Matrix Metalloproteinase-19 Promotes Metastatic Behavior<i>In Vitro</i>and Is Associated with Increased Mortality in Non–Small Cell Lung Cancer

Yu, Guoying; Herazo-Maya, José D.; Nukui, Tomoko; Romkes, Marjorie; Parwani, Anil V.; Juan-Guardela, Brenda; Robertson, John C.; Gauldie, Jack; Siegfried, Jill M.; Kaminski, Naftali; Kass, Daniel J.

doi:10.1164/rccm.201310-1903oc

Cited by 55 publications

(47 citation statements)

References 55 publications

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“…Thus MMP-19 may be associated with the development and progression of non-small cell lung cancer and may be a potential biomarker of disease severity and outcome. 186 …”

Section: Special Attributes Of Specific Mmpsmentioning

confidence: 99%

Biochemical and Biological Attributes of Matrix Metalloproteinases

Cui

Khalil

2017

Progress in Molecular Biology and Translational Science

1,005

891

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Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that are involved in the degradation of various proteins in the extracellular matrix (ECM). Typically, MMPs have a propeptide sequence, a catalytic metalloproteinase domain with catalytic zinc, a hinge region or linker peptide, and a hemopexin domain. MMPs are commonly classified on the basis of their substrates and the organization of their structural domains into collagenases, gelatinases, stromelysins, matrilysins, membrane-type (MT)-MMPs, and other MMPs. MMPs are secreted by many cells including fibroblasts, vascular smooth muscle (VSM) and leukocytes. MMPs are regulated at the level of mRNA expression and by activation of their latent zymogen form. MMPs are often secreted as inactive proMMP form which is cleaved to the active form by various proteinases including other MMPs. MMPs cause degradation of ECM proteins such as collagen and elastin, but could influence endothelial cell function as well as VSM cell migration, proliferation, Ca2+ signaling and contraction. MMPs play a role in tissue remodeling during various physiological processes such as angiogenesis, embryogenesis, morphogenesis and wound repair, as well as in pathological conditions such as myocardial infarction, fibrotic disorders, osteoarthritis, and cancer. Increases in specific MMPs could play a role in arterial remodeling, aneurysm formation, venous dilation and lower extremity venous disorders. MMPs also play a major role in leukocyte infiltration and tissue inflammation. MMPs have been detected in cancer, and elevated MMP levels have been associated with tumor progression and invasiveness. MMPs can be regulated by endogenous tissue inhibitors of metalloproteinases (TIMPs), and the MMP/TIMP ratio often determines the extent of ECM protein degradation and tissue remodeling. MMPs have been proposed as biomarkers for numerous pathological conditions and are being examined as potential therapeutic targets in various cardiovascular and musculoskeletal disorders as well as cancer.

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“…Thus MMP-19 may be associated with the development and progression of non-small cell lung cancer and may be a potential biomarker of disease severity and outcome. 186 …”

Section: Special Attributes Of Specific Mmpsmentioning

confidence: 99%

Biochemical and Biological Attributes of Matrix Metalloproteinases

Cui

Khalil

2017

Progress in Molecular Biology and Translational Science

1,005

891

View full text Add to dashboard Cite

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“…Findings suggest that MMP‐19 is associated with the development and progression of non‐small cell lung cancer (NSCLC) and may be a potential biomarker of disease severity and outcome. Increased expression of MMP‐19 is associated with decreased survival in NSCLC patients (Yu et al, ). On the other hand, the expression of MMP‐19 in idiopathic pulmonary fibrosis (IPF) might be beneficial to the patients.…”

Section: Matrix Metalloproteinase‐19mentioning

confidence: 99%

Intricate Functions of Matrix Metalloproteinases in Physiological and Pathological Conditions

Mittal

Patel

Debs

et al. 2016

Journal Cellular Physiology

147

115

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Matrix metalloproteinases (MMPs) are a diverse group of proteolytic enzymes and play an important role in the degradation and remodeling of the extracellular matrix (ECM). In normal physiological conditions, MMPs are usually minimally expressed. Despite their low expression, MMPs have been implicated in many cellular processes ranging from embryological development to apoptosis. The activity of MMPs is controlled at three different stages: (1) transcription; (2) zymogen activation; and (3) inhibition of active forms by tissue inhibitor metalloproteinases (TIMPs). They can collectively degrade any component of ECM and basement membrane, and their excessive activity has been linked to numerous pathologies mainly including, but not limited to, tumor invasion and metastasis. The lack of information about several MMPs and the steady stream of new discoveries suggest that there is much more to be studied in this field. In particular, there is a need for controlling their expression in disease states. Various studies over the past 30 years have found that each MMP has a specific mode of activation, action, and inhibition. Drugs specifically targeting individual MMPs could revolutionize the treatment of a great number of health conditions and tremendously reduce their burden. In this review article, we have summarized the recent advances in understanding the role of MMPs in physiological and pathological conditions. J. Cell. Physiol. 231: 2599-2621, 2016. © 2016 Wiley Periodicals, Inc.

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“…MMP19 was cloned from a human liver cDNA library and the expression of mRNA was detected in several tissues (placenta, lung, pancreas, ovary, spleen, and intestine) [33]. Previous studies show the possible association between MMP19 and cancer development (lung cancer and ovarian cancer) [34,35], but no study has examined the relationship or expressions of MMP19 in placenta. This is the first study to demonstrate MMP19 protein expression in trophoblast.…”

Section: Discussionmentioning

confidence: 99%

Possible Association between Cathepsin V and the Development of Placenta Accreta Spectrum Disorders

Matsukawa

Sato

Kotani

et al. 2019

Gynecol Obstet Invest

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Background/Aims: The study aimed to evaluate molecular changes related to trophoblast adhesion in placenta accreta spectrum (PAS) disorders. Methods: A retrospective analysis of 10 PAS cases in which both the trophoblast adherent site and the non-adherent site were identified was performed in April 2010 and March 2013. Microarray analysis and reverse transcription polymerase chain reaction (RT-PCR) analyses were performed to extract upregulated genes in the adherent site. Gene expression changes were examined by immunohistochemistry. Results: Microarray analysis showed that 157 transcripts were > 3-fold upregulated, including the following: a disintegrin and metalloproteinase-28 (ADAM28), 3.10-fold; cathepsin V (CTSV), 3.73-fold; cathepsin S (CTSS), 3.46-fold; and matrix metalloproteinase-19 (MMP19), 3.41-fold. RT-PCR showed relatively high mRNA expressions. On immunohistochemistry, extravillous trophoblast (EVT) at the non-adherent site showed weak or no CTSV expression, whereas EVT that invaded myometrium at the adherent site showed strong expression (histological score, median [min-max], 115.6 [37.6–153.6] vs. 184.8 [56.4–222.8], p < 0.05). MMP19 showed moderate staining, with no difference between the adherent and non-adherent sites. ADAM28 and CTSS showed weak or no staining. Discussion: This limited study suggests that CTSV may be involved in the pathogenesis of PAS.

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Matrix Metalloproteinase-19 Promotes Metastatic BehaviorIn Vitroand Is Associated with Increased Mortality in Non–Small Cell Lung Cancer

Cited by 55 publications

References 55 publications

Biochemical and Biological Attributes of Matrix Metalloproteinases

Biochemical and Biological Attributes of Matrix Metalloproteinases

Intricate Functions of Matrix Metalloproteinases in Physiological and Pathological Conditions

Possible Association between Cathepsin V and the Development of Placenta Accreta Spectrum Disorders

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