Journal articles: 'Human bioactivity'

1

Simpson, B. J. B., C. G. Tsonis, and F. C. W. Wu. "INHIBIN BIOACTIVITY IN HUMAN TESTICULAR EXTRACTS." Journal of Endocrinology 115, no. 2 (November 1987): R9—R12. http://dx.doi.org/10.1677/joe.0.115r009.

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ABSTRACT Inhibin bioactivity was measured in human testicular extracts by a sensitive sheep pituitary cell bioassay. The relationship between testicular inhibin bioactivity, daily sperm production (DSP) and plasma concentrations of FSH, LH, testosterone and oestradiol were examined. The mean level of testicular inhibin bioactivity was 4.4 ±1.3 U/g (mean ± SD) with a significantly lower value in those who received radiotherapy (3.2 ± 1.4 U/g) than in the untreated group (4.8 ± 1.1 U/g). In contrast to the rat, human testicular inhibin bioactivity was not significantly correlated to FSH or DSP. These findings suggest that inhibin may have a complex role in normal and/or pathological testicular function.

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De Aza, P. N., Z. B. Luklinska, M. R. Anseau, F. Guitian, and S. De Aza. "Bioactivity of pseudowollastonite in human saliva." Journal of Dentistry 27, no. 2 (February 1999): 107–13. http://dx.doi.org/10.1016/s0300-5712(98)00029-3.

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Katlinski, Kanstantsin, Sviatlana Akalovich, Yuliya Katlinskaya, Anton Sholukh, Tatyana Doroshenko, Yury Chaly, and Nikolai N. Voitenok. "Soluble human CXCR2: Structure, properties, bioactivity." Cytokine 48, no. 1-2 (October 2009): 2. http://dx.doi.org/10.1016/j.cyto.2009.07.377.

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Katlinski, Kanstantsin, Sviatlana Akalovich, Yuliya Katlinskaya, Anton Sholukh, Tatyana Doroshenko, Yury Chaly, and Nikolai N. Voitenok. "Soluble human CXCR2: Structure, properties, bioactivity." Cytokine 48, no. 1-2 (October 2009): 102. http://dx.doi.org/10.1016/j.cyto.2009.07.431.

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Page, S. R., A. H. Taylor, W. Driscoll, M. Baines, R. Thorpe, A. P. Johnstone, S. S. Nussey, and G. St J. Whitley. "Modulation of the biological activity of thyrotrophin by anti-human thyrotrophin monoclonal antibodies." Journal of Endocrinology 126, no. 2 (August 1990): 333–40. http://dx.doi.org/10.1677/joe.0.1260333.

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ABSTRACT The mechanism by which monoclonal antibodies enhance the biological activity of a number of hormones is poorly understood. One such antibody (GC73), which binds to human but not bovine TSH, enhances the bioactivity of human TSH in vivo. We have investigated whether GC73 enhancement of TSH bioactivity involves potentiation of hormone-receptor activation assessed by the cyclic AMP (cAMP) responses of both primary human thyrocyte cultures and a TSH-responsive human thyrocyte cell line (SGHTL-45). GC73 had no effect on basal cAMP production. In contrast to its enhancement of the bioactivity of human TSH in vivo, it markedly inhibited the cAMP response to 1 and 10 mU human TSH/ml in primary thyrocytes. This effect was dose-dependent with neutralization of the bioactivity of TSH occurring at 2 mg GC73/ml. GC73 had no effect on the bioactivity of bovine TSH. In contrast, a second anti-TSH monoclonal antibody (TC12), which binds to both human and bovine TSH, inhibited the bioactivity of both species of TSH. Similar results were obtained using SGHTL-45 cells, although the peak concentrations of cAMP were lower. We conclude that binding of GC73 to human TSH resulted in inhibition rather than enhancement of the in-vitro biological activity of human TSH. We suggest that GC73 enhancement of human TSH bioactivity seen in vivo does not result from a mechanism involving potentiation of receptor activation by human TSH. Journal of Endocrinology (1990) 126, 333–340

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Ackland, J. F., S. J. Ratter, G. L. Bourne, and L. H. Rees. "Corticotrophin-releasing factor-like immunoreactivity and bioactivity of human fetal and adult hypothalami." Journal of Endocrinology 108, no. 2 (February 1986): 171–80. http://dx.doi.org/10.1677/joe.0.1080171.

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ABSTRACT Corticotrophin releasing factor-like immunoreactivity (CRF-LI) and bioactivity, and arginine vasopressinlike immunoreactivity (AVP-LI) have been measured in extracts of human fetal and adult hypothalamic tissue and their development with the gestational age of the fetuses (12–27 weeks) studied. CRF-LI was measured by a radioimmunoassay developed for ovine corticotrophin-releasing factor (oCRF-41). Corticotrophin-releasing factor bioactivity was measured in a rat isolated anterior pituitary cell perfusion system. CRF-LI and bioactivity and AVP-LI were all detectable in fetal hypothalamic extracts from 12 to 13 weeks of gestational age. CRF-LI was also present in human fetal pituitary glands from 12 weeks of gestational age. The concentration of CRF-LI in the fetal hypothalamic extracts (9·2±11·4 ng/g, mean ± s.e.m., n = 33) showed no significant correlation with the gestational age of the fetuses. However the concentration of AVP-LI (25·0–36·8 ng/g, n = 17) did show a positive correlation (r = 0·508, P<0·05) with gestational age, as did the concentration of CRF bioactivity (471·3–556·3 ng ACTH released/g tissue, n = 13, r = 0·725, P < 0·01). The CRF bioactivity of all fetal hypothalamic extracts was potentiated by the addition of synthetic human (h)AVP, but the bioactivity of the adult hypothalamic extracts was not, presumably because of the higher levels of AVP-LI already present in the adult extracts. Pretreatment of tissue extracts with antisera to oCRF-41 and/or hAVP reduced the CRF bioactivity of all hypothalamic extracts. Sephadex chromatography of fractions which co-eluted with synthetic oCRF-41 or hAVP contained CRF bioactivity and this bioactivity was potentiated when synthetic hAVP or oCRF-41, respectively, were added to the fractions. However, a larger molecular weight form of CRF-LI (8000–10 000 daltons), which was observed only in fetuses of 20 weeks of gestational age or less, did not contain any significant CRF bioactivity. J. Endocr. (1986) 108, 171–180

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Fukushima, Naobumi, Kanji Nagashima, and Takayoshi Kuroume. "Fibronectin Synthesis Bioactivity in Human Breast Milk." Neonatology 65, no. 2 (1994): 77–84. http://dx.doi.org/10.1159/000244030.

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Iriti, Marcello, and Franco Faoro. "Bioactivity of Grape Chemicals for Human Health." Natural Product Communications 4, no. 5 (May 2009): 1934578X0900400. http://dx.doi.org/10.1177/1934578x0900400502.

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Grapevine ( Vitis vinifera) products, grape and grape juice, represent a valuable source of bioactive phytochemicals, synthesized by three secondary metabolic pathways (phenylpropanoid, isoprenoid and alkaloid biosynthetic routes) and stored in different plant tissues. In the last decades, compelling evidence suggested that regular consumption of these products may contribute to reducing the incidence of chronic illnesses, such as cancer, cardiovascular diseases, ischemic stroke, neurodegenerative disorders and aging, in a context of the Mediterranean dietary tradition. The health benefits arising from grape product intake can be ascribed to the potpourri of biologically active chemicals occurring in grapes. Among them, the recently discovered presence of melatonin adds a new element to the already complex grape chemistry. Melatonin, and its possible synergistic action with the great variety of polyphenols, contributes to further explaining the observed health benefits associated with regular grape product consumption.

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Elliott, Steve, Tony Lorenzini, David Chang, Jack Barzilay, and Evelyne Delorme. "Mapping of the Active Site of Recombinant Human Erythropoietin." Blood 89, no. 2 (January 15, 1997): 493–502. http://dx.doi.org/10.1182/blood.v89.2.493.

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Abstract Recombinant human erythropoietin (rHuEPO) variants have been constructed to identify amino acid residues important for biological activity. Immunoassays were used to determine the effect of each mutation on rHuEPO folding. With this strategy, we could distinguish between mutations that affected bioactivity directly and those that affected bioactivity because the mutation altered rHuEPO conformation. Four regions were found to be important for bioactivity: amino acids 11 to 15, 44 to 51, 100 to 108, and 147 to 151. EPO variants could be divided into two groups according to the differential effects on EPO receptor binding activity and in vitro biologic activity. This suggests that rHuEPO has two separate receptor binding sites. Mutations in basic residues reduced the biologic activity, whereas mutations in acidic residues did not. This suggests that electrostatic interactions between rHuEPO and the human EPO receptor may involve positive charges on rHuEPO.

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Li, Yun Cang, Jian Yu Xiong, C. S. Wong, Peter D. Hodgson, and Cui E. Wen. "Bioactivating the Surfaces of Titanium by Sol-Gel Process." Materials Science Forum 614 (March 2009): 67–71. http://dx.doi.org/10.4028/www.scientific.net/msf.614.67.

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In the present study, titanium (Ti) samples were surface-modified by titania (TiO2), silica (SiO2) and hydroxyapatite (HA) coatings using a sol-gel process. The bioactivity of the film-coated Ti samples was investigated by cell attachment and morphology study using human osteoblast-like SaOS-2 cells. Results of the cell attachment indicated that the densities of cell attachment on the surfaces of Ti samples were significantly increased by film coatings; the density of cell attachment on HA film-coated surface was higher than those on TiO2 and SiO2 film-coated surfaces. Cell morphology study showed that the cells attached, spread and grew well on the three kinds of film-coated surfaces. It can be concluded that the three kinds of film coatings can bioactivate the surfaces of Ti samples effectively. Overall, Ti sample with HA film-coated surface exhibited the best bioactivity.

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Funakoshi, Akihiro, Kyoko Miyasaka, Rieko Nakamura, Kenichi Kitani, Susumu Funakoshi, Hirokazu Tamamura, Nobutaka Fujii, and Haruaki Yajima. "Bioactivity of synthetic human pancreastatin on exocrine pancreas." Biochemical and Biophysical Research Communications 156, no. 3 (November 1988): 1237–42. http://dx.doi.org/10.1016/s0006-291x(88)80765-4.

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Kratzer, Paul G., Mitchell S. Golbus, David E. Finkelstein, and Robert N. Taylor. "Trisomic pregnancies have normal human chorionic gonadotropin bioactivity." Prenatal Diagnosis 11, no. 1 (January 1991): 1–6. http://dx.doi.org/10.1002/pd.1970110102.

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De Aza, Piedad N., Zofia B. Luklinska, and Michel Anseau. "Bioactivity of diopside ceramic in human parotid saliva." Journal of Biomedical Materials Research Part B: Applied Biomaterials 73B, no. 1 (2005): 54–60. http://dx.doi.org/10.1002/jbm.b.30187.

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Yao, Wenrong, Lei Yu, Wenhong Fan, Xinchang Shi, Lan Liu, Yonghong Li, Xi Qin, Chunming Rao, and Junzhi Wang. "A Cell-Based Strategy for Bioactivity Determination of Long-Acting Fc-Fusion Recombinant Human Growth Hormone." Molecules 24, no. 7 (April 9, 2019): 1389. http://dx.doi.org/10.3390/molecules24071389.

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The long-acting growth hormone (LAGH) is a promising alternative biopharmaceutical to treat growth hormone (GH) deficiency in children, and it was developed using a variety of technologies by several pharmaceutical companies. Most LAGH preparations, such as Fc fusion protein, are currently undergoing preclinical study and clinical trials. Accurate determination of bioactivity is critical for the efficacy of quality control systems of LAGH. The current in vivo rat weight gain assays used to determine the bioactivity of recombinant human GH (rhGH) in pharmacopoeias are time-consuming, expensive, and imprecise, and there are no recommended bioassays for LAGH bioactivity in pharmacopoeias. Therefore, we developed a cell-based bioassay for bioactivity determination of therapeutic long-acting Fc-fusion recombinant human growth hormone (rhGH-Fc) based on the luciferase reporter gene system, which is involved in the full-length human GH receptor (hGHR) and the SG (SIE and GAS) response element. The established bioassay was comprehensively validated according to the International Council for Harmonization (ICH) Q2 (R1) guidelines and the Chinese Pharmacopoeia, and is highly precise, time-saving, simple, and robust. The validated bioassay could be qualified for bioactivity determination during the research, development, and manufacture of rhGH-Fc, and other LAGH formulations.

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Richard, Craig A. H., Mitchell D. Creinin, Carolyn J. Kubik, and Julie A. DeLoia. "Enzymatic removal of asparagine-linked carbohydrate chains from heterodimer human chorionic gonadotrophin and effect on bioactivity." Reproduction, Fertility and Development 19, no. 8 (2007): 933. http://dx.doi.org/10.1071/rd07077.

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The native form of human chorionic gonadotropin (hCG) is a heterodimer protein with two asparagine (Asn)-linked carbohydrate chains on each subunit. Removal of the Asn-linked carbohydrate chains from hCG has resulted in hCG variants with consistent antagonistic properties on isolated murine cells. Specific and direct enzymatic removal of these carbohydrate chains from native hCG with resultant antagonistic properties has not been reported. An antagonist to the hCG/luteinising hormone (LH) receptor could be used as an anticancer therapy, emergency contraceptive or for therapeutic resolution of ectopic pregnancies. Therefore, our aim was to use enzymes to specifically remove Asn-linked carbohydrate chains from hCG in the heterodimer form and analyse the resultant bioactivity. Native hCG was treated with endoglycosidases, carbohydrate removal was analysed with electrophoresis and the hCG variants were tested for altered bioactivity with human and murine cells. Endoglycosidases were able to cleave most of the Asn-linked carbohydrate chains from the native hCG. The deglycosylated hCG demonstrated a 75% reduction in bioactivity on a murine Leydig cell line and a 65% reduction in bioactivity on human granulosa cells. These results exemplify a simple and efficient method for creating deglycosylated hCG and provide the most direct evidence for the importance of Asn-linked carbohydrate chains in maintaining hCG bioactivity.

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Chen, Jian-Wen, Thomas Ledet, Hans Ørskov, Niels Jessen, Sten Lund, Jonathan Whittaker, Pierre De Meyts, Maj Britt Larsen, Jens Sandahl Christiansen, and Jan Frystyk. "A highly sensitive and specific assay for determination of IGF-I bioactivity in human serum." American Journal of Physiology-Endocrinology and Metabolism 284, no. 6 (June 1, 2003): E1149—E1155. http://dx.doi.org/10.1152/ajpendo.00410.2002.

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At present, the circulating bioactivity of insulin-like growth factor I (IGF-I) is estimated by immunological measurements of IGF-I levels. However, immunoassays ignore the modifying effects of the IGF-binding proteins (IGFBPs) on the interaction between IGF-I and the IGF-I receptor (IGF-IR). Therefore, we developed an IGF-I kinase receptor activation assay (KIRA) based on cells transfected with the human IGF-IR gene. The bioassay was sensitive (detection limit 0.08 μg/l), specific (cross-reactivity of insulin, insulin analogs, and proinsulin was <1%; IGF-II cross-reactivity was 12%), and accurate (within- and between-assay coefficients of variation <7 and <15%). The operational range of the assay (0.25–10.0 μg/l) allowed for determination of IGF-I bioactivity in serum from patients with, for example, growth hormone deficiency, type 1 diabetes, and acromegaly. Addition of IGFBPs dose dependently reduced the KIRA signal, whereas addition of IGF-II to preformed complexes (1:1 molar ratio) of IGF-I and IGFBP dose dependently increased IGF-I bioactivity by displacement of bound IGF-I. In conclusion, the KIRA will enable us to compare IGF-I bioactivity with existing immunological measurements of IGF-I in serum and, hopefully, to elucidate the factors that determine IGF-I bioactivity in vivo.

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Namachivayam, Kopperuncholan, Cynthia L. Blanco, Brandy L. Frost, Aaron A. Reeves, Ramasamy Jagadeeswaran, Krishnan MohanKumar, Azif Safarulla, et al. "Preterm human milk contains a large pool of latent TGF-β, which can be activated by exogenous neuraminidase." American Journal of Physiology-Gastrointestinal and Liver Physiology 304, no. 12 (June 15, 2013): G1055—G1065. http://dx.doi.org/10.1152/ajpgi.00039.2013.

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Human milk contains substantial amounts of transforming growth factor (TGF)-β, particularly the isoform TGF-β2. We previously showed in preclinical models that enterally administered TGF-β2 can protect against necrotizing enterocolitis (NEC), an inflammatory bowel necrosis of premature infants. In this study we hypothesized that premature infants remain at higher risk of NEC than full-term infants, even when they receive their own mother's milk, because preterm human milk contains less bioactive TGF-β than full-term milk. Our objective was to compare TGF-β bioactivity in preterm vs. full-term milk and identify factors that activate milk-borne TGF-β. Mothers who delivered between 23 0/7 and 31 6/7 wk or at ≥37 wk of gestation provided milk samples at serial time points. TGF-β bioactivity and NF-κB signaling were measured using specific reporter cells and in murine intestinal tissue explants. TGF-β1, TGF-β2, TGF-β3, and various TGF-β activators were measured by real-time PCR, enzyme immunoassays, or established enzymatic activity assays. Preterm human milk showed minimal TGF-β bioactivity in the native state but contained a large pool of latent TGF-β. TGF-β2 was the predominant isoform of TGF-β in preterm milk. Using a combination of several in vitro and ex vivo models, we show that neuraminidase is a key regulator of TGF-β bioactivity in human milk. Finally, we show that addition of bacterial neuraminidase to preterm human milk increased TGF-β bioactivity. Preterm milk contains large quantities of TGF-β, but most of it is in an inactive state. Addition of neuraminidase can increase TGF-β bioactivity in preterm milk and enhance its anti-inflammatory effects.

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Burgon, Patrick G., Peter G. Stanton, Kim Pettersson, and David M. Robertson. "Effect of desialylation of highly purified isoforms of human luteinizing hormone on their bioactivity in vitro, radioreceptor activity and immunoactivity." Reproduction, Fertility and Development 9, no. 5 (1997): 501. http://dx.doi.org/10.1071/r96123.

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To establish whether sialic acid content is responsible for an observed 7–8-fold variability in bioactivity in vitro of highly purified human pituitary luteinizing hormone (hLH) isoforms, the bioactivity in vitro, radioreceptor activity and immunoactivity of hLH isoforms were determined before and after enzymatic desialylation. Three immunofluorometric assays with different hLH specificities allowed characterization of 13–24 pituitary hLH isoform preparations of pI 7·03–8·98 in terms of sialic acid content (1–5 sialic acid residues per LH molecule), bioactivity in vitro (4030–30 000 I.U. mg-1), radioreceptor activity (6420–25 400 I.U. mg-1) and hLH immunoactivity (2900–4400 to 18 300–27 300 I.U. mg-1). Significant positive correlations between sialic acid content and either immunoactivity or in vitro bioactivity were observed, whereas radioreceptor activity showed a curvilinear response. Following more than 90% removal of sialic acid, both in vitro bioactivity and radioreceptor activity were increased, although specific activity still differed between isoforms; immunoactivities were unaffected. It is concluded that the presence of the sialic acid residue(s) on hLH isoforms does partially contribute to the in vitro bioactivity and radioreceptor activity of the isoforms, but that hLH immunoactivity is independent of sialic acid content.

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van Kessel, K. P., J. A. van Strijp, and J. Verhoef. "Inactivation of recombinant human tumor necrosis factor-alpha by proteolytic enzymes released from stimulated human neutrophils." Journal of Immunology 147, no. 11 (December 1, 1991): 3862–68. http://dx.doi.org/10.4049/jimmunol.147.11.3862.

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Abstract Activated human neutrophils (PMN) degrade rTNF-alpha resulting in a loss of cytotoxic activity against murine L-929 cells (L cells). This inactivation is mediated through proteases released from activated PMN. Exposure of TNF to H2O2, glucose oxidase, xanthine oxidase, or myeloper-oxidase-H2O2-halide did not affect TNF cytotoxicity for L cells. Exposure to trypsin, chymotrypsin, pronase E, or elastase, however, did diminish TNF bioactivity. FMLP-stimulated PMN in the presence, but not in the absence, of cytochalasin B reduced TNF activity, whereas PMA-stimulated PMN did not affect TNF. Stimulation of PMN with opsonized bacteria also induced TNF inactivation as well as the supernatant of FMLP-stimulated cells. Addition of protease inhibitors to the FMLP-stimulated cytochalasin B-treated PMN abrogated the inactivation of TNF cytotoxicity for L cells, whereas scavengers were not protective. In addition, PMN from a chronic granulomatous disease patient also decreased TNF bioactivity. Inactivation of TNF by activated PMN correlated with granule release and not with superoxide production. Exposure of TNF to proteases and FMLP-activated PMN also resulted in a loss of reactivity with anti-TNF antibodies, as measured by ELISA, and in the formation of an approximately 10-kDa split product from the 17-kDa rTNF molecule. Partial degradation of TNF by proteases released from activated PMN may result in a diminished TNF bioactivity and thereby contribute to the regulation of local inflammatory reactions.

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Thakur, A. N., R. Coles, A. Sesay, B. Earley, H. S. Jacobs, and R. P. Ekins. "A rat granulosa cell plasminogen activator bioassay for FSH in human serum." Journal of Endocrinology 126, no. 1 (July 1990): 159–68. http://dx.doi.org/10.1677/joe.0.1260159.

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ABSTRACT A previously described in-vitro rat granulosa cell plasminogen activator bioassay for FSH has been modified and applied in the assay of human serum. This modified method consists of exposing the diethylstilboestrol-stimulated granulosa cells from 25- to 26-day-old rats to FSH or test substance for 3·5 h in wells coated with 125I-labelled fibrinogen and treated with thrombin. Following stimulation with FSH, the dose-related production of plasminogen activator was measured as the degree of 125I-labelled fibrinolysis in the presence of added plasminogen. Using the urinary FSH/LH bioassay reference preparation as the assay standard, the useful range of the assay was 0·3–15IU/l, with an assay sensitivity of 0·3 IU/l. As determined using purified glycoprotein hormone preparations, the assay was highly specific for FSH. The minor degree of FSH bioactivity measured in some of the hormone preparations was accounted for by the amount of FSH contamination in these preparations. To abolish interference caused by unknown serum factors, we heat-treated the serum samples for 15 min at 56 °C before the assay. The results indicated that neither immunoreactivity nor bioactivity was affected by this treatment. Furthermore, heat-treated human sera gave responses parallel to the standard curve at the three dose levels (2, 4 and 8 μl) studied. We used this bioassay to estimate the FSH-like bioactivity in 15 human serum samples. The estimates of immunoreactive FSH in these samples correlated well with the corresponding FSH bioactivity (r = 0·745, n = 15 and P < 0·05). The results indicate that with this sensitive and rapid (completed within 24 h) bioassay, it should be possible to measure FSH bioactivity in heat-treated human serum samples. Journal of Endocrinology (1990) 126, 159–168

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Namachivayam, Kopperuncholan, Hayley P. Coffing, Nehru Viji Sankaranarayanan, Yingzi Jin, Krishnan MohanKumar, Brandy L. Frost, Cynthia L. Blanco, et al. "Transforming growth factor-β2is sequestered in preterm human milk by chondroitin sulfate proteoglycans." American Journal of Physiology-Gastrointestinal and Liver Physiology 309, no. 3 (August 1, 2015): G171—G180. http://dx.doi.org/10.1152/ajpgi.00126.2015.

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Human milk contains biologically important amounts of transforming growth factor-β2isoform (TGF-β2), which is presumed to protect against inflammatory gut mucosal injury in the neonate. In preclinical models, enterally administered TGF-β2can protect against experimental necrotizing enterocolitis, an inflammatory bowel necrosis of premature infants. In this study, we investigated whether TGF-β bioactivity in human preterm milk could be enhanced for therapeutic purposes by adding recombinant TGF-β2(rTGF-β2) to milk prior to feeding. Milk-borne TGF-β bioactivity was measured by established luciferase reporter assays. Molecular interactions of TGF-β2were investigated by nondenaturing gel electrophoresis and immunoblots, computational molecular modeling, and affinity capillary electrophoresis. Addition of rTGF-β2(20–40 nM) to human preterm milk samples failed to increase TGF-β bioactivity in milk. Milk-borne TGF-β2was bound to chondroitin sulfate (CS) containing proteoglycan(s) such as biglycan, which are expressed in high concentrations in milk. Chondroitinase treatment of milk increased the bioactivity of both endogenous and rTGF-β2, and consequently, enhanced the ability of preterm milk to suppress LPS-induced NF-κB activation in macrophages. These findings provide a mechanism for the normally low bioavailability of milk-borne TGF-β2and identify chondroitinase digestion of milk as a potential therapeutic strategy to enhance the anti-inflammatory effects of preterm milk.

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Isigkeit, Laura, Apirat Chaikuad, and Daniel Merk. "A Consensus Compound/Bioactivity Dataset for Data-Driven Drug Design and Chemogenomics." Molecules 27, no. 8 (April 13, 2022): 2513. http://dx.doi.org/10.3390/molecules27082513.

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Publicly available compound and bioactivity databases provide an essential basis for data-driven applications in life-science research and drug design. By analyzing several bioactivity repositories, we discovered differences in compound and target coverage advocating the combined use of data from multiple sources. Using data from ChEMBL, PubChem, IUPHAR/BPS, BindingDB, and Probes & Drugs, we assembled a consensus dataset focusing on small molecules with bioactivity on human macromolecular targets. This allowed an improved coverage of compound space and targets, and an automated comparison and curation of structural and bioactivity data to reveal potentially erroneous entries and increase confidence. The consensus dataset comprised of more than 1.1 million compounds with over 10.9 million bioactivity data points with annotations on assay type and bioactivity confidence, providing a useful ensemble for computational applications in drug design and chemogenomics.

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Brugts, M. P., A. W. van den Beld, L. J. Hofland, K. van der Wansem, P. M. van Koetsveld, J. Frystyk, S. W. J. Lamberts, and J. A. M. J. L. Janssen. "Low Circulating Insulin-Like Growth Factor I Bioactivity in Elderly Men Is Associated with Increased Mortality." Journal of Clinical Endocrinology & Metabolism 93, no. 7 (July 1, 2008): 2515–22. http://dx.doi.org/10.1210/jc.2007-1633.

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Abstract Context: Low IGF-I signaling activity prolongs lifespan in certain animal models, but the precise role of IGF-I in human survival remains controversial. The IGF-I kinase receptor activation assay is a novel method for measuring IGF-I bioactivity in human serum. We speculated that determination of circulating IGF-I bioactivity is more informative than levels of immunoreactive IGF-I. Objective: Our objective was to study IGF-I bioactivity in relation to human survival. Design, Setting, and Study Participants: We conducted a prospective observational study at a clinical research center at a university hospital of 376 healthy elderly men (aged 73–94 yr). Main Outcome Measures: IGF-I bioactivity was determined by the IGF-I kinase receptor activation assay. Total and free IGF-I were determined by IGF-I immunoassays. Mortality was registered during follow-up (mean 82 months). Results: During the follow-up period of 8.6 yr, 170 men (45%) died. Survival of subjects in the highest quartile of IGF-I bioactivity was significantly better than in the lowest quartile, both in the total study group [hazard ratio (HR) = 1.8; 95% confidence interval (95% CI) = 1.2–2.8; P = 0.01] as well as in subgroups having a medical history of cardiovascular disease (HR = 2.4; 95% CI = 1.3–4.3; P = 0.003) or a high inflammatory risk profile (HR = 2.3; 95% CI = 1.2–4.5; P = 0.01). Significant relationships were not observed for total or free IGF-I. Conclusion: Our study suggests that a relatively high circulating IGF-I bioactivity in elderly men is associated with extended survival and with reduced cardiovascular risk.

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Maddox, Paul R., Derek L. Jones, and Robert E. Mansel. "Basal prolactin and total lactogenic hormone levels by microbioassay and immunoassay in normal human sera." Acta Endocrinologica 125, no. 6 (December 1991): 621–27. http://dx.doi.org/10.1530/acta.0.1250621.

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Abstract. The availability of an improved microbioassay for prolactin measurement has enabled comparison of lactogenic hormone bioactivity and immunoactivity in normal human serum. Serum was studied from 61 normal females and 15 normal males. The correlation of both assays was very close for all subjects with a mean ratio of bioassay to immunoassay of 1.5 (range 0.8-2.0) for prolactin and 1.4 (range 0.5-1.9) for total lactogenic hormone. There was no significant variation in prolactin or total lactogenic hormone values by microbioassay or immunoassay with sexual or menstrual status. Postmenopausal prolactin levels were lower by both assays compared with premenopausal values with a relative and absolute decrease in prolactin bioactivity with age. These findings indicate that there is a good correlation between prolactin bioactivity and immunoactivity in human serum.

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Xu, Fangfang, Kevin Yueju Wang, Nan Wang, Gangqiang Li, and Dehu Liu. "Bioactivity of a modified human Glucagon-like peptide-1." PLOS ONE 12, no. 2 (February 2, 2017): e0171601. http://dx.doi.org/10.1371/journal.pone.0171601.

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Funakoshi, Akihiro, Atsuo Jimi, Yohichi Yasunami, Kayoko Tateishi, Susumu Funakoshi, Hirokazu Tamamura, and Haruaki Yajima. "Bioactivity of human pancreastatin and its localization in pancreas." Biochemical and Biophysical Research Communications 159, no. 3 (March 1989): 913–18. http://dx.doi.org/10.1016/0006-291x(89)92195-5.

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Thornton, Catherine A., Judith A. Holloway, Janis K. Shute, John W. Holloway, Norma D. Diaper, and John O. Warner. "Human mid-gestation amniotic fluid contains interleukin-16 bioactivity." Immunology 126, no. 4 (April 2009): 543–51. http://dx.doi.org/10.1111/j.1365-2567.2008.02903.x.

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Swencki-Underwood, Bethany, Mark R. Cunningham, George A. Heavner, Cheryl Blasie, Stephen G. McCarthy, Tara Dougherty, Mike Brigham-Burke, George R. Gunn, Theresa J. Goletz, and Linda A. Snyder. "Engineering human IL-18 with increased bioactivity and bioavailability." Cytokine 34, no. 1-2 (April 21, 2006): 114–24. http://dx.doi.org/10.1016/j.cyto.2006.04.004.

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Rodgers, M., R. Mitchell, A. Lambert, N. Peers, and W. R. Robertson. "Human chorionic gonadotrophin contributes to the bioactivity of Pergonal." Clinical Endocrinology 37, no. 6 (December 1992): 558–64. http://dx.doi.org/10.1111/j.1365-2265.1992.tb01488.x.

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Gorinstein, >Shela, Abraham Caspi, Imanuel Libman, Hanna Leontowicz, Maria Leontowicz, Zev Tashma, Elena Katrich, Zenon Jastrzebski, and Simon Trakhtenberg. "Bioactivity of beer and its influence on human metabolism." International Journal of Food Sciences and Nutrition 58, no. 2 (January 2007): 94–107. http://dx.doi.org/10.1080/09637480601108661.

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Chizzonite, R., T. Truitt, F. J. Podlaski, A. G. Wolitzky, P. M. Quinn, P. Nunes, A. S. Stern, and M. K. Gately. "IL-12: monoclonal antibodies specific for the 40-kDa subunit block receptor binding and biologic activity on activated human lymphoblasts." Journal of Immunology 147, no. 5 (September 1, 1991): 1548–56. http://dx.doi.org/10.4049/jimmunol.147.5.1548.

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Abstract IL-12, formerly known as cytotoxic lymphocyte maturation factor, is a cytokine that stimulates proliferation of PHA-activated human peripheral blood lymphoblasts and synergizes with low concentrations of IL-2 in the induction of lymphokine-activated killer cells. IL-12 is a 75-kDa heterodimer composed of disulfide-bonded 40-kDa and 35-kDa subunits. mAb prepared against a partially purified preparation of natural IL-12 have been characterized by 1) immunoprecipitation of 125I-labeled IL-12, 2) immunodepletion of IL-12 bioactivity, 3) Western blotting of IL-12, 4) inhibition of [125I]IL-12 binding to its cellular receptor, and 5) neutralization of IL-12 bioactivity. Twenty antibodies immunoprecipitate 125I-labeled IL-12 and immunodeplete IL-12 bioactivity as assessed in the T cell proliferation and lymphokine-activated killer cell induction assays. Western blot analysis demonstrated that each antibody binds to the 75-kDa heterodimer and to the 40-kDa subunit. An IL-12R-binding assay identified 12 individual antibodies that inhibited the binding of [125I]IL-12 to its cellular receptor. Two inhibitory antibodies, 4A1 and 7B2, were tested in the neutralization assay and found to block IL-12 bioactivity whereas one noninhibitory antibody, 8E3, was shown not to neutralize IL-12 bioactivity. Antibodies 4A1 and 8E3 can simultaneously bind to the 75-kDa heterodimer demonstrating that inhibitory and noninhibitory epitopes are spatially distinct on the 40-kDa protein. The ability of antibodies specific for the 40-kDa subunit of IL-12 to block receptor binding of [125I]IL-12 and to neutralize IL-12 bioactivity suggests that localized determinants on the 40-kDa subunit may be necessary for binding to the IL-12 cellular receptor.

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Tan Timur, Ufuk, Marjolein Caron, Guus van den Akker, Anna van der Windt, Jenny Visser, Lodewijk van Rhijn, Harrie Weinans, Tim Welting, Pieter Emans, and Holger Jahr. "Increased TGF-β and BMP Levels and Improved Chondrocyte-Specific Marker Expression In Vitro under Cartilage-Specific Physiological Osmolarity." International Journal of Molecular Sciences 20, no. 4 (February 13, 2019): 795. http://dx.doi.org/10.3390/ijms20040795.

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During standard expansion culture (i.e., plasma osmolarity, 280 mOsm) human articular chondrocytes dedifferentiate, making them inappropriate for autologous chondrocyte implantation to treat cartilage defects. Increasing the osmolarity of culture media to physiological osmolarity levels of cartilage (i.e., 380 mOsm), increases collagen type II (COL2A1) expression of human articular chondrocytes in vitro, but the underlying molecular mechanism is not fully understood. We hypothesized that TGF-β superfamily signaling may drive expression of COL2A1 under physiological osmolarity culture conditions. Human articular chondrocytes were cultured in cytokine-free medium of 280 or 380 mOsm with or without siRNA mediated TGF-β2 knockdown (RNAi). Expression of TGF-β isoforms, and collagen type II was evaluated by RT-qPCR and immunoblotting. TGF-β2 protein secretion was evaluated using ELISA and TGF-β bioactivity was determined using an established reporter assay. Involvement of BMP signaling was investigated by culturing human articular chondrocytes in the presence or absence of BMP inhibitor dorsomorphin and BMP bioactivity was determined using an established reporter assay. Physiological cartilage osmolarity (i.e., physosmolarity) most prominently increased TGF-β2 mRNA expression and protein secretion as well as TGF-β bioactivity. Upon TGF-β2 isoform-specific knockdown, gene expression of chondrocyte marker COL2A1 was induced. TGF-β2 RNAi under physosmolarity enhanced TGF-β bioactivity. BMP bioactivity increased upon physosmotic treatment, but was not related to TGF-β2 RNAi. In contrast, dorsomorphin inhibited COL2A1 mRNA expression in human articular chondrocytes independent of the osmotic condition. Our data suggest a role for TGF-β superfamily member signaling in physosmolarity-induced mRNA expression of collagen type II. As physosmotic conditions favor the expression of COL2A1 independent of our manipulations, contribution of other metabolic, post-transcriptional or epigenetic factors cannot be excluded in the underlying complex and interdependent regulation of marker gene expression. Dissecting these molecular mechanisms holds potential to further improve future cell-based chondral repair strategies.

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Mestieri, Leticia Boldrin, Ana Lívia Gomes-Cornélio, Elisandra Márcia Rodrigues, Gisele Faria, Juliane Maria Guerreiro-Tanomaru, and Mário Tanomaru-Filho. "Cytotoxicity and Bioactivity of Calcium Silicate Cements Combined with Niobium Oxide in Different Cell Lines." Brazilian Dental Journal 28, no. 1 (February 2017): 65–71. http://dx.doi.org/10.1590/0103-6440201700525.

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Abstract The aim of this study was to evaluate the cytotoxicity and bioactivity of calcium silicate-based cements combined with niobium oxide (Nb2O5) micro and nanoparticles, comparing the response in different cell lines. This evaluation used four cell lines: two primary cultures (human dental pulp cells - hDPCs and human dental follicle cells - hDFCs) and two immortalized cultures (human osteoblast-like cells - Saos-2 and mouse periodontal ligament cells - mPDL). The tested materials were: White Portland Cement (PC), mineral trioxide aggregate (MTA), white Portland cement combined with microparticles (PC/Nb2O5µ) or nanoparticles (PC/Nb2O5n) of niobium oxide (Nb2O5). Cytotoxicity was evaluated by the methylthiazolyldiphenyl-tetrazolium bromide (MTT) and trypan blue exclusion assays and bioactivity by alkaline phosphatase (ALP) enzyme activity. Results were analyzed by ANOVA and Tukey test (a=0.05). PC/Nb2O5n presented similar or higher cell viability than PC/Nb2O5µ in all cell lines. Moreover, the materials presented similar or higher cell viability than MTA. Saos-2 exhibited high ALP activity, highlighting PC/Nb2O5µ material at 7 days of exposure. In conclusion, calcium silicate cements combined with micro and nanoparticles of Nb2O5 presented cytocompatibility and bioactivity, demonstrating the potential of Nb2O5 as an alternative radiopacifier agent for these cements. The different cell lines had similar response to cytotoxicity evaluation of calcium silicate cements. However, bioactivity was more accurately detected in human osteoblast-like cell line, Saos-2.

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Weng, Jie, Bo Feng, Min Wang, and Xing Dong Zhang. "Nucleation and Growth of Bone-Like Apatite on Surfaces of Metals, Ceramics and Polymers in Simulated Body Fluids." Key Engineering Materials 288-289 (June 2005): 277–80. http://dx.doi.org/10.4028/www.scientific.net/kem.288-289.277.

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The biomimetic approach of mineralization in vitro is adopted to investigate systematically the nucleation and growth of bone-like apatite on the surface of biomaterials such as bioceramics, metals and polymers, and those chemically surface-treated. The simulated environment is kept isothermic at the human body temperature of 36.5C with three kinds of simulated physiological fluids. The experimental results show that (1) inherent properties of biomaterials determine their bioactivity and the different crystalline structure of same materials results in the difference in bioactivity; (2) the bioactivity can effectively be improved by the surface treatment of biomaterials via chemical methods and by the addition of bioactive particles in a polymer matrix; (3) the bone-like apatite, nucleated and grown in the simulated body fluid with the same ion concentrations to that of the human plasma, possesses the same composition, structure and morphology despite of matrixes; (4) the difference in bioactivity with biomaterials is indicated by the different time for bone-like apatite to nucleate and to grow on their surfaces.

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Abbott, Glenn L., Xing Wu, Zhufeng Zhao, Lei Guo, Vladimir B. Birman, Brian B. Hasinoff, and Gary I. Dmitrienko. "Prekinamycin and an isosteric-isoelectronic analogue exhibit comparable cytotoxicity towards K562 human leukemia cells." Med. Chem. Commun. 5, no. 9 (2014): 1364–70. http://dx.doi.org/10.1039/c4md00197d.

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Waddell, B. J., and P. J. Burton. "Release of bioactive ACTH by perifused human placenta at early and late gestation." Journal of Endocrinology 136, no. 2 (February 1993): 345–53. http://dx.doi.org/10.1677/joe.0.1360345.

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ABSTRACT This study assessed whether bioactive ACTH is released by the human placenta during perifusion in vitro at early and late gestation. Human placental villous fragments from early (8–12 weeks) and late (38–40 weeks) gestation were perifused at a constant rate for 6·5 h. To assess ACTH-like bioactivity released by this tissue, the perifusion effluent was redirected through adjacent chambers containing freshly dispersed adrenocortical cells obtained from adult rats. Baseline secretion of corticosterone by these adrenocortical cells averaged 95±26 (s.e.m.) fmol/min, and this increased at least fivefold (P <0·01, two-way ANOVA) in response to placental effluent at early and late gestation. The magnitude of this increase, expressed as a percentage of the maximal response to a subsequent stimulus with ACTH(1–24), was similar for placentas obtained at early (41 ± 12% of maximal response) and late (42 ± 17%) gestation. Immunoreactive (I)-ACTH was readily detectable in placental effluent from all preparations (5·5±2·3 fmol/min per g tissue), and there was no apparent difference with stage of gestation. To determine whether all of the ACTH-like bioactivity released by the placenta was attributable to I-ACTH, a second series of placental/adrenal perifusions was conducted. In these, I-ACTH was selectively removed from placental effluent by immunoneutralization, and the residual bioactivity measured. Immunoneutralization involved preincubation of placental effluent with ACTH antiserum (1:100), and preincubation with normal rabbit serum (NRS) served as a control. Preincubation with ACTH antiserum, but not with NRS, resulted in a marked reduction in ACTH-like bioactivity present in placental effluent at both early (P <0·01, paired t-test) and late (P <0·05) gestation. This inhibition was significantly more effective (P <0·05, unpaired t-test) at early than at late gestation. Overall, these data establish that the human placenta can release bioactive ACTH-like activity at both early and late gestation, and that much, but not all, of this bioactivity is directly attributable to I-ACTH. These findings clearly demonstrate a potential role for placental ACTH in directly influencing the maternal and/or fetal hypothalamic-pituitary-adrenal axes during human pregnancy. Journal of Endocrinology (1993) 136, 345–353

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HUBER, GEROLD K., PO FONG, ERLINDA S. CONCEPCION, and TERRY F. DAVIES. "Recombinant Human Thyroid-Stimulating Hormone: Initial Bioactivity Assessment using Human Fetal Thyroid Cells*." Journal of Clinical Endocrinology & Metabolism 72, no. 6 (June 1991): 1328–31. http://dx.doi.org/10.1210/jcem-72-6-1328.

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Dattani, M. T., P. C. Hindmarsh, C. G. D. Brook, I. C. A. F. Robinson, and N. J. Marshall. "Inhibition of growth hormone bioactivity by recombinant human growth hormone-binding protein in the eluted stain assay system." Journal of Endocrinology 140, no. 3 (March 1994): 445–53. http://dx.doi.org/10.1677/joe.0.1400445.

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Abstract The effects of a recombinant human GH-binding protein (rhGHBP; amino acids 1–238) on GH stimulation of rat Nb2 lymphoma cells were examined with an eluted stain assay system (ESTA). This precise bioassay utilizes the colorimetric reduction by stimulated Nb2 cells of a yellow tetrazolium salt (3-[4,5-dimethyl-thiazol-2-yl]-2,5-diphenyl-tetrazolium bromide) to a purple formazan as its end-point. The use of a lactogenic bioassay allowed the investigation of hGHBP specificity for human GH (hGH) as opposed to prolactin. rhGHBP inhibited pituitary hGH bioactivity in a dose-dependent manner. No significant inhibition of prolactin or ACTH bioactivity occurred. It was confirmed that recombinant 20 kDa hGH also stimulated the Nb2 cells and that its relative potency was ∼ 10% of that of pituitary-derived hGH. Stimulation by 20 kDa hGH was also inhibited by rhGHBP. The highly quantitative ESTA system demonstrated that the binding protein inhibited in a competitive manner. hGH activation of the Nb2 cells did not appear to be governed by a Michaelian first-order reaction. As might then be anticipated, the concentration of rhGHBP required for 50% inhibition of GH bioactivity (IC50) changed with agonist concentrations for both 20 kDa and 22 kDa hGH. However, with equimolar concentrations of these two isohormones, the IC50 of the binding protein was virtually identical. Potentiation of hGH bioactivity in vivo by low concentrations of hGHBP has been reported but was not observed in our in vitro system when tested over a wide range of binding protein concentrations. In conclusion, the ESTA bioassay system permitted a detailed characterization of the inhibition of hGH bioactivity by rhGHBP. The hormonal specificity confirms earlier radioligand binding studies, except that we found that the 20 kDa hGH variant interacts with the rhGHBP. Journal of Endocrinology (1994) 140, 445–453

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Zhang, Yang-De. "Expression, purification and bioactivity of human augmenter of liver regeneration." World Journal of Gastroenterology 12, no. 27 (2006): 4401. http://dx.doi.org/10.3748/wjg.v12.i27.4401.

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Hassan, Mohamed, Razina Rouf, Evelin Tiralongo, Tom May, and Joe Tiralongo. "Mushroom Lectins: Specificity, Structure and Bioactivity Relevant to Human Disease." International Journal of Molecular Sciences 16, no. 12 (April 8, 2015): 7802–38. http://dx.doi.org/10.3390/ijms16047802.

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Zhang, Wenrui. "Bioactivity Applications of Lycium Barbarum Polysaccharide In Regulating Human Health." Highlights in Science, Engineering and Technology 11 (August 23, 2022): 152–57. http://dx.doi.org/10.54097/hset.v11i.1362.

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For approximately 2,000 years, Lycium barbarum was regarding as a traditional medicine, and was believed that Wolfberry can nourish the liver, eyes, and kidneys. The fruit of Goji berries can also be eaten as food, and these berries have various biological importance, its anti-inflammatory, antioxidant, anti-tumor, hypoglycemic, hypolipidemic and anti-aging effects were discovered. Among those bioactive components, the most important one is Lycium Barbarum polysaccharide (LBP). LBP main structures include β-(1→3)-galp, α-(1→4)-galA, α-(1→6)-glc, β-(1→6)-galp, β-(1→4)-galp, and α-(1→5)-ara. There are various ways in which LBP is extracted. Various studies have demonstrated that LBP possess various biological activities. The main activities of LBP are anti-oxidation, anti-cancer and metabolic regulation. It can also be used in nerve damage repair, liver protection and eye protection. In this article, the structure of LBP and its medicinal value will be summarized as a reference for its further applications.

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Ehret, D. L. "Phytochemicals in human health research: Bioactivity versus physiological relevance – Preface." Canadian Journal of Plant Science 86, no. 3 (July 7, 2006): 763. http://dx.doi.org/10.4141/p05-249.

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Andrews, Allison-Lynn, Neil V. McFerran, and John Nelson. "Bioactivity of B-Loop mutants of human Epidermal Growth Factor." Biochemical Society Transactions 28, no. 5 (October 1, 2000): A444. http://dx.doi.org/10.1042/bst028a444c.

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Tanaka, T., S. Umezawa, H. Yano, I. Hibi, Y. Shishiba, A. Teramoto, E. Ishikawa, and Y. Murakami. "Bioactivity of Human Growth Hormone in Urine from Acromegalic Patients." Hormone and Metabolic Research 21, no. 06 (June 1989): 324–27. http://dx.doi.org/10.1055/s-2007-1009226.

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Chang, Yi, Wei-Fan Chen, Kuan-Hung Lin, Cheng-Ying Hsieh, Duen-Suey Chou, Li-Jyun Lin, Joen-Rong Sheu, and Chao-Chien Chang. "Novel Bioactivity of Ellagic Acid in Inhibiting Human Platelet Activation." Evidence-Based Complementary and Alternative Medicine 2013 (2013): 1–9. http://dx.doi.org/10.1155/2013/595128.

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Pomegranates are widely consumed either as fresh fruit or in beverage form as juice and wine. Ellagic acid possesses potent antioxidative properties; it is known to be an effective phytotherapeutic agent with antimutagenic and anticarcinogenic qualities. Ellagic acid (20 to 80 μM) exhibited a potent activity in inhibiting platelet aggregation stimulated by collagen; however, it did not inhibit platelet aggregation stimulated by thrombin, arachidonic acid, or U46619. Treatment with ellagic acid (50 and 80 μM) significantly inhibited platelet activation stimulated by collagen; this alteration was accompanied by the inhibition of relative[Ca2+]imobilization, and the phosphorylation of phospholipase C (PLC)γ2, protein kinase C (PKC), mitogen-activated protein kinases (MAPKs), and Akt, as well as hydroxyl radical (OH●) formation. In addition, ellagic acid also inhibited p38 MAPK and Akt phosphorylation stimulated by hydrogen peroxide. By contrast, ellagic acid did not significantly affect PKC activation and platelet aggregation stimulated by PDBu. This study is the first to show that, in addition to being considered a possible agent for preventing tumor growth, ellagic acid possesses potent antiplatelet properties. It appears to initially inhibit the PLCγ2-PKC cascade and/or hydroxyl radical formation, followed by decreased phosphorylation of MAPKs and Akt, ultimately inhibiting platelet aggregation.

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Raivio, T. "Novel Assay for Determination of Androgen Bioactivity in Human Serum." Journal of Clinical Endocrinology & Metabolism 86, no. 4 (April 1, 2001): 1539–44. http://dx.doi.org/10.1210/jc.86.4.1539.

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Horikawa, K., H. Nakakuma, S. Nagakura, M. Kawakita, T. Kagimoto, M. Iwamori, Y. Nagai, T. Abe, and K. Takatsuki. "Hemolysis of human erythrocytes is a new bioactivity of gangliosides." Journal of Experimental Medicine 174, no. 6 (December 1, 1991): 1385–91. http://dx.doi.org/10.1084/jem.174.6.1385.

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Using sheep erythrocytes and liposomes, an inhibitory effect of gangliosides has been shown on the activation of the alternative pathway of complement. However, in studies using human erythrocytes, we found that gangliosides had hemolytic activity that was possibly mediated through activation of the alternative pathway. Pretreatment of human erythrocytes obtained from healthy volunteers or paroxysmal nocturnal hemoglobinuria (PNH) patients with a ganglioside mixture purified from human erythrocytes enhanced their susceptibility to homologous human complement, and resulted in dose-dependent hemolysis. The enhancement was more marked in PNH erythrocytes than control cells. Protease treatment of the ganglioside mixture did not change its hemolytic activity, but sialidase treatment abolished the activity. Among the major erythrocyte gangliosides, II3NeuAc-LacCer (GM3) was the most potent hemolytic agent. Gangliosides purified from bovine brain were also active, while neither nonsialylated glycosphingolipids, the ceramide moiety, or sialic acid alone were active. Sialic acid residues in the ganglioside molecules were essential to this activity, but the amount of the residue or the source of the gangliosides seemed not to be important. Several treatments inhibiting the alternative but not classical complement pathway markedly reduced the ganglioside hemolytic activity. This novel bioactivity of gangliosides was thus suggested to be mediated partly by activation of the alternative pathway.

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Weinberg, David S., Jieru E. Lin, Nathan R. Foster, Gary Della'Zanna, Asad Umar, Drew Seisler, Walter K. Kraft, et al. "Bioactivity of Oral Linaclotide in Human Colorectum for Cancer Chemoprevention." Cancer Prevention Research 10, no. 6 (April 10, 2017): 345–54. http://dx.doi.org/10.1158/1940-6207.capr-16-0286.

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Raivio, Taneli, Jorma J. Palvimo, Leo Dunkel, Sanna Wickman, and Olli A. Jänne. "Novel Assay for Determination of Androgen Bioactivity in Human Serum1." Journal of Clinical Endocrinology & Metabolism 86, no. 4 (March 1, 2001): 1539–44. http://dx.doi.org/10.1210/jcem.86.4.7329.

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Raivio, Taneli, Jorma J. Palvimo, Senja Kannisto, Raimo Voutilainen, and Olli A. Jänne. "Transactivation Assay for Determination of Glucocorticoid Bioactivity in Human Serum." Journal of Clinical Endocrinology & Metabolism 87, no. 8 (August 1, 2002): 3740–44. http://dx.doi.org/10.1210/jcem.87.8.8729.

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Journal articles on the topic 'Human bioactivity'

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