TY - JOUR
T1 - Antibodies to lipoprotein lipase application to perfused heart
AU - Schotz, Michael C.
AU - Jer-Shung, Twu
AU - Pedersen, Mary E.
AU - Chi-Hong, Chen
AU - Garfinkel, Arlene S.
AU - Borensztajn, Jayme
N1 - Funding Information:
This work was supported in part by funds from: the National Institutes of Health, HL16577 and HL17246; the American Heart Association, 76-666; the American Heart Association, Greater Los Angeles Affiliate, 4921G4; and the Veterans Administration Medical Research. The authors wish to thank Judith Nikazy and Raymond Miller for their expert technical help. In addition, the authors would like to express their gratitude to Drs. I. Nilsson-Ehle and W. Palin for their help in the preparation of antiserum, and to Dr. R.O. for the gift of rat mammary gland acetone powder.
PY - 1977/11/24
Y1 - 1977/11/24
N2 - An antibody was prepared against purified rat heart lipoprotein lipase. 1. 1. This antibody showed marked species specificity. It inhibited almost totally the lipoprotein lipase activity from all rat tissues examined (i.e., heart, adipose, postheparin plasma, and mammary gland), while having no effect on the activity of lipoprotein lipase partially purified from rabbit, guinea pig and bovine heart and from bovine milk. The antibody also had no effect on the hepatic lipase activity of rat postheparin plasma. 2. 2. After antibody to rat heart lipoprotein lipase was recirculated for 5 min through isolated rat hearts, little or no lipoprotein lipase activity could be detected in the perfusate during 0-20 s of a subsequent non-recirculating perfusion with buffer containing 1 unit heparin/ml. 3. 3. Following recirculation of antibody to lipoprotein lipase for 10 min and a non-recirculating perfusion with buffer for 2 min, the hearts no longer oxidized any significant amounts of 14C-labelled palmitate chylomicron triacylglycerol fatty acid to 14CO2 during a 15-min perfusion. The data give compelling evidence that the functional fraction of lipoprotein lipase in hearts is at the endothelial cell surface accessible to lipoprotein lipase antibody.
AB - An antibody was prepared against purified rat heart lipoprotein lipase. 1. 1. This antibody showed marked species specificity. It inhibited almost totally the lipoprotein lipase activity from all rat tissues examined (i.e., heart, adipose, postheparin plasma, and mammary gland), while having no effect on the activity of lipoprotein lipase partially purified from rabbit, guinea pig and bovine heart and from bovine milk. The antibody also had no effect on the hepatic lipase activity of rat postheparin plasma. 2. 2. After antibody to rat heart lipoprotein lipase was recirculated for 5 min through isolated rat hearts, little or no lipoprotein lipase activity could be detected in the perfusate during 0-20 s of a subsequent non-recirculating perfusion with buffer containing 1 unit heparin/ml. 3. 3. Following recirculation of antibody to lipoprotein lipase for 10 min and a non-recirculating perfusion with buffer for 2 min, the hearts no longer oxidized any significant amounts of 14C-labelled palmitate chylomicron triacylglycerol fatty acid to 14CO2 during a 15-min perfusion. The data give compelling evidence that the functional fraction of lipoprotein lipase in hearts is at the endothelial cell surface accessible to lipoprotein lipase antibody.
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U2 - 10.1016/0005-2760(77)90140-0
DO - 10.1016/0005-2760(77)90140-0
M3 - Article
C2 - 922025
AN - SCOPUS:0017671096
SN - 0005-2760
VL - 489
SP - 214
EP - 224
JO - Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
JF - Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
IS - 2
ER -