Search results for "Primary immune response"
showing 3 items of 3 documents
Cops and robbers: putative evolution of copper oxygen-binding proteins.
2000
Two closely related copper proteins, phenoloxidase and haemocyanin, are known to be involved in different physiological functions such as the primary immune response and oxygen transport. Although the proteins differ structurally, they have the same active site by which dioxygen is bound. Recent results reveal that haemocyanin also exhibits phenoloxidase activity. A scenario is proposed for the evolutionary relationships among copper oxygen-binding proteins (COPs).
Copper Proteins with Dinuclear Active SitesBased in part on the article Copper Proteins with Dinuclear Active Sites by Konrad Lerch which appeared in…
2006
Copper proteins with dinuclear active sites comprise proteins with different structures and functions. The phenoloxidase, tyrosinase, and catecholoxidase are responsible for browning by starting the synthesis of melanin. These enzymes are involved in the primary immune response in invertebrates, plants, fungi as well as in the sclerotization of arthropods. The respiratory proteins hemocyanins are responsible for oxygen transport in some arthropods and molluscs. However, they can be converted to enzymes exhibiting phenoloxidase activity. Based on X-ray structures of hemocyanins and a catecholoxidase, large parts of folding motifs are very similar although the sequence identities are far belo…
Development of Rat DC by in Vitro Culture of Bone Marrow Cells
1995
Dendritic cells (DC) represent a subpopulation of leukocytes of bone marrow (BM) origin, involved in crucial immunological reactions. DC play a fundamental role in the primary immune response by stimulating quiescent T cells. In this study we describe an in vitro culture system to raise DC from unfractionated bone marrow (BM) cells of LEWIS rats in the presence of low doses of mouse recombinant GM-CSF, that was successfully used in previous work to culture mouse DC1,2,3.