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The distribution of latent and active matrilysin-1 (MMP-7) throughout the menstrual cycle was examined by immunohistochemistry in cryosections of human endometrium. ProMMP-7 was immunolocalized in the basal cytoplasm of epithelial cells, whereas the signal for active MMP-7 underlined epithelial cell periphery, suggesting association with their plasma membrane. Previous work in rat periphery, suggesting association with their plasma membrane. Previous work in rat uterine cells and on MMP-7 binding properties prompted us to hypothesize thaht MMP-7 preferentially binds to heparan sulfate proteoglycans, especially CD-44 isoforms containing the v3 exon. The nature of MMP-7 receptor was characterised by measuring membrane binding variations of recombinant active MMP-7 on cells from endometrial carcinoma in response to treatment with heparin and glycosidases. In parallel, we identified CD44 mRNA isoforms present in human endometrium, in particular those containing v3, and we measured their variations of expression throughout the menstrual cycle La distribution des formes latente et active de la matrilysine-1 (MMP-7)à au cours du cycle menstruel a été étudiée par immunohistochimie sur coupes d’endomètre humain. L’anticorps reconnaissant la forme latente de MMP-7 marque la cytoplasme du pôle basal des cellules épithéliales, tandis que l’anticorps dirigé contre la forme active souligne la périphérie des cellules épithéliales, produisant un marquage « en nid d’abeilles » qui suggère un accrochage à le membrane plasmique des cellules épithéliale. Compte tenu des affinités de liaison de la MMP-7 ainsi que de travaux antérieurs sur des cellules utérine de rat, nous avons émis l’hypothèse que les meilleurs candidats récepteurs étaient des protéoglycants à héparane sulfate, en particulier les isoformes du CD44 contenant l’exon v3. La nature du récepteur pour la MMP-7 a donc été caractérisée par mesure des variations de fixation membranaire de MMP-7 recombinante sur des cellules d’adénocarcinome endométrial (Ishikawa) en réponse à leur traitement à l’héparine ou par des glycosidases. En parallèle, nous avons identifié les isoformes d’ARNm de CD44 présentes dans l’endomètre humain, en particulier celles contenant l’exon v3, et nous en avons mesuré les variations d’expression au cours du cycle menstruel

Matrix Metalloproteinase 7 --- Epithelial Cells --- Endometrium

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Endometrium --- low Density Lipoprotein Receptor-Related Protein-2 --- Matrix Metalloproteinase 2

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Matrix metalloproteinases (MMPs) are members of an enzyme family and are critical for maintaining tissue allostasis. MMPs can catalyze normal turnover of the extracellular matrix (ECM) together with other metalloproteinases such as ADAM (a disintegrin and metalloproteinase) and ADAMTS (a disintegrin and metalloproteinase with thrombospondin motif) families. MMP activity is also regulated by a group of endogenous proteins called tissue inhibitor of metalloproteinases (TIMPs). All these proteins have a pivotal role involving ECM remodelling in normal physiological processes such as wound healing, embryogenesis, angiogenesis, bone remodelling, immunity, and the female reproductive cycle. An imbalance in the expression or activity of MMPs can also have important consequences in diseases such as cancer, cardiovascular disease, peripheral vascular disease, chronic leg ulcers, and multiple sclerosis. In recent years, MMPs have been found to play an important role in the field of precision medicine, as they may serve as biomarkers that may predict an individual’s disease predisposition, state, or progression. MMPs are also thought to be a sensible target for molecular therapy. The aim of this Special Issue is to explore the most recent findings in this field that may have an impact in healthcare systems.

Humanities --- Social interaction --- hypersensitivity pneumonitis --- metalloproteinases --- genetic association --- autoantibodies --- MMP1 --- MMP2 --- SNPs --- MMPs --- TIMPs --- CKD --- peripheral vascular disease --- biomarkers --- proteinuria --- eGFR --- PAD. --- NGAL --- statins --- arterial aneurysms --- patients --- collagenases --- Crohn’s disease --- dental caries --- mouth --- periodontitis --- matrix metalloproteinase-9 --- dialysis --- on-line hemodiafiltration --- high-flux dialysis --- renal replacement therapy --- kidney transplantation --- Mac-1 --- CD147 --- leukocytes --- platelets --- adhesion --- integrin αMβ2 --- matrix metalloproteinases --- TIMP --- synthetic inhibitors --- RECK --- matrix metalloproteinase --- MAPKs --- ischemia/reperfusion --- eNOS --- iNOS --- inflammatory bowel disease --- inflammation --- NO --- MMP-9 --- cGMP --- Caco-2 --- matrix metalloproteinase-7 --- fibrosis --- acute kidney injury --- chronic kidney disease --- apoptosis --- health --- disease

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Matrix metalloproteinases (MMPs) are members of an enzyme family and are critical for maintaining tissue allostasis. MMPs can catalyze normal turnover of the extracellular matrix (ECM) together with other metalloproteinases such as ADAM (a disintegrin and metalloproteinase) and ADAMTS (a disintegrin and metalloproteinase with thrombospondin motif) families. MMP activity is also regulated by a group of endogenous proteins called tissue inhibitor of metalloproteinases (TIMPs). All these proteins have a pivotal role involving ECM remodelling in normal physiological processes such as wound healing, embryogenesis, angiogenesis, bone remodelling, immunity, and the female reproductive cycle. An imbalance in the expression or activity of MMPs can also have important consequences in diseases such as cancer, cardiovascular disease, peripheral vascular disease, chronic leg ulcers, and multiple sclerosis. In recent years, MMPs have been found to play an important role in the field of precision medicine, as they may serve as biomarkers that may predict an individual’s disease predisposition, state, or progression. MMPs are also thought to be a sensible target for molecular therapy. The aim of this Special Issue is to explore the most recent findings in this field that may have an impact in healthcare systems.

Humanities --- Social interaction --- hypersensitivity pneumonitis --- metalloproteinases --- genetic association --- autoantibodies --- MMP1 --- MMP2 --- SNPs --- MMPs --- TIMPs --- CKD --- peripheral vascular disease --- biomarkers --- proteinuria --- eGFR --- PAD. --- NGAL --- statins --- arterial aneurysms --- patients --- collagenases --- Crohn’s disease --- dental caries --- mouth --- periodontitis --- matrix metalloproteinase-9 --- dialysis --- on-line hemodiafiltration --- high-flux dialysis --- renal replacement therapy --- kidney transplantation --- Mac-1 --- CD147 --- leukocytes --- platelets --- adhesion --- integrin αMβ2 --- matrix metalloproteinases --- TIMP --- synthetic inhibitors --- RECK --- matrix metalloproteinase --- MAPKs --- ischemia/reperfusion --- eNOS --- iNOS --- inflammatory bowel disease --- inflammation --- NO --- MMP-9 --- cGMP --- Caco-2 --- matrix metalloproteinase-7 --- fibrosis --- acute kidney injury --- chronic kidney disease --- apoptosis --- health --- disease --- hypersensitivity pneumonitis --- metalloproteinases --- genetic association --- autoantibodies --- MMP1 --- MMP2 --- SNPs --- MMPs --- TIMPs --- CKD --- peripheral vascular disease --- biomarkers --- proteinuria --- eGFR --- PAD. --- NGAL --- statins --- arterial aneurysms --- patients --- collagenases --- Crohn’s disease --- dental caries --- mouth --- periodontitis --- matrix metalloproteinase-9 --- dialysis --- on-line hemodiafiltration --- high-flux dialysis --- renal replacement therapy --- kidney transplantation --- Mac-1 --- CD147 --- leukocytes --- platelets --- adhesion --- integrin αMβ2 --- matrix metalloproteinases --- TIMP --- synthetic inhibitors --- RECK --- matrix metalloproteinase --- MAPKs --- ischemia/reperfusion --- eNOS --- iNOS --- inflammatory bowel disease --- inflammation --- NO --- MMP-9 --- cGMP --- Caco-2 --- matrix metalloproteinase-7 --- fibrosis --- acute kidney injury --- chronic kidney disease --- apoptosis --- health --- disease

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In the two last decades, proteases have constituted one of the primary and important targets in drug discovery. The U.S. FDA has approved more than 12 protease therapies in the last 10 years, and a number of next-generation or completely new proteases are under clinical development. Protease inhibition strategies are one of the fastest expanding areas in the field of of drugs that show considerable promise. This Special Issue will focus on the recent advances in the discovery and development of protease inhibitors, covering the synthesis of protease inhibitors, the design of new chemical entities acting as inhibitors of special/particular types of proteases, and their mode of actions (Frolova et al. 2020; Slapak et al. 2020; Künnapuu et al. 2021). In addition, the new applications of these interesting compounds/biomolecules and their limitations have been discussed and described (Wang et al. 2020; Bartošová-Sojková et al. 2021).

Research & information: general --- MMP --- MMP2 --- MMP9 --- MMP7 --- MMP14 --- matrix metalloproteases --- PDAC --- pancreatic cancer --- Bowman–Birk inhibitor --- ranacyclin --- trypsin inhibitor --- structure–activity relationship --- synergistic effect --- Gentamicin --- matrix metalloproteinase --- extracellular matrix --- nuclei --- cancer --- apoptosis --- immune response --- cysteine protease inhibitor --- stefin --- signal peptide --- parasite --- phylogenetic analysis --- diversification --- protein structure --- vascular endothelial growth factors (VEGFs) --- VEGF-A --- PlGF --- VEGF-B --- VEGF-C --- VEGF-D --- angiogenesis --- lymphangiogenesis --- CCBE1 --- proteases --- ADAMTS3 --- plasmin --- cathepsin D --- KLK3 --- prostate-specific antigen (PSA) --- thrombin --- wound healing --- metastasis --- proteolytic activation --- vascular biology --- lymphedema --- MMP --- MMP2 --- MMP9 --- MMP7 --- MMP14 --- matrix metalloproteases --- PDAC --- pancreatic cancer --- Bowman–Birk inhibitor --- ranacyclin --- trypsin inhibitor --- structure–activity relationship --- synergistic effect --- Gentamicin --- matrix metalloproteinase --- extracellular matrix --- nuclei --- cancer --- apoptosis --- immune response --- cysteine protease inhibitor --- stefin --- signal peptide --- parasite --- phylogenetic analysis --- diversification --- protein structure --- vascular endothelial growth factors (VEGFs) --- VEGF-A --- PlGF --- VEGF-B --- VEGF-C --- VEGF-D --- angiogenesis --- lymphangiogenesis --- CCBE1 --- proteases --- ADAMTS3 --- plasmin --- cathepsin D --- KLK3 --- prostate-specific antigen (PSA) --- thrombin --- wound healing --- metastasis --- proteolytic activation --- vascular biology --- lymphedema