TY - JOUR
T1 - Identification of the metal associated with the insulin degrading enzyme
AU - Ebrahim, Alireza
AU - Hamel, Frederick G.
AU - Bennett, Robert G.
AU - Duckworth, William C.
N1 - Funding Information:
ACKNOWLEDGMENTS This work supported by the Department of Veterans Affairs Research Service and a grant from the Juvenile Diabetes Foundation. The authors thank Jennifer Larsen, MD for reviewing the manuscript and Kim Dempsey for secretarial assistance.
PY - 1991/12/31
Y1 - 1991/12/31
N2 - Insulin degrading enzyme (IDE) is a thiol-dependent metalloendoprotease that is responsible for initiation of cellular insulin degradation. However, its exact mode of action and the factors controlling it are poorly understood. Since IDE is a metal requiring enzyme, we have examined which metal(s) is(are) endogenously associated with it. Using neutron activation analysis, we studied the metal content of a partially purified enzyme from three different tissues: rat skeletal muscle, rat liver, and human placenta. Our results indicate that zinc and manganese are associated with the enzyme with approximately 10 times more zinc as manganese being present. These results suggest that one or both of these two metals are endogenously associated with this enzyme and are a means of controlling the enzyme's activity.
AB - Insulin degrading enzyme (IDE) is a thiol-dependent metalloendoprotease that is responsible for initiation of cellular insulin degradation. However, its exact mode of action and the factors controlling it are poorly understood. Since IDE is a metal requiring enzyme, we have examined which metal(s) is(are) endogenously associated with it. Using neutron activation analysis, we studied the metal content of a partially purified enzyme from three different tissues: rat skeletal muscle, rat liver, and human placenta. Our results indicate that zinc and manganese are associated with the enzyme with approximately 10 times more zinc as manganese being present. These results suggest that one or both of these two metals are endogenously associated with this enzyme and are a means of controlling the enzyme's activity.
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U2 - 10.1016/0006-291X(91)92094-Z
DO - 10.1016/0006-291X(91)92094-Z
M3 - Article
C2 - 1764090
AN - SCOPUS:0026321395
SN - 0006-291X
VL - 181
SP - 1398
EP - 1406
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -