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Subject:
From:
Juliann Seebauer <[log in to unmask]>
Reply To:
Milk/Casein/Lactose-Free List <[log in to unmask]>
Date:
Wed, 29 Jan 2003 13:51:13 -0600
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Record 7 of 10 in Biological Abstracts 1999/01-1999/06

TI:  An update on allergens: Cow's milk allergens.
AU:  Wal-J-M {a}
SO:  Allergy-Copenhagen. Nov., 1998; 53 (11) 1013-1022.
PY:  1998
LA:  English
AN:  199900044537
UD:  19990223

Record 8 of 10 in Biological Abstracts 1998/07-1998/12

TI:  Enhancement of antigen-specific IFN-gamma production from CD8+ T
cells by a single amino acid-substituted peptide derived from bovine
alphas1-Casein.
AU:  Totsuka-Mamoru; Kakehi-Masahiro; Kohyama-Masako;
Hachimura-Satoshi; Hisatsune-Tatsuhiro; Kaminogawa-Shunichi
SO:  Clinical-Immunology-and-Immunopathology. Sept., 1998; 88 (3) 277-286.
PY:  1998
LA:  English
AB:  Modulation of CD8+ T-cell responses specific for an exogenous
antigen by epitope variants would be advantageous to develop a novel
means of antigen-specific immune regulation. We have analyzed CD8+
T-cell responses to single amino acid-substituted variants of a
peptide corresponding to residues 142-149 (p142-149; LAYFYPEL) of
alphas1-casein, a major milk allergen, which is a dominant
determinant restricted by H-2kb. An analog peptide L142I with a
substitution of Ile for Leu at the nonanchor N-terminal residue
induced more IFN-gamma secretion than p142-149 from specific CD8+ T
cells. Furthermore, L142I could prime CD8+ T cells more efficiently
in vivo, and these L142I-primed cells secreted more IFN-gamma than
p142-149-primed CD8+ T cells upon stimulation with p142-149 in vitro.
These findings are mainly explained by the greater ability of L142I
to form stable Kb-peptide complexes. These findings indicate that
appropriate analog peptides may be useful as efficient inducers of
CD8+ T cells which recognize the parent peptide and secrete
IFN-gamma, a potent inhibitor of Th2-dependent events, including IgE
production.
AN:  199800480414
UD:  19980921

Record 9 of 10 in Biological Abstracts 1998/07-1998/12

TI:  Increased expression of alpha4beta7 integrin on food
allergen-stimulated CD4+ T cells in active food allergic
enterocolitis.
AU:  Kohno-Yoichi {a}; Shimojo-Naoki; Aoyagi-Masahiko;
Sannomiya-Yoshio; Nishimuta-Toshiyuki; Kojima-Hiroyuki;
Katsuki-Toshiyuki; Tomiita-Minako; Lazarovits-Andrew-I;
Ringler-Douglas; Niimi-Hiroo
SO:  Allergology-International. June, 1998; 47 (2) 99-102.
PY:  1998
LA:  English
AB:  We used flow cytometry to investigate the expression of
alpha4beta7 integrin on peripheral blood CD4+ T cells stimulated with
alphas-casein, one of the major allergens in milk allergy, in
patients with milk-induced enterocolitis. In the active state of the
disease, the levels of alpha4beta7 integrin on
alphas-casein-stimulated CD4+ T cells, as well as the numbers of
positive cells, were higher than in the age-matched control. Upon
outgrowing milk allergy, alpha4beta7 integrin levels decreased to the
same levels as in the healthy control. The proliferative responses of
peripheral blood mononuclear cells to alphas-casein in the active
state did not differ from those in the outgrown state, suggesting
that the expression of alpha4beta7 integrin on milk
allergen-activated T cells is a marker of the activation state
leading to the pathogenesis of milk-allergic enterocolitis.
AN:  199800355502
UD:  19980629

Record 10 of 10 in BA on CD 1/95-6/95

TI:  CD23/CD21 interaction is required for presentation of soluble
protein antigen by lymphoblastoid B cell lines to specific CD4+ T
cell clones.
AU:  Grosjean-I; Lachaux-A; Bella-C; Aubry-J-P; Bonnefoy-J-Y; Kaiserlian-D
SO:  European Journal of Immunology 24(12): 2982-2986
PY:  1994
LA:  English
AB:  Previous studies have documented a role for membrane-bound CD23
(the low affinity Fc-epsilon-RII) in presentation of alloantigens by
B cells. The aim of the present study was to examine the involvement
of cell surface CD23 in presentation of more conventional soluble
protein antigens to T cells. We show that antibodies to CD23 and to
its lymphocyte-associated second ligand, CD21, inhibit presentation
of the cow's milk allergen casein, by autologous CD23+cd21+ B-EBV
cell lines to casein-specific HLA-DP-restricted CD4+ T cell clones
obtained from patients with either reaginic or enterophatic forms of
cow's milk protein intolerance. Maximal inhibition was achieved when
the antibodies were added at the initiation of the culture. The
absence of specific inhibition by an anti-DR-alpha monoclonal
antibody (mAb) argues against a steric hindrance phenomenon impeding
access of the T cell receptor to major histocompatibility complex
class II molecules. Rather, anti-CD23 and anti-CD21 mab-induced
inhibition of antigen presentation seems to affect at least partly,
heterotypic conjugate formation through CD23/CD21 interaction. Double
immunofluorescence labeling of the T cell clones and antibody
inhibition of T/B conjugate formation shows that functional CD23 and
CD21 molecules are induced on T cells following contact with B-EBV
cell lines. Taken together, these data indicate that CD23/CD21
interactions between T and B cells are required for presentation of
soluble protein antigens by B-EBV cell lines to specific CD4+ T
cells. The potential implications of these findings for
allergen-specific T cell activation are discussed.

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