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Molecular cloning of complementary DNA for human medullasin: an inflammatory serine protease in bone marrow cells
Abstract:
Medullasin, an inflammatory serine protease in bone marrow cells, modifies the functions of natural killer cells, monocytes, and granulocytes. We have cloned a medullasin cDNA from a human acute promyelocytic cell (ML3) cDNA library using oligonucleotide probes synthesized from the information of N-terminal amino acid sequence of natural medullasin. The cDNA contained a long open reading frame encoding 237 amino acid residues beginning from the second amino acid of natural meduallasin. The deduced amino acid sequence of medullasin shows a typical serine protease structure, with 41% homology with pig elastase 1.
Insights
Researchers cloned the medullasin cDNA, identifying it as an inflammatory serine protease. This enzyme modifies immune cell functions, showing structural similarity to pig elastase 1.
Area of Science:
- Biochemistry
- Immunology
- Molecular Biology
Background:
- Medullasin is an inflammatory serine protease found in bone marrow cells.
- It is known to modulate the functions of natural killer cells, monocytes, and granulocytes.
Purpose of the Study:
- To clone the medullasin cDNA from a human acute promyelocytic cell line.
- To analyze the deduced amino acid sequence and structural characteristics of medullasin.
Main Methods:
- Cloning of medullasin cDNA using oligonucleotide probes derived from the N-terminal amino acid sequence.
- Sequence analysis of the cloned cDNA to determine the open reading frame and deduce the amino acid sequence.
Main Results:
- Successfully cloned a medullasin cDNA from a human acute promyelocytic (ML3) cell line.
- The cDNA contains an open reading frame encoding 237 amino acid residues.
- The deduced amino acid sequence exhibits a typical serine protease structure with 41% homology to pig elastase 1.
Conclusions:
- Medullasin is a serine protease with structural similarities to other proteases like pig elastase 1.
- The cloning and sequencing provide a basis for further functional studies of medullasin in immune cell modulation.