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Biomedical subjects

B B Aggarwal

Publications and source records attributed to B B Aggarwal.

214 records · Page 12Linked to original sources
PubMed1980

Purification and characterization of the gonadotropin secreted by cultured horse trophoblast cells.

Equine chorionic gonadotropin (eCG) secreted by horse trophoblast cells cultivated in vitro was isolated and its chemical, immunochemical, and biological characteristics were compared to those of the gonadotropin secreted in vivo and isolated from PMS. It was also compared with eCG isolated from the tissue of origin, the endometrial cups. The gonadotropin secreted in vitro had a smaller molecular size, contained appreciably less carbohydrate, and showed different amino-terminal residues from that secreted in vivo. In addition, there were significant differences in amino acid composition between eCG secreted in vivo and that secreted in vitro. The reactivity of eCG (isolated from the medium of cultured trophoblast cells) in homologous eCG (isolated from PMS) and equine LH and FSH RIAs suggested close antigenic similarities to eCG isolated from PMS. However, compared to serum-derived eCG, eCG secreted in vitro showed reduced activity in both LH (13%) and FSH (9-24%) bioassays and in LH and FSH radioreceptor assays (40-50%). The differences in bioassay potencies may be accounted for in part by the lower sialic acid content of the gonadotropin secreted in vitro. With respect to both bioactivity and chemical composition, the eCG secreted in vitro more closely resembled the eCG isolated from endometrial cups than that isolated from serum.

Amino Acids↗
PubMed1980

Purification and characterization of donkey chorionic gonadotrophin.

Serum of the pregnant donkey, like that of the mare, contains a gonadotrophin of chorionic origin. The chorionic gonaditrophin of the donkey (dCG) has been isolated in purified form from the serum of pregnant donkeys using methodology previously employed for the purification of pregnant mare chorionic gonadotrophin (eCG). Unlike eCG, dCG is predominatly an LH in biological tests. In the in-vitro rat Leydig cell assay, dCG was as active as eCG, but in the in-vitro rat seminiferous tubule assay for FSH and in the augmentation assay, dCG was considerably less potent than eCG (1-10%). Specific rat testis radioreceptor assays for LH and FSH also showed dCG to be at least nine times more potent in LH than in FSH activity. Chemically, dCG was found to be similar to eCG in fractionation behaviour and glycoprotein nature. However, dCG had significantly less carbohydrate (31%) than had eCG (45%) and several differences were noted in a comparison of amino-acid compositions. A single amino-terminal residue, phenylalanine, was detected in dCG. Immunologically, dCG cross-reacted in homologous radio-immunoassays for eCG, equine LH and equine FSH, but its inhibition curves were all nonparallel with those of the respective equine gonadotrophin standards.

Amino Acids↗
PubMed1979

Biological and binding activities of equine pituitary gonadotrophins and pregnant mare serum gonadotrophin.

The biological and binding activities of pregnant mare serum gonadotrophin (PMSG) were compared with those of highly purified FSH and LH from the pituitary gland of the same species. Pregnant mare serum gonadotrophin showed activity in bioassays considered to be specific for both FSH (e.g. the Steelman-Pohley ovarian augmentation test and cyclic AMP production by rat seminiferous tubules) and LH(androgen production by rat Leydig cells), as well as activity in a variety of radioreceptor assay systems previously considered to be specific for one of the two types of gonadotrophin. The potency of PMSG was high compared with that of purified ovine FSH or LH standards in all assays but PMSG was considerably less active than equine FSH and LH in vitro. In radioreceptor assays employing rat, pig and horse tissues, the activity of PMSG was equivalent to only 1--5% of equine FSH in competing for FSH-binding sites and only 3--35% of equine LH in competing for LH-binding sites. Pregnant mare serum gonadotrophin was least active in homologous binding assays with horse testis and equine LH as radioligand. In the rat Leydig cell bioassay, the activity of PMSG was only 2.0% that of equine LH. Furthermore, in some assays equine LH was found to resemble PMSG in exhibiting a high degree of FSH-like activity that could not be accounted for by cross-contamination. The FSH immunoactivity of equine LH was less than 0.5% that of equine FSH, but equine LH was up to 63% as potent as equine FSH in competition for FSH-binding sites and it was 20% as active in the Steelman-Pohley ovarian augmentation bioassay. Equine LH did not, however, show the expected activity in the cyclic AMP production bioassay. Thus, the FSH-binding sites and physiological receptors may not be identical. Overall, comparison of PMSG with pituitary gonadotrophins from homologous species shows that the apparent dual activity of PMSG may not be a unique feature of this pregnancy hormone since equine LH also exhibits some FSH activities. The chemical resemblance between PMSG and equine LH is noteworthy in this regard.

Animals↗
PubMed1978

Damage to mitochondrial electron transport and energy coupling by visible light.

The effect of treating mitochondria with visible light above 400 nm on electron transport and coupled reactions was examined. The temporal sequence of changes was: stimulation of respiration coupled to ATP synthesis, a decline in ATP synthesis, inactivation of respiration, increased ATPase activity and, later, loss of the membrane potential. Loss of respiration was principally due to inactivation of dehydrogenases. Of the components of dehydrogenase systems, flavins and quinones were most susceptible to illumination, the iron-sulfur centers were remarkably resistant to being damaged. Succinate dehydrogenase was inactivated before choline and NADH dehydrogenase. Redox reactions of cytochromes and cytochrome c oxidase activity were unaffected. Inactivation was O2-dependent and prevented by anaerobiosis or the presence of substrates for the dehydrogenases. Light in the range 400-500 nm was most effective and the presence of free flavins greatly enhanced inactivation of all of the above mitochondrial activities. This suggests that visible light mediates a flavin-photosensitized reaction that initiates damage involving participation of an activated species of oxygen in the damage propagation.

Animals↗
PubMedDate not supplied

Optimum needle length for DPT inoculation of Indian infants.

Correct placement of the injected DPT vaccine into the deep muscular layers decreases the local reactions, including the sterile abscess formation. However, recommendations on size of the needle to be used and the angle of injection are not easily available, are not uniform and are based on case reports. The only study based on scientific data of ultrasonographic measurement of fat layer and muscle layer thickness of thigh of only 24 infants of 4 months age covers only American children. (Hick et al, Pediatrics 1989; 84: 136-37). In the present study, we have produced similar data on 215 Indian children belonging to all those age groups in which DPT vaccinations are given. Mean thickness of skin + fat layer in the middle one-third of the anterolateral aspect of thigh was 1.03 +/- 0.23 cm, 1.04 +/- 0.21 cm, 0.95 +/- 0.19 cm and 1.06 +/- 0.27 cm in the age groups of 6-12 weeks (Groups I), 13-18 weeks (Group II), 19-24 weeks (Groups III) and 18 +/- 1 month (Group IV) respectively. These age groups correspond to the timings of first 3 primary doses and the first booster dose of the DPT vaccine in our immunization clinic. Mean thickness of all the soft tissues together at the same site were 1.87 +/- 0.35, 2.17 +/- 0.38, 2.07 +/- 0.39 and 2.07 +/- 0.26 cm respectively for the groups I to IV.(ABSTRACT TRUNCATED AT 250 WORDS)

Developing Countries↗
PubMedDate not supplied

Increased lymphotoxin in human malarial serum, and the ability of this cytokine to increase plasma interleukin-6 and cause hypoglycaemia in mice: implications for malarial pathology.

The origin of illness and pathology in malaria is now largely attributed to high levels of circulating tumour necrosis factor (TNF), released from cells of macrophage lineage after triggering by the products of malarial schizogony. The role of lymphocytes and their products in malarial pathology is not yet known. This paper reports the presence of a related cytokine, lymphotoxin, which is produced only by lymphocytes, in the serum of malarial patients. This is the first report of raised serum levels of lymphotoxin in a systemic disease state. When injected into mice, recombinant human lymphotoxin induced hypoglycaemia and increased serum levels of interleukin-6. These changes, which are seen in severe experimental and human malaria, were also provoked by TNF. Both of these cytokines acted synergistically with interleukin-1, which has also been reported to be raised in malaria, to produce these alterations. These observations imply that lymphotoxin, as well as TNF, may contribute to the hypoglycaemia and raised serum interleukin-6 observed in malaria. This reduces the likelihood of effectively blocking the pathology of this disease by the use of neutralizing antibody directed against just one member of this family of functionally overlapping mediators.

Adolescent↗
PubMedDate not supplied

Human tumour necrosis factor: precursor structure, expression and homology to lymphotoxin.

Human tumour necrosis factor has about 30% homology in its amino acid sequence with lymphotoxin, a lymphokine that has similar biological properties. Recombinant tumour necrosis factor can be obtained by expression of its complementary DNA in Escherichia coli and induces the haemorrhagic necrosis of transplanted methylcholanthrene-induced sarcomas in syngeneic mice.

Amino Acid Sequence↗
PubMedDate not supplied

Characterization of receptors for human tumour necrosis factor and their regulation by gamma-interferon.

Tumour necrosis factors, TNF-alpha and TNF-beta (previously called lymphotoxin), are the products of activated monocytes and lymphocytes, respectively, and both have recently been purified, sequenced and cloned by recombinant DNA methods, revealing 35% identity and 50% homology in the amino-acid sequence. Both proteins have been found to be specifically toxic to many tumour cells. Furthermore, it has been reported that various interferons are synergistic with TNF for anti-tumour effects in vitro, while activities attributed to the two proteins have also been shown to necrotize various tumours in vivo. We have now prepared 125I-labelled highly purified recombinant human TNF-alpha to study in detail its binding to the human cervical carcinoma cell line ME-180. Our results indicate that there is a single class of specific high-affinity receptors for TNF on this cell line which has a Kd of about 0.2 nM and an average of 2,000 receptor sites per cell. The binding of labelled TNF-alpha to these cells can be inhibited by both TNF-alpha and TNF-beta but not by gamma-interferon (IFN-gamma). However, preincubation of cells with IFN-gamma increases the total number of TNF receptors two to threefold without any significant change in the affinity constant. This is the first report that TNF-alpha and -beta share a common receptor and that the receptors can be up-regulated by interferon. Our results may explain previous observations regarding similar biological activities observed for these two cytotoxic proteins and also their synergistic action with interferons.

Cell Line↗