scholarly journals Characterization of Insulin-like Growth Factor-free Interaction between Insulin-like Growth Factor Binding Protein 3 and Acid Labile Subunit Expressed from Xenopus Oocytes

BMB Reports ◽  
2004 ◽  
Vol 37 (2) ◽  
pp. 153-158 ◽  
Author(s):  
Kyung-Yi Choi ◽  
Yoon-Joo Kyung ◽  
Chul-Young Lee ◽  
Dong-Hee Lee
Keyword(s):  
Growth Factor ◽  
Xenopus Oocytes ◽  
Binding Protein ◽  
Insulin Like Growth Factor ◽  
Factor Binding ◽  
Acid Labile Subunit ◽  
Free Interaction ◽  
Acid Labile

scholarly journals Measurement of the acid-labile subunit of the insulin-like growth factor binding protein complex in human serum: a comparison of four immunoassays

2000 ◽  
Vol 165 (2) ◽  
pp. 271-279 ◽  
Author(s):  
RC Baxter ◽  
M Svejkar ◽  
MJ Khosravi ◽  
GL Bennett ◽  
KV Hardman ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Growth Factor ◽  
Protein Complex ◽  
Binding Protein ◽  
Serum Marker ◽  
Healthy Children ◽  
Insulin Like Growth Factor ◽  
Factor Binding ◽  
Acid Labile Subunit ◽  
Acid Labile

The acid-labile subunit (ALS) of the high molecular weight insulin-like growth factor binding protein complex is a liver-derived glycoprotein which is regulated by growth hormone and serves as a serum marker of growth hormone action. We have compared the measurement of ALS by four immunoassay methods (two RIAs, two ELISAs) utilizing various polyclonal and monoclonal antibodies raised against natural or recombinant human ALS, or synthetic ALS peptides. Despite the variety of methodologies and reagents, results obtained by the four methods were highly correlated for 125 sera from various patient groups, and when compared for individual groups of sera from healthy children and adults, growth hormone-deficient children and adults, and subjects with acromegaly. Some weaker correlations among methods were seen when measuring ALS levels in groups of sera from pregnant subjects and subjects with chronic renal failure. An assay using antibodies raised against recombinant ALS yielded lower apparent values than the other methods in patient sera, the discrepancy probably being attributable to a difference in standardization. We conclude that a variety of assay formats and reagents can yield serum ALS values of potential clinical utility.

scholarly journals Molecular cloning of the porcine acid-labile subunit (ALS) of the insulin-like growth factor-binding protein complex and detection of ALS gene expression in hepatic and non-hepatic tissues

2001 ◽  
Vol 26 (2) ◽  
pp. 135-144 ◽  
Author(s):  
CY Lee ◽  
I Kwak ◽  
CS Chung ◽  
WS Choi ◽  
RC Simmen ◽  
...  
Keyword(s):  
Growth Factor ◽  
Genomic Dna ◽  
Binding Protein ◽  
Mrna Abundance ◽  
Daily Injection ◽  
Insulin Like Growth Factor ◽  
Factor Binding ◽  
Acid Labile Subunit ◽  
Low Levels ◽  
Acid Labile

The acid-labile subunit (ALS) is an approximately 85 kDa N-glycoprotein that is known primarily as a component of the systemic insulin-like growth factor-binding protein (IGFBP) complex. We have amplified, using a PCR, three overlapping porcine ALS genomic DNA fragments that together encode the distal region of the signal peptide through to the COOH-terminus. The compiled sequence of 1775 nucleotides of the three overlapping DNAs and the deduced amino acid sequence of the mature porcine ALS (pALS) protein exhibited 84/81%, 79/77%, 79/78% and 84/79% identities with respect to those of the human, the rat, the mouse and the baboon respectively. Four conserved cysteine residues in the NH(2)-terminal domain and 20 leucine-rich repeats in the central domain also were identified at identical positions in the porcine ALS. By using Northern blot analysis, with a genomic DNA fragment as the probe, it was determined that a 2.2 kb ALS mRNA was induced in the liver during the late fetal stage, and hepatic ALS mRNA abundance was increased post-natally. Moreover, hepatic ALS mRNA abundance was increased by daily injection of porcine somatotropin (100 microg/kg body weight) in cross-bred market pigs each weighing approximately 100 kg. The ALS mRNA was not detected by Northern analysis in any non-hepatic tissue examined. However, results of a more sensitive solution hybridization/RNAse protection assay indicated that low levels of ALS mRNA were also present in adult muscle, spleen, ovary and uterus, but not in lung, kidney, oviduct and placenta. Taken together, the present results suggest that although liver is the primary organ that expresses the ALS gene under somatotropin stimulation, some non-hepatic tissues also express the gene at low levels in the pig.

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