| First Author | MacIvor DM | Year | 1999 |
| Journal | Blood | Volume | 94 |
| Issue | 12 | Pages | 4282-93 |
| PubMed ID | 10590073 | Mgi Jnum | J:59006 |
| Mgi Id | MGI:1350771 | Doi | 10.1182/blood.v94.12.4282.424k45_4282_4293 |
| Citation | MacIvor DM, et al. (1999) Normal neutrophil function in cathepsin G-deficient mice. Blood 94(12):4282-93 |
| abstractText | Cathepsin G is a neutral serine protease that is highly expressed at the promyelocyte stage of myeloid development. We have developed a homologous recombination strategy to create a loss-of-function mutation for murine cathepsin G. Bone marrow derived from mice homozygous for this mutation had no detectable cathepsin G protein or activity, indicating that no other protease in bone marrow cells has the same specificity. Hematopoiesis in cathepsin G-/- mice is normal, and the mice have no overt abnormalities in blood clotting. Neutrophils derived from cathepsin G-/- mice have normal morphology and azurophil granule composition; these neutrophils also display normal phagocytosis and superoxide production and have normal chemotactic responses to C5a, fMLP, and interleukin-8. Although cathepsin G has previously shown to have broad spectrum antibiotic properties, challenges of mice with Staphylococcus aureus, Klebsiella pneumoniae, or Escherichia coli yielded survivals that were not different from those of wild-type animals. In sum, cathepsin G-/- neutrophils have no obvious defects in function; either cathepsin G is not required for any of these normal neutrophil functions or related azurophil granule proteases with different specificities (ie, neutrophil elastase, proteinase 3, azurocidin, and/or others) can substitute for it in vivo. |
