DISTRIBUTION OF THE INTEGRAL PLASMA-MEMBRANE GLYCOPROTEIN CE9 (MRC OX-47) AMONG RAT-TISSUES AND ITS INDUCTION BY DIVERSE STIMULI OF METABOLIC-ACTIVATION
Cl. Nehme et al., DISTRIBUTION OF THE INTEGRAL PLASMA-MEMBRANE GLYCOPROTEIN CE9 (MRC OX-47) AMONG RAT-TISSUES AND ITS INDUCTION BY DIVERSE STIMULI OF METABOLIC-ACTIVATION, Biochemical journal, 310, 1995, pp. 693-698
We have compared the levels of the integral plasma membrane glycoprote
in CE9 (MRC OX-47) in different tissues of the rat and have ascertaine
d that the levels of CE9 protein and mRNA in selected tissues and cell
s exhibit moderate increases in response to diverse stimuli of metabol
ic activation. When normalized on the basis of total protein, the leve
l of CE9 detected in the different tissues was found to vary over a 50
-fold range. In addition, the apparent molecular mass of CE9 was obser
ved to vary from 40 kDa to 58 kDa as a consequence of tissue-specific
glycosylation, The highest level of CE9 was detected in brown adipose
tissue, where the protein was found to be localized to the plasma memb
ranes of the adipocytes, The metabolic activation of brown adipose tis
sue that occurs upon exposure of rats to the cold was found to be acco
mpanied by 3.0 +/- 0.4-fold and 1.7 +/- 0.2-fold increases in the leve
ls of CE9 mRNA and protein respectively, An intermediate level of CE9
was detected in the liver, where the protein is known to be expressed
within the basolateral domain of the hepatocyte plasma membrane. The m
etabolic activation of hepatocytes that occurs upon administration of
thyroid hormone to euthyroid rats was found to be accompanied by 2.2 /- 0.3-fold and 1.9 +/- 0.3-fold increases in the levels of CE9 mRNA a
nd protein respectively. A low level of CE9 was detected in the lympho
id organs, such as thymus and spleen. The metabolic activation of isol
ated rat splenocytes that occurs upon concanavalin A-mediated blast tr
ansformation in culture was found to be accompanied by 2.1 +/- 0.2-fol
d and 1.6 +/- 0.2-fold increases in the levels of CE9 mRNA and protein
respectively. On the basis of these and other observations, we sugges
t that the level, and possibly also the localization, of the integral
plasma membrane glycoprotein CE9 may be correlated in a positive fashi
on with metabolic activity in a diverse array of cell types.