Multifunctional intracellular matrix metalloproteinases: implications in disease

Matrix metalloproteinases (MMPs) are zinc‐dependent endopeptidases that were first discovered as proteases, which target and cleave extracellular proteins. During the past 20 years, however, intracellular roles of MMPs were uncovered and research on this new aspect of their biology expanded. MMP‐2 i...

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Published inThe FEBS journal Vol. 288; no. 24; pp. 7162 - 7182
Main Authors Bassiouni, Wesam, Ali, Mohammad A. M., Schulz, Richard
Format Journal Article
LanguageEnglish
Published England Blackwell Publishing Ltd 01.12.2021
Subjects
Animals
cancer
Cardiomyocytes
cardiovascular disease
Cardiovascular Diseases - enzymology
Cytosol
Humans
inflammation
Intracellular
Malignancy
Matrix metalloproteinase
Matrix metalloproteinases
Matrix Metalloproteinases - metabolism
metalloproteinases
Mitochondria
Myocytes
Neoplasms - enzymology
nucleus
Oxidative stress
Pathogenesis
Protease
Proteinase
Proteins
proteolysis
sarcomere
sarcomeres
Substrates
cardiovascular disease
cytosol
inflammation
mitochondria
matrix metalloproteinase
nucleus
cancer
proteolysis
sarcomere
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Abstract Matrix metalloproteinases (MMPs) are zinc‐dependent endopeptidases that were first discovered as proteases, which target and cleave extracellular proteins. During the past 20 years, however, intracellular roles of MMPs were uncovered and research on this new aspect of their biology expanded. MMP‐2 is the first of this protease family to be reported to play a crucial intracellular role where it cleaves several sarcomeric proteins inside cardiac myocytes during oxidative stress‐induced injury. Beyond MMP‐2, currently at least eleven other MMPs are known to function intracellularly including MMP‐1, MMP‐3, MMP‐7, MMP‐8, MMP‐9, MMP‐10, MMP‐11, MMP‐12, MMP‐14, MMP‐23 and MMP‐26. These intracellular MMPs are localized to different compartments inside the cell including the cytosol, sarcomere, mitochondria, and the nucleus. Intracellular MMPs contribute to the pathogenesis of various diseases. Cardiovascular renal disorders, inflammation, and malignancy are some examples. They also exert antiviral and bactericidal effects. Interestingly, MMPs can act intracellularly through both protease‐dependent and protease‐independent mechanisms. In this review, we will highlight the intracellular mechanisms of MMPs activation, their numerous subcellular locales, substrates, and roles in different pathological conditions. We will also discuss the future direction of MMP research and the necessity to exploit the knowledge of their intracellular targets and actions for the design of targeted inhibitors. Matrix metalloproteinases (MMPs) were first discovered as secreted proteases that cleave extracellular matrix proteins. However, by different mechanisms, they can also remain inside the cell and localize to different subcellular compartments and organelles including, for example, the cytosol, mitochondria, nuclei, and sarcomere. When intracellularly activated, MMPs can also proteolyze specific intracellular proteins to affect both pathological and physiological responses.
AbstractList Matrix metalloproteinases (MMPs) are zinc-dependent endopeptidases that were first discovered as proteases, which target and cleave extracellular proteins. During the past 20 years, however, intracellular roles of MMPs were uncovered and research on this new aspect of their biology expanded. MMP-2 is the first of this protease family to be reported to play a crucial intracellular role where it cleaves several sarcomeric proteins inside cardiac myocytes during oxidative stress-induced injury. Beyond MMP-2, currently at least eleven other MMPs are known to function intracellularly including MMP-1, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-14, MMP-23 and MMP-26. These intracellular MMPs are localized to different compartments inside the cell including the cytosol, sarcomere, mitochondria, and the nucleus. Intracellular MMPs contribute to the pathogenesis of various diseases. Cardiovascular renal disorders, inflammation, and malignancy are some examples. They also exert antiviral and bactericidal effects. Interestingly, MMPs can act intracellularly through both protease-dependent and protease-independent mechanisms. In this review, we will highlight the intracellular mechanisms of MMPs activation, their numerous subcellular locales, substrates, and roles in different pathological conditions. We will also discuss the future direction of MMP research and the necessity to exploit the knowledge of their intracellular targets and actions for the design of targeted inhibitors.
Matrix metalloproteinases (MMPs) are zinc‐dependent endopeptidases that were first discovered as proteases, which target and cleave extracellular proteins. During the past 20 years, however, intracellular roles of MMPs were uncovered and research on this new aspect of their biology expanded. MMP‐2 is the first of this protease family to be reported to play a crucial intracellular role where it cleaves several sarcomeric proteins inside cardiac myocytes during oxidative stress‐induced injury. Beyond MMP‐2, currently at least eleven other MMPs are known to function intracellularly including MMP‐1, MMP‐3, MMP‐7, MMP‐8, MMP‐9, MMP‐10, MMP‐11, MMP‐12, MMP‐14, MMP‐23 and MMP‐26. These intracellular MMPs are localized to different compartments inside the cell including the cytosol, sarcomere, mitochondria, and the nucleus. Intracellular MMPs contribute to the pathogenesis of various diseases. Cardiovascular renal disorders, inflammation, and malignancy are some examples. They also exert antiviral and bactericidal effects. Interestingly, MMPs can act intracellularly through both protease‐dependent and protease‐independent mechanisms. In this review, we will highlight the intracellular mechanisms of MMPs activation, their numerous subcellular locales, substrates, and roles in different pathological conditions. We will also discuss the future direction of MMP research and the necessity to exploit the knowledge of their intracellular targets and actions for the design of targeted inhibitors. Matrix metalloproteinases (MMPs) were first discovered as secreted proteases that cleave extracellular matrix proteins. However, by different mechanisms, they can also remain inside the cell and localize to different subcellular compartments and organelles including, for example, the cytosol, mitochondria, nuclei, and sarcomere. When intracellularly activated, MMPs can also proteolyze specific intracellular proteins to affect both pathological and physiological responses.
Matrix metalloproteinases (MMPs) are zinc-dependent endopeptidases that were first discovered as proteases, which target and cleave extracellular proteins. During the past 20 years, however, intracellular roles of MMPs were uncovered and research on this new aspect of their biology expanded. MMP-2 is the first of this protease family to be reported to play a crucial intracellular role where it cleaves several sarcomeric proteins inside cardiac myocytes during oxidative stress-induced injury. Beyond MMP-2, currently at least eleven other MMPs are known to function intracellularly including MMP-1, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-14, MMP-23 and MMP-26. These intracellular MMPs are localized to different compartments inside the cell including the cytosol, sarcomere, mitochondria, and the nucleus. Intracellular MMPs contribute to the pathogenesis of various diseases. Cardiovascular renal disorders, inflammation, and malignancy are some examples. They also exert antiviral and bactericidal effects. Interestingly, MMPs can act intracellularly through both protease-dependent and protease-independent mechanisms. In this review, we will highlight the intracellular mechanisms of MMPs activation, their numerous subcellular locales, substrates, and roles in different pathological conditions. We will also discuss the future direction of MMP research and the necessity to exploit the knowledge of their intracellular targets and actions for the design of targeted inhibitors.Matrix metalloproteinases (MMPs) are zinc-dependent endopeptidases that were first discovered as proteases, which target and cleave extracellular proteins. During the past 20 years, however, intracellular roles of MMPs were uncovered and research on this new aspect of their biology expanded. MMP-2 is the first of this protease family to be reported to play a crucial intracellular role where it cleaves several sarcomeric proteins inside cardiac myocytes during oxidative stress-induced injury. Beyond MMP-2, currently at least eleven other MMPs are known to function intracellularly including MMP-1, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-14, MMP-23 and MMP-26. These intracellular MMPs are localized to different compartments inside the cell including the cytosol, sarcomere, mitochondria, and the nucleus. Intracellular MMPs contribute to the pathogenesis of various diseases. Cardiovascular renal disorders, inflammation, and malignancy are some examples. They also exert antiviral and bactericidal effects. Interestingly, MMPs can act intracellularly through both protease-dependent and protease-independent mechanisms. In this review, we will highlight the intracellular mechanisms of MMPs activation, their numerous subcellular locales, substrates, and roles in different pathological conditions. We will also discuss the future direction of MMP research and the necessity to exploit the knowledge of their intracellular targets and actions for the design of targeted inhibitors.
Author Ali, Mohammad A. M.
Bassiouni, Wesam
Schulz, Richard
Author_xml – sequence: 1
  givenname: Wesam
  surname: Bassiouni
  fullname: Bassiouni, Wesam
  organization: University of Alberta
– sequence: 2
  givenname: Mohammad A. M.
  surname: Ali
  fullname: Ali, Mohammad A. M.
  email: mali@binghamton.edu
  organization: State University of New York‐Binghamton
– sequence: 3
  givenname: Richard
  orcidid: 0000-0002-5045-3193
  surname: Schulz
  fullname: Schulz, Richard
  email: richard.schulz@ualberta.ca
  organization: University of Alberta
BackLink https://www.ncbi.nlm.nih.gov/pubmed/33405316$$D View this record in MEDLINE/PubMed
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Issue 24
Keywords cardiovascular disease
cytosol
inflammation
mitochondria
matrix metalloproteinase
nucleus
cancer
proteolysis
sarcomere
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SecondaryResourceType review_article
Snippet Matrix metalloproteinases (MMPs) are zinc‐dependent endopeptidases that were first discovered as proteases, which target and cleave extracellular proteins....
Matrix metalloproteinases (MMPs) are zinc-dependent endopeptidases that were first discovered as proteases, which target and cleave extracellular proteins....
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SubjectTerms Animals
cancer
Cardiomyocytes
cardiovascular disease
Cardiovascular Diseases - enzymology
Cytosol
Humans
inflammation
Intracellular
Malignancy
Matrix metalloproteinase
Matrix metalloproteinases
Matrix Metalloproteinases - metabolism
metalloproteinases
Mitochondria
Myocytes
Neoplasms - enzymology
nucleus
Oxidative stress
Pathogenesis
Protease
Proteinase
Proteins
proteolysis
sarcomere
sarcomeres
Substrates
Title Multifunctional intracellular matrix metalloproteinases: implications in disease
URI https://onlinelibrary.wiley.com/doi/abs/10.1111%2Ffebs.15701
https://www.ncbi.nlm.nih.gov/pubmed/33405316
https://www.proquest.com/docview/2611549176
https://www.proquest.com/docview/2475533836
https://www.proquest.com/docview/2636384212
Volume 288
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