scholarly journals The subcellular localization of the β-galactoside-binding protein of rat lung

1982 ◽  
Vol 204 (1) ◽  
pp. 97-102 ◽  
Author(s):  
G L Sanford ◽  
L D Davis ◽  
J T Powell

The subcellular localization of the beta-galactoside-binding protein, or lectin, from rat lung was investigated by the specific binding of anti-lectin immunoglobulin G to subcellular fractions. We used both adult and immature (12-day-old) rats; the immature rat lungs have an 8-10-fold greater concentration than adult rat lungs [Powell & Whitney (1980) Biochem. J. 188, 1-8]. In both groups of animals we observed greater specific binding of anti-lectin immunoglobulin G to intracellular membrane (mitochondrial and microsomal fractions) than to plasma membranes. Pre-incubation of membrane fractions with lactose resulted in a marked diminution of anti-lectin immunoglobulin G binding. In the adult rat lung most (approx. 80%) of the lectin activity was membrane-associated. In the immature rat lung only approx. 30% of the lectin activity was membrane associated and most of the beta-galactoside-binding protein appeared to be a soluble cytoplasmic component. The rat lung beta-galactoside-binding protein appeared to have a broad but predominantly intracellular location, being associated with membranes through one of its galactoside-binding sites.

1987 ◽  
Vol 245 (3) ◽  
pp. 683-690 ◽  
Author(s):  
L B Clerch ◽  
P L Whitney ◽  
D Massaro

Soluble lectins are widely distributed cell-agglutinating proteins. Their activity is developmentally regulated in several tissues, including the lung, but virtually nothing is known about the mechanisms of the developmental regulation or the turnover of these proteins. We studied mechanisms that might be responsible for the developmentally regulated changes in the activity of a lectin (beta-galactoside-binding protein) found in the lung, and determined if its activity or turnover could be modulated by treatment of rat pups with a glucocorticosteroid hormone (dexamethasone). Our studies on the activity and turnover of the lectin indicated that the peak of lectin activity (units/mg of protein) that occurred at age 12 days appeared to be brought about by two means: an increase in the activity of the lectin molecule itself (units/micrograms of lectin) that occurred at age 8 days, and 1.5-fold increase in the absolute rate of lectin synthesis at age 11 days. The decline in lectin activity was associated with a decrease in its rate of synthesis, return to the baseline extent of activation, and an increased rate of degradation. Treatment of rat pups with dexamethasone diminished the peak of lectin activity (units/mg of protein) by about 25%. This effect of dexamethasone was due, at least in part, to the complete prevention of activation of the lectin molecule (units/micrograms of lectin) and a premature increase in the rate of lectin degradation. Perhaps the normal fall in lectin activity after age 11 days is caused by mechanisms induced by the increase in serum corticosteroid that occurs at that age.


1984 ◽  
Vol 104 (4_Supplb) ◽  
pp. S91-S92
Author(s):  
G. DAXENBICHLER ◽  
E. H. MOSER
Keyword(s):  
Rat Lung ◽  

Neonatology ◽  
1995 ◽  
Vol 67 (4) ◽  
pp. 254-263 ◽  
Author(s):  
N. Benlounes ◽  
R. Chedid ◽  
F. Thuillier ◽  
J.F. Desjeux ◽  
F. Rousselet ◽  
...  

1992 ◽  
Vol 268 (2) ◽  
pp. 277-281 ◽  
Author(s):  
Kojiro Wasano ◽  
Yasuhiro Hirakawa ◽  
Keiichiro Nakamura

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