RESUMO
It has been demonstrated that induction of immune responses, infectious diseases and autoimmune manifestations can be associated with at least four gene loci: the major histocompatibility complex (MHC) locus; the immunoglobulin (Ig) heavy chain (Hc) locus; and the T-cell receptor (TCR) TCR-alpha or TCR-beta chain loci. In the present study, we have analysed whether T-cell responses of IE-negative C57Bl/6 (B6) mice to IE alloantigen (IE alpha transgenic B6 mice = B6.E alpha 16) or to trinitrophenylated (TNP) syngeneic spleen cells were influenced by changes in the Ig-Hc locus or the TCRa locus. Whereas the fine specificity of T-cell responses to IE alloantigen was the same in B6 mice and in Ig-Hc congenic B6.26a or TCRa congenic B6.10TCa mice, the latter strain of mice demonstrated much higher IE-specific T-cell responses against B6.E alpha 16 spleen cells than B6 or B6.26a mice. This high responsiveness was a dominant feature and associated with the TCRa locus. In addition, the TCRV alpha or V beta repertoire of the congenic strains of mice was polyclonal and very similar. The TNP-specific T-cell responses of B6 and B6.10TCa mice showed the same restricted TCRV alpha and V beta repertoire. It is concluded that in both an oligoclonal T-cell response (anti-TNP) and a polyclonal T-cell response (anti-IE), exchange of Ig-Hc or TCRa loci does not significantly influence the TCRV alpha or V beta repertoire in IE-negative C57Bl/6 mice.
Assuntos
Rearranjo Gênico do Linfócito T , Rearranjo Gênico da Cadeia alfa dos Receptores de Antígenos dos Linfócitos T , Antígenos H-2/imunologia , Animais , Linhagem Celular , Rearranjo Gênico do Linfócito T/imunologia , Rearranjo Gênico da Cadeia alfa dos Receptores de Antígenos dos Linfócitos T/imunologia , Antígenos H-2/genética , Camundongos , Camundongos Endogâmicos C57BL , Camundongos Endogâmicos , RNA Mensageiro/análise , Baço/imunologiaRESUMO
The Km constant and the sensitivity to inhibitors were determined for the rare variant KUK of red cell acid phosphatase. At the same time, the thermodynamic energies of activation and of inactivation were measured. The kinetic parameters were not very different from those of the usual ACP1 C alloenzymes. However, they differed in their thermodynamic energies: the conformational structure of the ACP1 KUK protein being less stable.
