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Immunoglobulin Isotypes in Human Minor Gland Saliva

Journal of Dental Research, 1991
Lower labial, upper labial, palatine (minor), and parotid (major) gland saliva samples from 18 young adult males were quantitatively assayed for the presence of IgAl, IgA2, IgM, and IgG. The mean (± standard deviation) concentrations of IgA (sum of IgAl + IgA2) were 79 ± 42 μg/mL (parotid), 111 ± 42 μg/mL (lower labial), 69 ± 72 μg/mL (upper labial ...
D J, Smith, M A, Taubman, P, Ali-Salaam
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Regulation of Isotype Immunoglobulin Production by Adjuvants in Vivo

Scandinavian Journal of Immunology, 1990
Mice were immunized against fiuorescein isothiocyanate (FITC)‐labelled human gamma globulin (HGG) or dexlran sulphate (DXS) in the absenee or presence of different adjuvants. The immune response was assayed as the total Ig‐secreting cells and FITC‐speeilic plaque‐forming cells (PFC) found in various lymphoid organs. The adjuvants inliueneed the isolype
E E, Karagouni   +1 more
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Lymphokine Control of In Vivo Immunoglobulin Isotype Selection

Annual Review of Immunology, 1990
Several specific conclusions can be drawn from these studies: 1. IL-4 is required for the generation of both primary polyclonal and secondary antigen-specific IgE responses in vivo. 2. IL-4 is required to maintain established, ongoing, antigen-specific and polyclonal IgE responses. 3.
F D, Finkelman   +9 more
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Models for the dynamics and order of immunoglobulin isotype switching

Bulletin of Mathematical Biology, 2005
Experiments show that class switch recombination (CSR) depends on the number of divisions that the cell has performed rather than on the time since stimulation. Using computer simulations of CSR dynamics in B cell populations, we addressed the following questions.
Barak, Yaish, Ramit, Mehr
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Immunoglobulin isotype knowledge and application to Fc engineering

Current Opinion in Immunology, 2016
Monoclonal antibody-based drugs continue to be one of the most rapidly growing classes of therapeutic molecules. At present, the majority of approved therapeutic antibodies are of the human IgG1 format, which can elicit immune effector functions (e.g., antibody-dependent cellular cytotoxicity, antibody-dependent cellular phagocytosis, and complement ...
Randall J, Brezski, George, Georgiou
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Immunoglobulin isotype in the murine response to polysaccharide antigens

European Journal of Immunology, 1983
AbstractMurine antisera specific for the α (1→3) and α (1→6)‐linked glucosyl determinants of dextran, as well as for meningococcal polysaccharide group C, have been examined for the distribution of their immunoglobulin classes and subclasses. Whereas the thymus‐independent anti‐α (1→3) dextran response in BALB/c mice was found to be IgM > IgG3 > ...
C, Moreno, J, Esdaile
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In vitro immunoglobulin isotype suppression in immunoglobulin A nephropathy.

Experimental nephrology, 1994
IgA nephropathy (IgAN) is characterized by mesangial IgA deposition, and up-regulation of the IgA system is frequently described. This study investigated in vitro immunoglobulin isotype production by peripheral blood mononuclear cells from patients with IgAN and controls, without mitogenic stimulation and under the influence of cell cycle inhibitors ...
A C, Allen   +3 more
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Biosynthesis of immunoglobulin isotypes in human periapical lesions

Journal of Endodontics, 1980
Periapical lesions from five patients were incubated with radioactive amino acids ( 14 C isoleucine and 14 C lysine). Immunoglobulin synthesis was detected by autoradiography of an immunoelectrophoretic pattern. IgG and IgA were synthesized in vitro by lymphocytes from all of the periapical lesions studied.
O J, Jones, E T, Lally
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Isotypes in Human Immunoglobulin λ-Chains

Nature New Biology, 1971
IMMUNOGLOBULIN polypeptide chains consist of a variable N-terminal region and a constant C-terminal part1. The variability of the N-terminal part is due to multiple amino-acid exchanges and deletions, which can be arranged into chemically distinct subgroups2–9.
MAXIME HESS   +4 more
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The Relevance of Immunoglobulin Isotype to Neutralization

1993
The immunoglobulin isotypes G1, G2, G3 and G4 (in man) and G1, G2a, G2b and G3 (in mouse), A and M differ variously in size (Table 5) and other properties relating mainly to the sequence and structure of the constant region of their heavy chains (Roitt et al. 1989; Burton 1990).
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