Molecular cloning and sequence analysis of human preprocathepsin C

Area of Science:

• Molecular Biology
• Genetics
• Biochemistry

Background:

• Cathepsin C is a cysteine protease involved in various biological processes.
• Understanding human cathepsin C is crucial for its role in health and disease.

Purpose of the Study:

• To isolate and characterize the human preprocathepsin C cDNA.
• To determine the nucleotide sequence and deduce the amino acid sequence of human cathepsin C.
• To investigate the evolutionary relationship of human cathepsin C with other proteases.

Main Methods:

• Isolation of a human preprocathepsin C cDNA clone (C1) from a human ileum cDNA library.
• Utilized a rat kidney-derived reverse transcription-polymerase chain reaction (RT-PCR) probe for isolation.
• Determined the complete nucleotide sequence of the cDNA clone.
• Performed multiple sequence alignment for comparative analysis.

Main Results:

• Successfully isolated and sequenced the full-length 1857 bp cDNA clone for human preprocathepsin C.
• The sequence codes for a protein of 463 amino acid residues with a molecular mass of 51848 Da.
• Deduced amino acid sequence shows 87.5% identity to rat preprocathepsin C.
• Alignment confirms human cathepsin C (233 residues for mature protein) belongs to the papain superfamily of cysteine proteinases.

Conclusions:

• The study provides the complete sequence of human preprocathepsin C.
• Human cathepsin C is highly conserved among mammalian species.
• This characterization contributes to understanding the structure and function of papain superfamily proteases.