Biomedical subjects
Publications and source records attributed to J Spiess.
IgE-antibodies against venoms and wholebody extracts of bees and wasps and hemagglutinins against phospholipase A were determined in patients with allergy to insect stings before and during hyposensitization therapy. The results show that venoms are superior to wholebody extracts for diagnosis and therapy of insect sting allergy.
The previously developed two-step method using soluble polystyrene sulfonate-Na for the detection of allergic reactions to small molecular drugs has been replaced by a one-step method using particles of the same substance. The new method is simpler to perform. Particulate polystyrene sulfonate is commercially available. The drug is added in increasing concentrations to diluted serum samples and the light scattering is measured with a highly sensitive nephelometer. Both the specific serum factor in the patient's serum (globulins) and the non-specific factor contained in most fresh human sera are particularly labile.
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Specific IgE-antibodies and haemagglutinins to bee venom were determined in fifty-five bee sting allergic patients, fifty-seven bee keepers and fifty-two blood donors without evident allergy to hymenoptera stings. IgE-antibodies were detected by RAST in 70% of allergic patients, 40% of bee keepers and 12% of blood donors. Most bee keepers with detectable IgE-antibodies to bee venom recorded severe local or even general reactions to bee stings. Most blood donors with detectable specific IgE had been stung by hymenoptera in the past. High titres of haemagglutinating antibodies against phospholipase A were found in most bee keepers, occasionally in bee sting allergic patients but only rarely in blood donors. The determination of specific IgE-antibodies to insect venoms by RAST seems to be a valuable method for the diagnosis of hymenoptera sting allergy.
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The importance of the hypothalamus in the regulation of growth hormone (GH) secretion from the adenohypophysis has been supported by experimental and clinical evidence. It has been observed that GH secretion is in part controlled by hypothalamic GH release-inhibiting factors, two forms of which, somatostatin-14 (ref. 5) and somatostatin-28 (refs 6-9), have been characterized. Peptides with GH-releasing activity were recently purified from two human pancreatic tumours of acromegalic patients and characterized. Synthetic versions of these human pancreatic tumour GH-releasing factors (hpGRFs) were found to be potent GH secretagogues in vitro and in vivo and to exhibit actions and interactions similar to those observed with partially purified hypothalamic GRF. GH-releasing peptides have been purified from hypothalami of various species but the structure of natural hypothalamic GRF has not yet been reported. We now describe the purification, sequence analysis and synthesis of a 43-residue polypeptide isolated from rat hypothalamic extracts on the basis of its ability to stimulate GH secretion from cultured rat adenohypophyseal cells. The native polypeptide and its synthetic replicate do not differ significantly in their biological potencies and intrinsic activities. We propose that this polypeptide, which shows 67% homology with the corresponding N-terminal 43 residues in hpGRF-44, is the long-sought rat hypothalamic GRF (rhGRF).
A variety of hypophysiotropic peptides or proteins have been reported to be present in mammalian gonads. Inhibin, a hormone that under most circumstances selectively suppresses the secretion of follicle-stimulating hormone (FSH) but not luteinizing hormone (LH), has been isolated from the gonadal fluids of several species and characterized as a heterodimeric protein consisting of alpha- and beta-polypeptides associated by disulphide bonds. The complete amino-acid sequences of the precursors of porcine and human inhibin alpha-subunits and two distinct porcine inhibin beta-subunits (beta A and beta B) have been deduced from complementary DNA sequences. Gonadotropin releasing peptides have also been found in the gonad and have generally been shown to be active in radioreceptor assays for gonadotropin releasing hormone (GnRH) but to exhibit different chromatographic and immunological characteristics from those of GnRH. During our purification of inhibin from porcine follicular fluid, we noted fractions that could stimulate the secretion of FSH by cultured anterior pituitary cells. We report here the purification of an FSH releasing protein (FRP) and its characterization by SDS-polyacrylamide gel electrophoresis under non-reducing and reducing conditions and by partial sequence analysis. Our results indicate that porcine gonadal FRP is a homodimer consisting of two inhibin beta A-chains linked by disulphide bonds. FRP is highly potent (50% effective concentration (EC50) approximately 25 pM) in stimulating the secretion and biosynthesis of FSH but not of LH or any other pituitary hormone. In contrast to the effects of GnRH and other reported gonadal gonadotropin releasing fractions, the action of FRP is not mediated by GnRH receptors.