Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0393754 (HSA)
 2,996 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Sera taken from AKR/J mice 7 d after the intravenous injection of 2,4,6-trinitrophenyl-lys-Ficoll (TNP-F) caused a specific inhibition of anti- trinitrophenol (TNP) plaque-forming cells (PFC) in vitro. This inhibition was reversed by the incorporation of 10(-8)-10(-7) M 2,4,6-trinitrophenyl- epsilon-amino-n-caproic acid (TNP-EACA) into the agar during the PFC assay. The factor responsible for the hapten-reversible PFC inhibition was removed from serum by passage through an anti-immunoglobulin column or through a 2,4,-dinitrophenyl-human-serum-albumin-bromoacetylcellulose plus anti-TNP- antibody column, but not by DNP-HSA-BAC alone. It was concluded that this immunoglobulin-like substance, lacking anti-TNP activity but reacting with anti-TNP antibody of AKR/J origin, was most likely an auto-anti-idiotypie antibody that had been produced during the normal course of the response of AKR/J mice to TNP-F. Pools of anti-idiotypic-antibody-containing antisera inhibited anti-TNP plaque formation to varying degrees when tested on d-4 PFC from different mice of the same inbred strain, suggesting a variability in idiotype expression. 4 d after transfer of immune (7 d after 10 mug TNP-F, administered intravenously) AKR/J spleen cells plus 10 mug TNP-F into syngeneic mice, the number of PFC detectable in the recipients' spleens could be markedly augmented by the inclusion of TNP-EACA in the agar during the PFC assay. Incubation of spleen cells containing such hapten-augmentable PFC with TNP- EACA yielded a factor in the supernate that caused a specific, in vitro, hapten-reversible inhibition of anti-TNP PFC. Studies with immunoadsorbents indicated that this PFC-inhibiting factor was antigenically immunoglobulin- like, lacked anti-TNP-antibody activity, but reacted with anti-TNP antibody of AKR/J origin. The results are consistent with the view that this PFC inhibitor is auto-anti-idiotypic antibody that is involved in the normal regulation of the immune response. It is proposed that hapten-reversible inhibition of plaque formation can be employed as an assay for anti-idiotypic antibody and the conditions for such an assay are described. It is further proposed that the detection of hapten-augmentable PFC suggests the presence of auto-anti-idiotypic antibody.
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PMID:Production of auto-anti-idiotypic antibody during the normal immune response to TNP-Ficoll. II. Hapten-reversible inhibition of anti-TNP plaque-forming cells by immune serum as an assay for auto-anti-idiotypic antibody. 31 4

A 17-year-old man was occupationally exposed to pyromellitic acid dianhydride dust during the production of epoxy resin in a chemical factory. He was clinically diagnosed as having acute hemorrhagic alveolitis associated with anemia. The serologic analysis revealed a high concentration of IgG antibodies against pyromellitic acid dianhydride-treated human serum albumin (PMDA-HSA). Immunoblotting with PMDA-treated human serum as antigen and the patient's serum as the first antibody showed that additional PMDA-modified serum proteins other than HSA were recognized by the patient's IgG antibodies in the higher mol. mass range (> 67 kDa). No specific IgG could be detected against other anhydride conjugates (maleic acid, MA; phthalic acid, PA) with the exception of a reaction with the trimellitic acid anhydride-conjugated HSA (TMA-HSA). No specific IgE antibodies could be detected against any of the above mentioned antigens, but immunoblotting of the patient's serum indicated IgG4-type autoantibodies against in vitro PMDA-treated Ig molecules of normal serum proteins.
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PMID:Acute autoimmune response in a case of pyromellitic acid dianhydride-induced hemorrhagic alveolitis. 809 30

Phthalate plasticizers have been subjected to close scrutiny and evidences of their toxicity and other negative environmental impacts have arisen as a result of their use in food in some countries. Once entering human body, plasticizers could affect the conformation of human serum albumin and protein function. The interaction between two phthalate plasticizers and human serum albumin was investigated by multispectroscopic techniques and molecular modeling. The alteration in protein conformational stability was determined by fluorescence quenching data. The thermodynamic parameters indicated that the hydrophobic interactions played a major role in the process. In addition, the alterations of HSA secondary structure in the presence of phthalate plasticizers were investigated. Molecular modeling and displacement experiments showed that phthalate plasticizers situated within subdomain IIA (site I) of HSA. Furthermore, the binding distances for the plasticizers-HSA system were provided by the efficiency of fluorescence resonance energy transfer.
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PMID:The binding affinity of phthalate plasticizers-protein revealed by spectroscopic techniques and molecular modeling. 2499 62