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J Biol Chem, Vol. 273, Issue 12, 6937-6943, March 20, 1998
,,,§,
From the Sucrose-density flotation analysis of
Triton-insoluble membrane domains isolated from highly purified sheep
ventricular sarcolemma revealed the presence of two major 120- and
100-kDa proteins. Both species migrated in two-dimensional isoelectric
focussing/SDS gels with an apparent pI of ~4.3, suggesting that they
might be related. Microsequence analysis of peptides derived from the
100-kDa protein yielded amino acid sequences with high homology to
T-cadherin, a truncated cadherin lacking a cytoplasmic domain. The
similarity was confirmed using antibodies to chicken T-cadherin that
reacted with both proteins on immunoblots. T-cadherin was released from the detergent-insoluble sarcolemmal fraction by phospholipase C
treatment indicating that it is linked to the membrane by a glycophosphoinositol anchor. T-cadherin could be ADP-ribosylated by a
transferase that was also present in the caveolin-enriched Triton-insoluble fraction. T-cadherin-containing membrane fragments cofractionated on sucrose gradients with caveolin-3, a marker protein
for myocyte caveolae. However, immunopurified caveolin-3-containing membranes contained no associated T-cadherin. Immunocytochemical analysis of cultured rat atrial myocytes revealed that T-cadherin and
caveolin have related but nonoverlapping staining patterns. These
results suggest that T-cadherin is a major glycophosphoinositol-linked protein in cardiac myocytes and that it may be located in plasma membrane "rafts" distinct from but possibly adjacent to
caveolae.
Department of Medicine and
§ Department of Pharmacological and Physiological Sciences,
University of Chicago, Chicago, Illinois 60637 and ¶ Burnham
Research Institute, La Jolla, California
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