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Advances in Metalloproteinase
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Advances in Metalloproteinase

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Macromolecules".

Deadline for manuscript submissions: 20 July 2025 | Viewed by 2290

Special Issue Editor

Dr. Kyu-Yeon Han

E-Mail Website
Guest Editor
Department of Ophthalmology and Visual Sciences, Illinois Eye and Ear Infirmary, College of Medicine, University of Illinois at Chicago, Chicago, IL 60612, USA
Interests: matrix metalloproteinases; VEGF and VEGF receptors; MMPs inhibitors; angiogenesis; wound healing; cornea
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Matrix metalloproteinases (MMPs) are a family of calcium-dependent zinc-containing endopeptidases that actively participate in the degradation of the extracellular matrix. These MMPs play pivotal roles in various pathological conditions, including cancer, inflammation, angiogenesis, atheroma, arthritis, and ulceration. Understanding the specific roles of MMPs in these processes is crucial for developing targeted therapeutic interventions. In some cases, MMP inhibitors are being explored as potential treatments for diseases where MMP activity is dysregulated.

This Special Issue, titled “Advances in Metalloproteinase”, delves into the intricate functions of MMPs, their substrate specificity, tissue inhibitors of metalloproteinases, and the activation of proMMP in disease contexts. We invite contributions in the form of original research and review articles focusing on the diverse aspects of MMPs.

Dr. Kyu-Yeon Han
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • matrix metalloproteinases (MMPs)
  • substrate specificity
  • pathological condition
  • metalloproteinases inhibitors

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Published Papers (3 papers)

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Research

14 pages, 749 KiB  
Article
Plasma Levels of Matrilysins (MMP-7 and MMP-26) and Stromelysins (MMP-3 and MMP-10) in Diagnosis of Endometrial Cancer Patients
by Ewa Gacuta, Michał Ławicki, Monika Kulesza, Paweł Ławicki, Aleksandra Kicman, Emilia Łubińska and Sławomir Ławicki
Int. J. Mol. Sci. 2025, 26(8), 3824; https://doi.org/10.3390/ijms26083824 - 18 Apr 2025
Viewed by 186
Abstract
Metalloproteinases (MMPs) play a significant role in cancer pathogenesis. We investigated the levels of MMP-7, MMP-26, MMP-3, and MMP-10 in comparison with the levels of a tumor marker (CA125) in the plasma of postmenopausal patients in early stages of endometrial cancer (EC) compared [...] Read more.
Metalloproteinases (MMPs) play a significant role in cancer pathogenesis. We investigated the levels of MMP-7, MMP-26, MMP-3, and MMP-10 in comparison with the levels of a tumor marker (CA125) in the plasma of postmenopausal patients in early stages of endometrial cancer (EC) compared with control groups: patients with benign lesions (myoma uteri) and healthy controls. Plasma MMP levels were determined by ELISA and CA125 by CMIA methods. The study showed that plasma MMP-7 levels were significantly higher in EC patients compared to both control groups, whereas MMP-3 and MMP-26 levels were significantly higher in EC patients than in healthy women. MMP-7 showed the highest diagnostic sensitivity (SE), specificity (SP), positive (PPV) and negative predictive value (NPV), and diagnostic power (AUC) compared to other MMPs or CA125 in EC patients overall and patients with stage I and II EC. A combined analysis showed higher SE, NPV, and AUC levels in total EC patients and stage I and II EC patients—with the highest values for the combination MMP-7+CA125 (96%, 92%, 95%; 95%, 96%, and 98%; 0.9420, 0.9158, and 0.9693, respectively) or MMP-26 with CA125 (86%, 86%, and 86%; 59%, 73%, 73%; 0.8219, 0.8086, and 0.8353, respectively). The results suggest the usefulness of MMPs, especially MMP-7 and MMP-26, in combined panels with CA125 in diagnosing EC patients. Full article
(This article belongs to the Special Issue Advances in Metalloproteinase)
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10 pages, 366 KiB  
Article
A Single Bout of Physical Exercise Mimicking a Motor Seizure Increases Serum MMP-9, but Not S100B
by Jan Karol Sielczak, Maciej Krawczyk, Agnieszka Cudna and Iwona Kurkowska-Jastrzębska
Int. J. Mol. Sci. 2025, 26(5), 1906; https://doi.org/10.3390/ijms26051906 - 23 Feb 2025
Viewed by 515
Abstract
MMP-9 and S100B, the proteins involved in blood-brain barrier integrity, are widely studied as biomarkers in many diseases, including epilepsy. They are elevated in epilepsy patients both interictally and following motor seizures. To determine whether motor activity influences their serum concentrations, we investigated [...] Read more.
MMP-9 and S100B, the proteins involved in blood-brain barrier integrity, are widely studied as biomarkers in many diseases, including epilepsy. They are elevated in epilepsy patients both interictally and following motor seizures. To determine whether motor activity influences their serum concentrations, we investigated the effects of brief, seizure-like physical exercise on serum MMP-9 and S100B levels in healthy individuals. Participants performed two different 5-min exercise protocols mimicking the motor activity of bilateral tonic–clonic seizures, one of the sets of exercises that contribute to to muscle failure. Serum samples were collected before exercise, 3 h after exercise, and the next day (time points 0, 3 h, and 24 h). Our results demonstrated that both sets of motor exercises led to a similar increase in MMP-9 levels, while neither affected S100B levels. No significant differences in MMP-9 levels were observed due to muscle failure. We suggest that the increase in MMP-9 seen after seizures is induced partially by peripheral mechanisms, such as muscle contraction. S100B appears to be a promising biomarker in epilepsy, as it is not induced by physical activity but does increase following seizures. Further research is needed to fully elucidate the mechanisms underlying biomarker release in epilepsy and to determine the specific contributions of muscle contractions versus other seizure-related processes. Full article
(This article belongs to the Special Issue Advances in Metalloproteinase)
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21 pages, 6017 KiB  
Article
Structure-Function Relationship of the β-Hairpin of Thermus thermophilus HB27 Laccase
by Beatriz Miranda-Zaragoza, Guillermo A. Huerta-Miranda, Wendy I. García-García, Elizabeth Hernández-Álvarez, Alejandro Solano-Peralta, Jaeyong Lee, Natalie Strynadka, Margarita Miranda-Hernández and Claudia Rodríguez-Almazán
Int. J. Mol. Sci. 2025, 26(2), 735; https://doi.org/10.3390/ijms26020735 - 16 Jan 2025
Viewed by 942
Abstract
Thermus thermophilus HB27 laccase (Tth-Lac) is a thermostable enzyme that contains a β-hairpin (Ala292-Gln307) covering the substrate entrance. We analyzed the role of this β-hairpin in the enzymatic activity of Tth-Lac through three β-hairpin mutants: two variants without the β-hairpin (C1Tth-Lac and C2Tth-Lac) [...] Read more.
Thermus thermophilus HB27 laccase (Tth-Lac) is a thermostable enzyme that contains a β-hairpin (Ala292-Gln307) covering the substrate entrance. We analyzed the role of this β-hairpin in the enzymatic activity of Tth-Lac through three β-hairpin mutants: two variants without the β-hairpin (C1Tth-Lac and C2Tth-Lac) and one with a partially modified β-hairpin (P1Tth-Lac). Enzymatic activity was assayed with different substrates with and without copper. C1Tth-Lac showed a higher dependency on copper, increasing its activity by 1600-fold for syringaldazine (SGZ). All mutants presented a higher activity than Tth-Lac with phenolic substrates in the presence of copper. The position of the signal associated with CuT2 also changed, as shown in EPR spectra. Elucidation of the crystal structure of P1Tth-Lac mutant (PDB: 9CPM) showed that the partial deletion of the β-hairpin did not significantly affect the overall tertiary structure compared to the wild-type (PDB: 2xu9) nor the coordination of the four internally bound Cu atoms. Higher B-factors of the residues downstream of the deletion indicate increased flexibility (Q307, G308, P309, S310) that were otherwise more ordered in the Tth-Lac structure. Redox potential experiments on platinum electrodes have shown that all proteins have high redox potential, a finding that could have significant implications in the field of protein research. Full article
(This article belongs to the Special Issue Advances in Metalloproteinase)
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