| Chapter title |
Human neutrophil granule cationic protein CAP37 is a specific macrophage chemotaxin that shares homology with inflammatory proteinases.
|
|---|---|
| Chapter number | 11 |
| Book title |
Chemotactic Cytokines
|
| Published in |
Advances in experimental medicine and biology, January 1991
|
| DOI | 10.1007/978-1-4684-6009-4_11 |
| Pubmed ID | |
| Book ISBNs |
978-1-4684-6011-7, 978-1-4684-6009-4
|
| Authors |
J G Morgan, H A Pereira, T Sukiennicki, J K Spitznagel, J W Larrick, Morgan, John G., Pereira, H. Anne, Sukiennicki, Teresa, Spitznagel, John K., Larrick, James W. |
| Abstract |
Cationic antimicrobial protein CAP37 (Mr = 37 kD) is derived from the azurophilic granules of human PMN. In vitro and in vivo studies demonstrate that CAP37 is a novel monocyte-specific chemoattractant. The N-terminal amino acid sequence of CAP37 shares significant homology with a number of inflammatory molecules with protease activity including elastase and cathepsin G. However, substitutions in the catalytic triad (serine for a histidine at position 41 and glycine for a serine at position 175), may account for its lack of serine protease activity. A full length cDNA for CAP37 was identified in an HL60 cDNA library screened with oligonucleotide probes designed from the N-terminal amino acid sequence. Sequencing of the cDNA reveals a protein of 225 amino acids with significant nucleotide homology to cathepsin G and human neutrophil elastase. |
Mendeley readers
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 6 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 2 | 33% |
| Professor | 1 | 17% |
| Other | 1 | 17% |
| Student > Master | 1 | 17% |
| Researcher | 1 | 17% |
| Other | 0 | 0% |
| Readers by discipline | Count | As % |
|---|---|---|
| Medicine and Dentistry | 3 | 50% |
| Agricultural and Biological Sciences | 2 | 33% |
| Immunology and Microbiology | 1 | 17% |