41 research outputs found
Multiple (inverse) binomial sums of arbitrary weight and depth and the all-order epsilon-expansion of generalized hypergeometric functions with one half-integer value of parameter
We continue the study of the construction of analytical coefficients of the
epsilon-expansion of hypergeometric functions and their connection with Feynman
diagrams. In this paper, we show the following results:
Theorem A: The multiple (inverse) binomial sums of arbitrary weight and depth
(see Eq. (1.1)) are expressible in terms of Remiddi-Vermaseren functions.
Theorem B: The epsilon expansion of a hypergeometric function with one
half-integer value of parameter (see Eq. (1.2)) is expressible in terms of the
harmonic polylogarithms of Remiddi and Vermaseren with coefficients that are
ratios of polynomials. Some extra materials are available via the www at this
http://theor.jinr.ru/~kalmykov/hypergeom/hyper.htmlComment: 24 pages, latex with amsmath and JHEP3.cls; v2: some typos corrected
and a few references added; v3: few references added
Distribution of intestinal mast cell proteinase in blood and tissues of normal and Trichinella-intected mice
The isolation and characterization of globule leucocytes: their derivation from mucosal mast cells in parasitized sheep
Proteinase phenotypes and fixation properties of rat mast cells in parasitic lesions caused by Mesocestoides corti: selective and site-specific recruitment of mast cell subsets
The action of a mast cell protease on the cuticular collagens of Necator americanus.
Collagen-like proteins, thought to be responsible for maintaining the structural integrity of the nematode cuticle, were isolated from adult Necator americanus and shown to be susceptible to digestion by purified mast cell proteases. Although these collagens would appear normally to be masked by superficially expressed (surface) antigens, it is suggested that a sufficiently avid and specific immune response could remove this potentially protective coat, rendering the structurally important underlying layers open to immune attack
Cytochemical observations on the development of antibody-forming cells in popliteal lymph nodes by an improved immunoperoxidase method
Mouse mast cell protease-1 is required for the enteropathy induced by gastrointestinal helminth infection in the mouse
The relationship between intestinal pathology and immune expulsion of gastrointestinal nematodes remains controversial. Immune expulsion of gastrointestinal helminth parasites is usually associated with Th2 responses, but the effector mechanisms directly responsible for parasite loss have not been elucidated. Mast cell hyperplasia is a hallmark of infection with gastrointestinal nematodes, in particular Trichinella spiralis. Although the precise mechanism by which mast cells induce expulsion of these parasites has not been elucidated, it has been proposed that mast cell mediators, including cytokines and granule chymases, act to create an environment inhospitable to the parasite, part of this being the induction of intestinal inflammation. Therefore, the aims of this study were to dissect the role of mast cells and mast cell proteases in the induction of parasite-induced enteropathy. Mast cell-deficient W/Wv and mouse mast cell protease-1 (mMCP-1)-deficient mice were infected with T. spiralis, and parasite expulsion, enteropathy, and Th2 responses were determined. Expulsion of the parasite was delayed in both strains of mice compared with wild-type controls; additionally, in both cases, the enteropathy was significantly ameliorated. Although Th2 responses were significantly reduced in mast cell-deficient W/Wv mice, those from mMCP-1-deficient mice were similar to wild-type mice. Additionally, levels of TNF-α and nitric oxide were significantly reduced in both W/Wv and mMCP-1 deficient mice. These results imply that mast cells may contribute to the induction of protective Th2 responses and, importantly, that the intestinal inflammation associated with gastrointestinal helminths is partly mediated by mMCP-1 MLN, mesenteric lymph node; MMC, mucosal mast cell; mMCP-1, mouse mast cell protease-1; MPO, myeloperoxidase; p.i., postinfection; TUNEL, terminal dUTP nick-end labeling; VCU, villus crypt uni