Function MMP9

1 function

1.1 neutrophil action
1.2 angiogenesis
1.3 wound repair

function

proteins of matrix metalloproteinase (mmp) family involved in breakdown of extracellular matrix in normal physiological processes, such embryonic development, reproduction, angiogenesis, bone development, wound healing, cell migration, learning , memory, in pathological processes, such arthritis, intracerebral hemorrhage, , metastasis. mmps secreted inactive proproteins activated when cleaved extracellular proteinases. enzyme encoded gene degrades type iv , v collagens , other extracellular matrix proteins. studies in rhesus monkeys suggest enzyme involved in il-8-induced mobilization of hematopoietic progenitor cells bone marrow, , murine studies suggest role in tumor-associated tissue remodeling.

thrombospondins, intervertebral disc proteins, regulate interaction matrix metalloproteinases (mmps) 2 , 9, key effectors of ecm remodeling.

neutrophil action

mmp9, along elastase, appears regulatory factor in neutrophil migration across basement membrane.

mmp9 plays several important functions within neutrophil action, such degrading extracellular matrix, activation of il-1β, , cleavage of several chemokines. in mouse model, mmp9 deficiency resulted in resistance endotoxin shock, suggesting mmp9 important in sepsis.

angiogenesis

mmp9 may play important role in angiogenesis , neovascularization. example, mmp9 appears involved in remodeling associated malignant glioma neovascularization. key regulator of growth plate formation- both growth plate angiogenesis , generation of hypertrophic chondrocytes. knock-out models of mmp9 result in delayed apoptosis, vascularization, , ossification of hypertrophic chondrocytes. lastly, there significant evidence gelatinase b required recruitment of endothelial stem cells, critical component of angiogenesis

wound repair

mmp9 upregulated during human respiratory epithelial healing. using mmp9 deficient mouse model, seen mmp9 coordinated epithelial wound repair , deficient mice unable remove fibrinogen matrix during wound healing. when interacting tgf-ß1, gelatinase b stimulates collagen contraction, aiding in wound closure.