Smooth muscle expresses a cardiac/slow muscle isoform of the Ca2+-transport ATPase in its endoplasmic reticulum.
نویسندگان
چکیده
Smooth muscle expresses in its endoplasmic reticulum an isoform of the Ca2+-transport ATPase that is very similar to or identical with that of the cardiac-muscle/slow-twitch skeletal-muscle form. However, this enzyme differs from that found in fast-twitch skeletal muscle. This conclusion is based on two independent sets of observations, namely immunological observations and phosphorylation experiments. Immunoblot experiments show that two different antibody preparations against the Ca2+-transport ATPase of cardiac-muscle sarcoplasmic reticulum also recognize the endoplasmic-reticulum/sarcoplasmic-reticulum enzyme of the smooth muscle and the slow-twitch skeletal muscle whereas they bind very weakly or not at all to the sarcoplasmic-reticulum Ca2+-transport ATPase of the fast-twitch skeletal muscle. Conversely antibodies directed against the fast-twitch skeletal-muscle isoform of the sarcoplasmic-reticulum Ca2+-transport ATPase do not bind to the cardiac-muscle, smooth-muscle or slow-twitch skeletal-muscle enzymes. The phosphorylated tryptic fragments A and A1 of the sarcoplasmic-reticulum Ca2+-transport ATPases have the same apparent Mr values in cardiac muscle, slow-twitch skeletal muscle and smooth muscle, whereas the corresponding fragments in fast-twitch skeletal muscle have lower apparent Mr values. This analytical procedure is a new and easy technique for discrimination between the isoforms of endoplasmic-reticulum/sarcoplasmic-reticulum Ca2+-transport ATPases.
منابع مشابه
Antibodies against the non-muscle isoform of the endoplasmic reticulum Ca2(+)-transport ATPase.
We report here the production of a polyclonal antiserum which specifically recognizes an epitope confined to the ultimate 12-residue-long C-terminus of an alternatively spliced transcript of gene 2 encoding the sarcoplasmic reticulum Ca2+ pump in slow skeletal and cardiac muscle. This alternatively spliced transcript was shown to be mainly represented in non-muscle tissues. These antibodies hav...
متن کاملA study of the organellar Ca2(+)-transport ATPase isozymes in pig cerebellar Purkinje neurons.
Pig cerebellar Purkinje neurons express a high level of Ca2(+)-transport ATPases in their intracellular Ca2+ stores. This was shown at the mRNA level by Northern blotting and in situ hybridization and at the protein level by Western blotting and immunocytochemistry. The majority of the Ca2(+)-transport ATPases in these neurons belongs to the SERCA2b type (i.e., the Ca2(+)-pump isoform found in ...
متن کاملCa2+-transport ATPases of vascular smooth muscle.
To characterize the Ca2+-transport properties of the plasma membrane and of the endoplasmic reticulum of bovine pulmonary artery, membrane vesicles are subfractionated by a procedure of density-gradient centrifugation that takes advantage of the selective effect of digitonin on the density of plasma-membrane vesicles. The obtained endoplasmic-reticulum fraction contains hardly any plasma-membra...
متن کاملExpression of endoplasmic-reticulum Ca2(+)-pump isoforms and of phospholamban in pig smooth-muscle tissues.
The expression of the gene 2 sarcoplasmic/endoplasmic-reticulum Ca2(+)-pump isoforms (SERCA2a and SERCA2b) and of phospholamban was studied in pig smooth muscle of the stomach, longitudinal ileum, pulmonary artery and aorta. mRNA levels were determined using an RNAase protection assay. The SERCA2 isoforms and phospholamban were tested on Western blots with a panel of antibodies, some of which w...
متن کاملInhibitory antibodies to plasmalemmal Ca 2 + - transporting
Antibodies directed against the purified calmodulin-binding (Ca2++ Mg2+)-ATPase [(Ca2+ + Mg2+)dependent ATPase] from pig erythrocytes and from smooth muscle of pig stomach (antral part) were raised in rabbits. Both the IgGs against the erythrocyte (Ca2++ Mg2+)-ATPase and against the smooth-muscle (Ca2+ + Mg2+)-ATPase inhibited the activity of the purified calmodulin-binding (Ca2++ Mg2+)-ATPase ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Biochemical journal
دوره 257 1 شماره
صفحات -
تاریخ انتشار 1989