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Cloning and expression of human apolipoprotein D cDNA
The Journal of Biological Chemistry
|December 15, 1986
Summary
Researchers determined the amino acid sequence of human apolipoprotein D, a high-density lipoprotein component. This protein shows homology to retinol-binding protein and alpha 2u-globulin superfamily members.
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- Apolipoprotein D (apoD) is a component of high-density lipoprotein (HDL).
- The complete amino acid sequence and functional characteristics of apoD are not fully elucidated.
Purpose of the Study:
- To obtain the amino acid sequence of human apolipoprotein D from its cloned cDNA.
- To investigate the structural and functional relationships of apoD with other proteins.
Main Methods:
- Cloning of apolipoprotein D cDNA.
- Amino acid sequencing.
- Homology analysis using bioinformatics tools.
- mRNA detection via Northern blot or in situ hybridization.
- Transfection of tissue culture cells with apoD cDNA.
Main Results:
- The 169-amino acid sequence of human apoD was determined.
- ApoD shows limited similarity to other apolipoproteins but significant homology to plasma retinol-binding protein and the alpha 2u-globulin superfamily.
- ApoD mRNA is expressed in various human tissues, including liver, intestine, and fetal brain.
- Transfected cells secrete apoD, confirming protein expression.
Conclusions:
- The deduced amino acid sequence provides a basis for understanding apoD structure and function.
- ApoD's homology suggests potential roles in lipid or retinol transport and its classification within the alpha 2u-globulin superfamily.
- The widespread tissue distribution of apoD mRNA indicates diverse physiological roles.