A dual role for the Ca2+-requiring proteinase in the degradation of hemoglobin by erythrocyte membrane proteinases.
AUTOR(ES)
Pontremoli, S
RESUMO
Binding of hemoglobin chains to erythrocyte membranes is an obligatory step in the conversion of hemoglobin to acid-soluble products by erythrocyte proteinases. This binding requires limited proteolysis of the hemoglobin chains and also modification of the inner surface of the erythrocyte membrane, both of which result from the action of a soluble Ca2+-requiring neutral proteinase. Final digestion of the bound hemoglobin chains in the membrane complex results from the action of intrinsic membrane endopeptidases. Regulation of the activity of the Ca2+-requiring proteinase by the substrate provides a mechanism for the initiation of selective protein turnover.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=392001Documentos Relacionados
- Binding of protein kinase C to neutrophil membranes in the presence of Ca2+ and its activation by a Ca2+-requiring proteinase.
- A malarial cysteine proteinase is necessary for hemoglobin degradation by Plasmodium falciparum.
- Modulation of erythrocyte membrane material properties by Ca2+ and calmodulin. Implications for their role in regulation of skeletal protein interactions.
- Lysis and killing of bacteria by lysosomal proteinases.
- Endogenous inhibitors of lysosomal proteinases.