Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.4.24.35 (
matrix metalloproteinase 9
)
2,207
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The shedding of membrane vesicles from the cell surface is a vital process considered to be involved in cell-cell and cell-matrix interactions and in tumor progression. By immunoelectron microscopic analysis of surface replicas of 8701-BC human breast carcinoma cells, we observed that membrane vesicles shed from plasma membranes contained densely clustered
gelatinase B
[
matrix metalloproteinase 9
(
MMP-9
)], beta1 integrins, and human
lymphocyte antigen
class I molecules. By contrast, alpha-folate receptor was uniformly distributed on the smooth cell membrane and shedding areas. Both cell surface clustering of selected molecules and membrane vesicle release were evident only when cells were cultured in the presence of serum. Vesicle shedding occurred preferentially at the edge or along narrow protrusions of the cell. Specific accumulation of proMMP-9 and active forms of
MMP-9
in shed vesicles was also demonstrated by gelatin zymography. In addition, Western blotting analysis showed the presence of a large amount of proMMP-9/tissue inhibitor of metalloproteinase 1 complex. The release of selected areas of plasma membranes enriched with
MMP-9
and beta1 integrins indicates that membrane vesicle shedding from tumor cells plays an important role in the directional proteolysis of the extracellular matrix during cellular migration. The presence of human
lymphocyte antigen
class I antigens suggests a mechanism for tumor cells to escape from immune surveillance.
...
PMID:Selective localization of matrix metalloproteinase 9, beta1 integrins, and human lymphocyte antigen class I molecules on membrane vesicles shed by 8701-BC breast carcinoma cells. 976 80
Cannabinoid receptor (CB)
2
is an immune cell-localized GPCR that has been hypothesized to regulate the magnitude of inflammatory responses. However, there is currently no consensus as to the mechanism by which CB
2
mediates its anti-inflammatory effects
in vivo
. To address this question, we employed a murine dorsal air pouch model with wild-type and CB
2
-/-
8-12-wk-old female and male C57BL/6 mice and found that acute neutrophil and
lymphocyte antigen
6 complex, locus C
hi
monocyte recruitment in response to Zymosan was significantly enhanced in CB
2
-/-
mice. Additionally, levels of
matrix metalloproteinase 9
and the chemokines C-C motif chemokine ligand (CCL)2, CCL4, and C-X-C motif chemokine ligand 10 in CB
2
-/-
pouch exudates were elevated at earlier time points. Importantly, using mixed bone marrow chimeras, we revealed that the proinflammatory phenotype in CB
2
-/-
mice is neutrophil-intrinsic rather than stromal cell-dependent. Indeed, neutrophils isolated from CB
2
-/-
mice exhibited an enhanced migration-related transcriptional profile and increased adhesive phenotype, and treatment of human neutrophils with a CB
2
agonist blocked their endothelial transmigration. Overall, we have demonstrated that CB
2
plays a nonredundant role during acute neutrophil mobilization to sites of inflammation and, as such, it could represent a therapeutic target for the development of novel anti-inflammatory compounds to treat inflammatory human diseases.-Kapellos, T. S., Taylor, L., Feuerborn, A., Valaris, S., Hussain, M. T., Rainger, G. E., Greaves, D. R., Iqbal, A. J. Cannabinoid receptor 2 deficiency exacerbates inflammation and neutrophil recruitment.
...
PMID:Cannabinoid receptor 2 deficiency exacerbates inflammation and neutrophil recruitment. 3079 31
