It is clinically characterized by the four major points described by Celse. The symptoms are usually associated with fever and with a biological syndrome including an increased sedimentation rate related to an elevation of inflammatory plasma proteins. The Acute Phase Reactant Proteins (orosomucoid, alpha 1-antitrypsin, alpha 1-antichymotrypsin, haptoglobin, ceruloplasmin, C reactive protein and fibrinogen) are released by the hepatocytes. The complement components C3 and C4, transferrin and alpha 2-macroglobulin can also be generated by the macrophages. At inflammation sites, the activated host phagocytes release a Leukocytic Endogenous Mediator (LEM) or Interleukin I. A circulating cleavage product of Interleukin I, called "Proteolysis Inducing Factor" induces an increased muscle proteolysis and hepatic amino acids uptake for inflammatory proteins synthesis, principaly in the form of Acute Phase Reactant Proteins. Furthermore, this monokin stimulates the T4 helpers lympocytes production of a lymphokin: Interleukin II. There is no "inflammation protein" characterized by the 5 criteria of the Clinical Biology French Society. Therefore the association of a high turn over protein (CRP) and a low turn over one (orosomucoid and/or haptoglobin) is usefull for the detection of an inflammatory process and to evaluate a therapeutic efficiency. These proteins are usually selected for early diagnosis of neonatal bacterial infections and for the diagnosis of myocardial infarction. In the present time, numerous studies using statistical methods try to separate inflammatory processes according to their etiology.
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PMID:[Inflammatory syndrome and changes in plasma proteins]. 243 74

A subline of the rat hepatoma (H-35) cells has been identified which responds to hepatocyte-stimulating factors (HSFs) of human squamous carcinoma cells by increased synthesis of all major rat acute phase plasma proteins. The regulation occurs at the level of mRNA. Two HSFs (HSF-I and HSF-II) have been purified from conditioned medium of the squamous carcinoma cells. HSF-I is a protein with an Mr = 18,000 and pI 5.5, and HSF-II is a glycoprotein with an Mr = 34,000 and a broad, neutral to basic charge. In H-35 cells, HSF-I predominantly stimulates the synthesis of complement C3 and haptoglobin and acts synergistically with dexamethasone to stimulate alpha 1-acid glycoprotein. HSF-II stimulates cysteine protease inhibitor, alpha 1-antichymotrypsin, alpha 1-antitrypsin, fibrinogen, and hemopexin, and acts synergistically with dexamethasone to stimulate alpha 2-macroglobulin. Each HSF is between 10 and 100 times less effective in regulating proteins of the other set. Human tumor necrosis factor and interleukin-1 increase complement C3, haptoglobin, and alpha 1-acid glycoprotein, as does HSF-I, but are unable to modulate any of the other acute phase proteins. The monokines differ from HSF-I is their low activity in HepG2 cells and rat hepatocytes.
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PMID:Distinct sets of acute phase plasma proteins are stimulated by separate human hepatocyte-stimulating factors and monokines in rat hepatoma cells. 243 11


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