Evidence for opiate receptors on pituicytes

A hypothalamo-neurohypophyseal enkephalinergic pathway has been described and the pars nervosa of the rat pituitary contains enkephalin-like material which may coexist in vasopressin and oxytocin terminals. At the level of the pars nervosa itself, stereospecific opiate receptors with properties very similar to those of brain receptors have been described, and opiates have been shown to inhibit the release of both vasopressin and oxytocin. The location of the opiate receptors involved has been presumed to be pre-terminal on the neurosecretory fibres. Using an autoradiographic technique to visualize opiate receptors, however, we now report that destruction of the neurosecretory fibres following pituitary stalk section does not result in a significant change in the neural lobe opiate receptor population. This suggests that the opiate receptors within the neural lobe may be present on pituicytes rather than on neurosecretory fibres.     

Effects on the early development of the pearl sac by cytochrome c, yolk lecithin and polyvinyplyrro

Mantle pieces ofHyriopisis cumingii was treated by three kinds of solution, These mantle pieces were inserted together with paraffin nucleuses into the connective tissue of three groups ofHyriopisis cumingii. These operated animals were cultured in a pool for a month. Several pearl sacs were put out and immersed by Bouin's solution after every five days. Sections of each animals were made by histological method. Those without treatment were in a control group. Observations of these sections showed that cytochrome c and yolk lecithin have an accelerated roles on pearl sac development and pearl layer secretion. No effects on pearl sac development by polyvinyplyrrolidone (PVP). Zheng Junying:born in May, 1966, Lecturer     

Evidence for two populations of excitatory receptors for noradrenaline on arteriolar smooth muscle

We have recorded the responses of arteriolar smooth muscle cells to iontophoretically applied noradrenaline. Records of both muscle movement and muscle membrane potential were made. We found that two distinct types of response could be detected, depending on the position of the noradrenaline micropipette. One type of response consisted of a localised constriction near the noradrenaline source: this effect could be abolished by the alpha-antagonist phentolamine and was not associated with a change in arteriolar membrane potential. The other type of response was a depolarisation similar to the excitatory junction potentials (e.j.ps) produced by sumpathetic nerve stimulation. These observations suggest that there are two populations of receptors for noradrenaline on arterioles, and could explain the paradoxical failure of alpha-antagonists to block neuromuscular transmission at some sutonomic end organs such as the vas deferens, arteries and arterioles.     

Detection of CD2 expression in chicken hematogenic embryo yolk sac lymphoid cells prior to thymus genesis

Lymphoid mononuclear cells from chick embryos at stage 16 were collected prior to fetal liver and thymus genesis to study the differentiation and function of the hematogenic yolk sac and to detect whether CD2 occurs on the surface of lymphoid mononuclear cells. The phenotype and functional activity of the cell surface protein E receptor and the ultrastructure of embryonic E＋ cells were compared with those of mature T cells. Our results indicate 99.36% homology between the E receptors of embryonic lymphocytes and mature T cells. Other similarities, including molecular distribution, motivation, the ability to form an erythrocyte rosette, the structure of the receptor-ligand complex, and the conformation of the signal channel, were detected between embryonic lymphocytes and mature CD2-expressing T cells. These results indicate that CD2 is already expressed prior to fetal liver and thymus genesis and that its expression is not dependent on the thymic microenvironment.     

Evidence for the bilobal nature of diferric rabbit plasma transferrin.

Plasma transferrin is involved in iron transport within the circulatory system of vertebrates, and provides an iron source for haemoglobin synthesis and other metabolic requirements. However, despite extensive studies by spectroscopic, biochemical and physiological techniques, the nature of iron binding and the mechanisms of uptake and release of iron are not fully understood. Plasma transferrins are monomeric glycoproteins with a molecular weight of approximately 80,000 (ref. 2); they have two similar and very strong binding sites for Fe(III), together with two associated anion binding sites. Fragmentation studies on various transferrins have shown that the polypeptide chain is composed of two domains formed from the N-terminal and C-terminal halves of the polypeptide chain. Each domain contains one metal binding site. The marked sequence similarities which exist between the two halves may reflect a doubling of an ancestral structural gene during the phylogenetic development of the protein. Preliminary crystallographic investigations of diferric rabbit plasma transferrin have been reported from this laboratory. We now report initial studies of the X-ray structure determination of dife-ric rabbit plasma transferrin which have led to a 6-A resolution electron density map.     

不同洗眼液对结膜囊冲洗效果的影响

目的:探讨用两种洗眼液进行结膜囊冲洗(简称洗眼)对眼部的影响效果。方法:将492人分为两组进行洗眼:A组304人用生理盐水进行洗眼2次;B组188人用蒸馏水进行洗眼2次,了解洗眼后的眼部不适和结膜充血情况。结果:两组间眼部不适和结膜充血有显著性。结论:用生理盐水洗眼较用蒸馏水洗眼可减轻眼部不适及结膜充血。     

A complementary DNA clone for a macrophage-lymphocyte Fc receptor

Macrophages, granulocytes and many lymphocytes express or secrete receptors for the Fc domain of immunoglobulins (Ig). These Fc receptors (FcRs) are heterogeneous and can be distinguished on the basis of their cellular distribution and specificities for different immunoglobulin isotypes. Although their functions are not completely understood, FcRs are known to be involved in triggering various effector cell functions and in regulating differentiation and development of B-cells. One of the best characterized is the mouse macrophage-lymphocyte receptor for IgG1 and IgG2b (ref. 5). On macrophages, this FcR mediates the endocytosis of antibody-antigen complexes via coated pits and coated vesicles, the phagocytosis of Ig-coated particles, and the release of various inflammatory and cytotoxic agents. It is possible that the receptor possesses an intrinsic ligand-activated ion channel activity responsible for some of these functions. The IgG1/IgG2b FcR has been isolated and shown to be a transmembrane glycoprotein of relative molecular mass (Mr) 47,000-60,000 (47-60 K) containing four N-linked oligosaccharide chains and a large (greater than 10K) cytoplasmic domain. It is also immunologically indistinguishable from the murine Ly-17 alloantigen which, in turn, is tightly linked to the Mls lymphocyte activation locus. Here we describe the isolation and characterisation of a complementary DNA clone encoding the whole of the IgG1/IgG2b FcR expressed by the mouse macrophage-like cell line P388D1. The receptor is a member of the immunoglobulin superfamily and, like Ly-17, maps to the distal portion of chromosome 1. cDNA probes detect one or two mRNA species in FcR+ macrophage and B-cell lines, but not in FcR- cells or a receptor-deficient variant derived from a FcR+ B-cell line. Finally, DNA hybridization analysis indicates the receptor gene is partially deleted or rearranged in the FcR- variant.     

Localization of the binding site for the human high-affinity Fc receptor on IgG

A major pathway in the clearance of pathogens involves the coating of the pathogen with specific antibodies, and the binding of the antibody Fc region to cell receptors. This can trigger engulfment of the pathogen by phagocytes or lysis by killer cells. By oligonucleotide site-directed mutagenesis we have engineered a single amino acid change in a mouse IgG2b antibody (Glu 235----Leu) which now enables the antibody to bind to the FcRI (high affinity) receptor on human monocytes with a 100-fold improvement in affinity. This indicates that Leu 235 is a major determinant in the binding of antibody to FcRI and that the receptor may interact directly with the region linking the CH2 domain to the hinge. Tailoring the affinity of antibodies for cell receptors could help dissect their role in clearing pathogen.