Lysosomal carboxypeptidase A |
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Authors: | Gacko Marek Worowska Anna Wo?niak Arkadiusz Jedynak Monika Panek Bogus?aw Lapiński Rados?aw |
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Institution: | Department of Vascular Surgery and Transplantation, Medical University of Bia?ystok, 24a M. Sk?odowska-Curie St., 15-269 Bia?ystok, Poland. chirnacz@amb.edu.pl |
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Abstract: | Lysosomal carboxypeptidase A (cathepsin A) is synthetized in the form of preproenzyme, which undergoes to active enzyme as a result of post-translational modification. It splits off C-terminal amino acid residues from peptides and proteins and synergizes with other proteases in degradation of cellular proteins in lysosomes. Lysosomal carboxypeptidase A has an effect on peptide hormones and peptides of biological activity of tissues and body fluids as well. It forms complexes with some glycosidases that protects them against proteolytic degradation. Deficiency of this enzyme induces storage diseases. Lysosomal carboxypeptidase A as multifunctional enzyme plays an important regulatory role in organismal metabolism. |
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