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

Experimentally delayed mouse blastocysts were activated to implant by exogenous estradiol and after varying duration of estrogen influence, the blastocysts were flushed out from the uterine horns. Then they were incubated in the cold with different, 125I-conjugated proteins and the amount of protein bound to the blastocysts was determined by radioassay. Three radiolabelled proteins: human serum albumin (125I-HSA), human serum transferrin (125I-HST) and normal rabbit IgG (125I-RIgG) were tested and it was found that the uptake of each protein markedly increased between 14 and 24 hours of estrogen-activation. It was possible to partially block the binding of 125I-HSA and 125I-RIgG with the respective unlabelled protein. Unlabelled RIgG could also partially block the uptake of 125I-HSA whereas HSA did not impede the binding of 125I-RIgG. During delay of implantation the protein binding was low and approximately the same as after 14 hours of activation. However, at 18 and 24 hours of activation protein uptake increased gradually. Raising the incubation temperature from 0 to 37 degrees C did not significantly influence the protein binding capacity of the 24-hour-activated blastocyts. Whole blastocyst autoradiography indicated that the labelled protein was heavily bound in patches, preferentially located in the abembryonic half of the postattachment blastocysts. It is assumed that the binding of protein to abembryonic trophoblast cells of the implanting blastocyst can be attributed to the presence of protein receptors on the surface of these cells.
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PMID:Binding of proteins to mouse blastocysts after the attachment stage of implantation. 101 63

To determine the extent of conservation between bovine syntenic group U10, human chromosome 21 (HSA 21), and mouse chromosome 16 (MMU 16), 11 genes were physically mapped by segregation analysis in a bovine-hamster hybrid somatic cell panel. The genes chosen for study span MMU 16 and represent virtually the entire q arm of HSA 21. Because the somatostatin gene (SST), an HSA 3/MMU 16 locus, was previously shown to be in U10, the transferrin gene (TF), an HSA 3/MMU 9 marker, was also mapped to determine whether U10 contains any HSA 3 genes not represented on MMU 16. With the exception of the protamine gene PRM1 (HSA 16/MMU 16), all of the genes studied were syntenic on bovine U10. Thus, all homologous loci from HSA 21 that have been studied in the cow are on a single chromosome. The bovine homolog of HSA 21 also carries several HSA 3 genes, two of which have homologous loci on MMU 16. The syntenic association of genes from the q arm of HSA 3 with HSA 21 genes in two mammalian species, the mouse and the cow, indicates that HSA 21 may have that contained genes now residing on HSA 3. Additionally, the syntenic association of TF with SST in the cow permits the prediction that the rhodopsin gene (RHO) is proximal to TF on HSA 3q.
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PMID:Evidence for the evolutionary origin of human chromosome 21 from comparative gene mapping in the cow and mouse. 198 61

A method was established for estimation of plasma volume and splenic plasma pool by quantitative scanning using 113mIn labelled transferrin (TF). The method was used in 12 patients with various haematological disorders and degrees of splenomegaly. 113mIn-TF consistently gave about 6% over-estimation of plasma volume by comparison with the standard 125I HSA method. The splenic plasma pool ranged from 1.2% to 11.4% of the total plasma volume. By concurrent measurement of splenic red cell pool the splenic haematocrit (SHct) was obtained: mean 0.51, SD 0.08; the SHct/PCV ratio was 1.21 (SD 0.31) and the SHct/body Hct ratio was 1.30 (SD 0.30). SHct was independent of PCV and body Hct but there was a trend to a lower SHct in cases where splenomegaly was more marked. Direct measurement of splenic plasma pool may help to elucidate the cause of increased total plasma volume in such patients.
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PMID:Splenic haematocrit and the splenic plasma pool. 359 58

Two strains of guinea pigs were parenterally immunized with well-characterized diisocyanate-protein conjugates. Hapten-specific IgE antibodies were detected in the sera of English short-hair strain guinea pigs immunized with either toluene diisocyanate-human serum albumin (TDI-HSA) or hexamethylene diisocyanate-HSA (HDI-HSA) when these sera were analyzed by the 168 hr passive cutaneous anaphylaxis (PCA) technique followed by intravenous challenges with conjugates of respective ligands coupled to an unrelated carrier protein, transferrin. IgG1 antibodies and precipitating antibodies were demonstrated in Hartley strain guinea pigs immunized with TDI/HDI-HSA conjugates. The hapten specificity of these antibodies was proved by PCA inhibition experiments and antibody absorption experiments. In the precipitating antibody system, this was further confirmed by immunoelectrophoretic analysis. Cross-reactivity between HDI and TDI was not observed in the PCA experiments. However, apparent cross-reactivity in the double gel diffusion experiments was due to new antigenic determinants formed by isocyanates after conjugation with proteins. It was therefore apparent that immune responses of guinea pigs immunized with protein conjugates of bifunctional isocyanates were heterogeneous and involved multiple specificities for hapten, carrier protein, and new antigenic determinants. It was postulated that the complex nature of the immune response generated by diisocyanate compounds in the guinea pig may also serve as a more appropriate model of isocyanate-induced human sensitivity reactions, which are known to involve diverse immunologic and nonimmunologic mechanisms.
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PMID:The guinea pig model of diisocyanate sensitization. I. Immunologic studies. 629 May 54

Microcarrier cell culture provides an efficient method for the production of cell products. Cytodex 3 microcarriers were used for the production of an active nerve growth-promoting substance from chicken heart fibroblasts (1 degree -4 degrees cultures). Such cells release into culture medium a factor which stimulates the growth of nerve fibres from explanted ciliary, sympathetic and spinal neurons. Furthermore, culture in low-serum or serum-free media reduces the presence of contaminating proteins and facilitates the production and biochemical analysis of this factor. A mixture of DME/F 10 was supplemented with either 10% (v/v) foetal calf serum (FCS), 0.5% FCS, a low molecular weight fraction of FCS, (MW less than 10,000; prepared by dialysis) or different hormones and growth factors. Cells cultured in medium supplemented with insulin (I, 1 microgram/ml), transferrin (T, 25 micrograms/ml), human serum albumin (HSA, 2 mg/ml) and fibronectin (F, 10 micrograms/ml) (ITAF) in combination with 0.5% FCS or a low molecular weight fraction of FCS progressed through the cell cycle with normal kinetics and maximum DNA synthesis was after 20 h. The results were similar to those obtained with a supplement of 10% FCS alone. Media supplemented with insulin, transferrin, fibronectin and HSA in combination with dexamethasone (200 ng/ml) or epidermal growth factor (10 ng/ml) did not promote cell proliferation to the same extent. The fibroblasts proliferated on Cytodex 3 at a rate similar to cells grown on cell culture plastic and produced sufficient amounts of nerve growth-promoting substance for biological analysis. Production of this factor was generally associated with cell proliferation.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:The use of Cytodex 3 microcarriers and reduced-serum media for the production of nerve growth promoters from chicken heart cells. 667 40

Coating of Immulon polystyrene plates with 0.2% casein in phosphate buffered saline (PBS) completely abolishes adsorption of human serum proteins to these plates. However, pretreatment of such plates with PBS or 0.15 M NaCl in deionized water (10 microS) before coating makes possible adsorption of human immunoglobulins G (HIgG) and M but not serum albumin (HSA) and transferrin (HTrf). Effect of pretreatment with PBS on adsorption of HIgG is long-term and rather stable. Results of experiments with radioiodinated HIgG, mouse IgG, HSA and human chorionic gonadotropin confirm the peculiar effect of pretreatment with PBS on casein coating. Pretreatment with deionized water, instead of PBS, markedly diminish adsorption but tap or commercial spring waters (> 1000 microS), even without 0.15 M NaCl, affect adsorption similarly to PBS in deionized water. Super pure water (0.05 microS) even with NaCl used for pretreatment does not influence adsorption of HIgG to plates coated with casein. Distinct differences in adsorption of HIgG and HTrf was demonstrated using solutions for ELISA prepared from super pure, deionized and tap waters.
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PMID:Effect of pretreatment of wells in polystyrene plates on adsorption of some human serum proteins. 750 47

Lactoferrin (LTF), which is the major iron-binding protein in milk and physiological fluids, belongs to the transferrin family. We report here the sequence of a caprine LTF cDNA, 2411 bp in length, encoding the pre-protein (709 amino acid residues). Sequence comparisons reveal that structural features, including iron-binding sites, cysteine residues involved in disulphide bonds are remarkably conserved between LTF proteins from various species. Of the 5 potential glycosylation sites identified, only one site appears to be conserved between artiodactyls, rodents and humans. Using a somatic cell hybrid panel, the LTF locus was assigned to the bovine U12 syntenic group. This assignment and the localization of the LTF gene on bovine chromosome 22 (BTA 22) by Schwerin et al. (1) using fluorescent in situ hybridization achieves an additional analogy between a synteny group and a chromosome in cattle. Since serum transferrin (STF) had been previously mapped on BTA 1, in cattle LTF and STF loci are not localized on the same chromosome, conversely to the situation observed in humans (HSA 3) and mice (MMU 9).
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PMID:Characterization of the goat lactoferrin cDNA: assignment of the relevant locus to bovine U12 synteny group. 809 48

The enzyme that catalyzed the conversion of human salivary alpha-amylase family A (HSA-A) to family B (HSA-B) was identified. It was partially purified from the precipitate obtained by centrifugation of human saliva at 105,000 x g for 60 min by solubilization with 3[(3-cholamidopropyl)dimethylammonio]-1-propane sulfonate and column chromatographies with Sephacryl S-300-HR and hydroxylapatite. The enzyme preparation was practically free from contaminating exoglycosidases and proteases. The enzyme cleaved the N,N'-diacetylchitobiose moiety of the sugar chain of HSA-A, as shown by the isolation of the protein moiety which contained 1 GlcNAc and 1 Fuc residue and the sugar chain (Gal)2(Fuc)1(GlcNAc)2(Man)3(GlcNAc). This enzyme also cleaved the N,N'-diacetylchitobiose moiety of the sugar chain of human transferrin tetraglycopeptide Asn-Tyr-Asn(GlcNAc)2(Man)3(GlcNAc)2(Gal)2-Lys to yield equimolar amounts of peptide Asn-Tyr-Asn(GlcNAc)Lys and sugar chain (Gal)2(GlcNAc)2(Man)3(GlcNAc). The enzyme was identified as an endo-beta-N-acetylglucosaminidase. The enzyme acted on HSA-A with desialylated and defucosylated outer chain moieties of the sugar chains at a similar rate as that of native HSA-A. The enzyme activity was reduced to 13 and 5% using HSA-A with the sugar chains whose outer chain moieties lacked Gal and GlcNAc, respectively, from the nonreducing end. The enzyme also acted on human transferrin, calf fetuin, and asparagine oligosaccharides of transferrin and fetuin. On the other hand, the enzyme did not act on ovalbumin, RNase B, Taka-amylase, yeast invertase, and ovalbumin asparagine oligosaccharides. These results indicate that human salivary endo-beta-N-acetylglucosaminidase is specific for complex type sugar chains and can release the sugar chains from native glycoproteins and glycopeptides regardless of the existence of a Fuc residue on the proximal GlcNAc of the N,N'-diacetylchitobiose core of their sugar chains. The source of the enzyme was epithelial cells peeling from the oral cavity epithelium into saliva. The enzyme was thought to be integrated on the surface of the epithelial cell membrane. This enzyme was named endo-beta-N-acetylglucosaminidase HS. Thus, these studies indicate that the properties of the enzyme are distinct from those of known endo-beta-N-acetylglucosaminidase and endo-beta-N-acetylglucosaminidase HS is a novel endo-beta-N-acetylglucosaminidase.
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PMID:Human salivary endo-beta-N-acetylglucosaminidase HS specific for complex type sugar chains of glycoproteins. 834 Apr 28

The genes for pituitary-specific transcription factor (PIT1), propionyl coenzyme A carboxylase, beta-polypeptide (PCCB), transferrin (TF), trichohyalin (THH), and involucrin (IVL) were mapped to cattle chromosome 1 (BTA 1) by isotopic in situ hybridization. Two of the loci were mapped from cattle PCR products and three from human ATCC probes. PIT1 localized to segment 1q2; PCCB to 1q3; and TF, THH, and IVL to 1q4. These localizations agree with the homology previously shown between BTA 1 and human chromosome 3 (HSA 3). Some homology with HSA 1 has been established with the mapping of THH and IVL to BTA 1q4.
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PMID:In situ hybridization of five loci to cattle chromosome 1. 969 Nov 75

Human transferrin was covalently coupled to ultrasmall superparamagnetic iron oxide (USPIO) particles, and the transferrin-USPIO obtained was investigated in vivo in experimental SMT/2A tumor-bearing rats (rat mammary carcinoma). Physicochemical characterization showed an overall size of 36 nm (DLS) with a core size of 5 nm (TEM). Relaxivities were R1 = 23.6 and R2 = 52.1 liter/mmol.s (0.47 T). Bound transferrin was 280 micrograms/mg of iron. Pharmacokinetic investigations revealed a half-life of 17 min in normal rats. The MR evaluation of tumor signal intensity over time showed a 40% (range 25-55%) signal reduction 150 min after injection with the reduction persisting for at least 8 h. Control experiments using the parent USPIO compound or USPIO labeled with a nonspecific human serum albumin (HSA-USPIO) showed a change of only 10% (range 5-15%) in tumor signal intensity over time. The results demonstrate that a combination of the USPIO relaxivity properties with the specificity of transferrin-mediated endocytosis allows in vivo detection of tumors by MR imaging.
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PMID:Targeting of ultrasmall superparamagnetic iron oxide (USPIO) particles to tumor cells in vivo by using transferrin receptor pathways. 970 5


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