Erythrocyte Adducin Differential Properties in the Normotensive and Hypertensive Rats of the Milan Strain

Autor:	Sergio Salardi, Beatrice Saccardo, Giuseppe Borsani, Rossana Modica, Mara Ferrandi, M. Grazia Tripodi, Marco Soria, Patrizia Ferrari, Francisco Ernesto Baralle, Alessandro Sidoli, Giuseppe Bianchi
Rok vydání:	1989
Předmět:	biology Calmodulin business.industry Clone (cell biology) RNA Phosphatidylserine Molecular biology chemistry.chemical_compound chemistry Affinity chromatography Internal Medicine biology.protein Medicine Antibody Cytoskeleton business Protein kinase C
Zdroj:	American Journal of Hypertension. 2:229-237
ISSN:	1941-7225 0895-7061
DOI:	10.1093/ajh/2.4.229
Popis:	Previous studies have shown that erythrocytes from the Milan hypertensive strain of rats (MHS) differ from erythrocytes from the control normotensive strain (MNS). These differences are determined within the stem cells, are genetically associated with the development of hypertension, and are similar to those found between the tubular cells of the two strains. Moreover they seem to be dependent upon the presence of the membrane skeleton proteins. In this paper we describe our studies aimed at identifying some precise protein difference between the membrane skeletons of the two strains, which may cause the cellular differences described above. Milan hypertensive strain and MNS rats were immunized with ghost or membrane skeleton extracts prepared from the other or their own strains. Only MHS rats immunized with MNS ghost or membrane skeleton extracts produced an antibody against a 105 KD protein in about 95% of the animals. This protein has been identified with the recently described cytoskeletal protein adducin on the following bases: the protein binds calmodulin (CaM) and protein kinase C (PKc) in a Ca2+ dependent way. It also binds phosphatidylserine, is the substrate of exogenous PKc, and finally it is purified by high salt extraction of Triton-X100 insoluble erythrocyte cytoskeletons followed by affinity chromatography on CaM-sepharose. Using this antibody the isolation from a mouse spleen library, the characterization and sequencing of a partial cDNA clone coding for this protein has been carried out. In conclusion adducin may be considered a very useful tool to test the hypothesis that the cellular differences between MHS and MNS may be caused by a difference in a membrane skeleton protein.
Databáze:	OpenAIRE
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