A novel murine cathelin-like protein expressed in bone marrow
| Autor: | Marina V. Zinovjeva, Willem E. Fibbe, J. Mark J. M. Zijlmans, Alexander V. Belyavsky, Anna E. Popsueva, Jan W.M. Visser |
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| Rok vydání: | 1996 |
| Předmět: |
DNA
Complementary Swine Molecular Sequence Data Antimicrobial peptides Biophysics Gene Expression Peptide Amphipathic α-helix Biology Biochemistry Protein Structure Secondary Mice Bone Marrow Cathelicidins Structural Biology Complementary DNA Genetics medicine Animals Amino Acid Sequence Cloning Molecular Protein Precursors Molecular Biology Protein secondary structure chemistry.chemical_classification Base Sequence Sequence Homology Amino Acid Proteins Hematopoietic stem/progenitor cells Cell Biology Antimicrobial Molecular biology Cathelin Antibacterial protein medicine.anatomical_structure chemistry Organ Specificity Protein Biosynthesis Indolicidin Bone marrow Antibacterial activity cDNA Antimicrobial Cationic Peptides |
| Zdroj: | FEBS Letters. 391:5-8 |
| ISSN: | 0014-5793 |
| Popis: | A novel cDNA encoding a putative secreted protein was isolated from murine bone marrow. The encoded protein named MCLP ( m urine c athelin- l ike p rotein) was found to be highly homologous to the pig cathelin, and to four neutrophil antimicrobial polypeptides: CAP 18, indolicidin, Bac 5 and FALL-39. Secondary structure prediction studies identified a highly cationic region in the C-terminal part of prepro-MCLP with a tendency to adopt an amphipathic α-helical conformation, as observed in many antimicrobial peptides. However, no antibacterial activity was observed with the synthetic peptide corresponding to this region of MCLP. |
| Databáze: | OpenAIRE |
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