Binding and internalization of atrial natriuretic factor by high-affinity receptors in A10 smooth muscle cells |
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| Authors: | M A Napier K E Arcuri R L Vandlen |
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| Affiliation: | 1. Departamento de Química Farmacológica y Toxicológica, Facultad de Ciencias Químicas y Farmacéuticas, Universidad de Chile, Santiago;2. Advanced Center for Chronic Diseases (ACCDiS), Sergio Livingstone 1007, Independencia, Santiago, Chile;3. Escuela de Biotecnología, Facultad de Ciencias, Universidad Santo Tomás, Ejercito 146, Santiago, Chile;4. Programa Institucional de Fomento a la I+D+I, Universidad Tecnológica Metropolitana, Edificio de Ciencia y Tecnologia, Ignacio Valdivieso 2409, San Joaquin;5. Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, Alameda 340, Santiago 8331010, Chile;6. Centro de envejecimiento y regeneración (CARE), Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, Santiago, Chile;7. Sección de Metrología Química, Comisión Chilena de Energía Nuclear, Nueva Bilbao 12501, La Reina, Santiago, Chile;8. Departamento de Ciencias Quimicas, Facultad de Ciencias Exactas, Universidad Andres Bello, Av. Republica 275, Santiago, Chile;9. Institute for Research in Biomedicine-Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028 Barcelona, Spain;1. Cellular Plasticity and Disease Group, Institute for Research in Biomedicine (IRB Barcelona), Barcelona Institute of Science and Technology (BIST), Barcelona, Spain;2. Catalan Institution for Research and Advanced Studies (ICREA), Barcelona, Spain |
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| Abstract: | A10 smooth muscle cells, derived from embryonic rat thoracic aorta, responded to the atrial natriuretic factor (ANF) with increased levels of cyclic GMP. These cells possess high-affinity (apparent Kd = 50 pM) plasma membrane receptors for ANF. Internalization of ANF at 37 degrees C was indicated by the following: approximately 25% of the 125I-ANF associated with the cells at elevated temperatures could not be dissociated from the surface of the cells, but could be released by permeabilization with saponin, and the amount of nondissociable ANF increased in the presence of chloroquine. In whole cells and in membranes, a single polypeptide of 60,000 Da was specifically labeled by a photoaffinity analog of 125I-ANF, as well as by crosslinking, and an IC50 of 80 pM for inhibition of the labeling by ANF was observed. The ANF receptor in A10 cells was distinguished from that in rabbit aorta by its high affinity for shorter and linear analogs of ANF, as well as by a different photolabeling pattern. |
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