TY - JOUR
T1 - The cardiac gap junction protein (Mr 47,000) has a tissue-specific cytoplasmic domain of Mr 17,000 at its carboxy-terminus
AU - Manjunath, C. K.
AU - Nicholson, B. J.
AU - Teplow, David
AU - Hood, Lee
AU - Page, E.
AU - Revel, J. P.
N1 - Funding Information:
We would like to express our thanks to Wade Hines for excellent technical assistance in sequence analysis and to Dr. Barbara Yancey and Jan Hoh for helpful discussions on the manuscript. Research was supported by the National Heart, Lung and Blood Institute, grants HLlO503 and HL20592 (Drs. Manjunath and Page), the American Heart Association, Los Angeles Affiliate, grant 769 F1.2 (Dr. Nicholson), the National Institutes of Health grant GM06965, the Biomedical Research Support Grant RR07003, and the Ruddock Fund (Dr. Revel).
PY - 1987/1/15
Y1 - 1987/1/15
N2 - The molecular weight of the heart gap junctional protein subunit was, until recently, believed to be about Mr 28,000-30,000, similar to that of other previously characterized gap junctional proteins. A larger polypeptide of about Mr 44,000-47,000, which undergoes proteolysis during isolation, has recently been proposed as the form of the heart junction protein in vivo. We show here that this entity has the same aminoterminal sequence as the previously characterized Mr 29,000-30,000 component. Thus, the cardiac junctional protein has, at its carboxy-terminus, a cytoplasmic domain of Mr 17,000; this domain is absent in the liver protein. These observations provide further evidence that gap junction proteins form a highly diversified family.
AB - The molecular weight of the heart gap junctional protein subunit was, until recently, believed to be about Mr 28,000-30,000, similar to that of other previously characterized gap junctional proteins. A larger polypeptide of about Mr 44,000-47,000, which undergoes proteolysis during isolation, has recently been proposed as the form of the heart junction protein in vivo. We show here that this entity has the same aminoterminal sequence as the previously characterized Mr 29,000-30,000 component. Thus, the cardiac junctional protein has, at its carboxy-terminus, a cytoplasmic domain of Mr 17,000; this domain is absent in the liver protein. These observations provide further evidence that gap junction proteins form a highly diversified family.
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U2 - 10.1016/0006-291X(87)90475-X
DO - 10.1016/0006-291X(87)90475-X
M3 - Article
C2 - 3028402
AN - SCOPUS:0023141815
SN - 0006-291X
VL - 142
SP - 228
EP - 234
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -