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Biomedicines
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10th Anniversary of Biomedicines—Advances in Proteinases and Proteinase Inhibitors
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10th Anniversary of Biomedicines—Advances in Proteinases and Proteinase Inhibitors

A special issue of Biomedicines (ISSN 2227-9059). This special issue belongs to the section "Endocrinology and Metabolism Research".

Deadline for manuscript submissions: closed (30 April 2023) | Viewed by 18702

Special Issue Editor

Prof. Dr. Salvatore Vincent Pizzo

E-Mail Website
Guest Editor
Department of Pathology, Duke University Medical Center, Durham, NC 27710, USA
Interests: intracellular proteins; cell surface; signaling receptors; expression; GRP 78; cancer cell proliferation
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The year 2023 marks the 10th anniversary of Biomedicines, a peer-reviewed open access journal in the biomedical field. Thus far, Biomedicines has published more than 2700 papers from more than 17,000 authors. We appreciate each author, reviewer, and academic editor whose support has brought us to where we are today.

To celebrate this significant milestone, we aim to publish a Special Issue entitled “10th Anniversary of Biomedicines—Advances in Proteinases and Proteinase Inhibitors". Proteinases and their inhibitors are key regulators of many biological processes, including cancer. Indeed, about 20% of plasma proteins are proteinase inhibitors. The role of metalloproteinases in metastasis is well known, but this is not the only role of proteinases in the biology of cancer.

This Special Issue focuses on the role of proteinases and proteinase inhibitors in human health and diseases and aims to collect submissions of original research articles or review articles describing the current state of the art of the field.

Prof. Dr. Salvatore Vincent Pizzo
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. Biomedicines is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 CHF (Swiss Francs). 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

  • proteinases
  • proteinase inhibitors
  • cancer
  • metalloproteinases

Related Special Issue

Published Papers (7 papers)

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Research

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15 pages, 2096 KiB  
Article
Analysis of Membrane Type-1 Matrix Metalloproteinase (MT1-MMP, MMP14) in Eutopic and Ectopic Endometrium and in Serum and Endocervical Mucus of Endometriosis
by Jane B. Maoga, Muhammad A. Riaz, Agnes N. Mwaura, Ezekiel Mecha, Charles O. A. Omwandho, Georgios Scheiner-Bobis, Ivo Meinhold-Heerlein and Lutz Konrad
Biomedicines 2023, 11(10), 2730; https://0-doi-org.brum.beds.ac.uk/10.3390/biomedicines11102730 - 09 Oct 2023
Viewed by 931
Abstract
Background: Membrane type-matrix metalloproteinases (MT-MMPs) are a subgroup of the matrix metalloproteinases (MMPs) family and are key molecules in the degradation of the extracellular matrix. Membrane type-1 matrix metalloproteinase (MT1-MMP, MMP14) is often deregulated in different cancer tissues and body fluids of human [...] Read more.
Background: Membrane type-matrix metalloproteinases (MT-MMPs) are a subgroup of the matrix metalloproteinases (MMPs) family and are key molecules in the degradation of the extracellular matrix. Membrane type-1 matrix metalloproteinase (MT1-MMP, MMP14) is often deregulated in different cancer tissues and body fluids of human cancer patients; however, MT1-MMP levels in endometriosis and adenomyosis patients are currently unknown. Materials and Methods: Tissue samples from patients with and without endometriosis or adenomyosis were analyzed with immunohistochemistry for the localization of MT1-MMP. Serum and endocervical mucus samples from patients with and without endometriosis or adenomyosis were investigated with MT1-MMP ELISAs. Results: MT1-MMP was localized preferentially in the glands of eutopic and ectopic endometrium. MT1-MMP protein levels are significantly reduced in ovarian endometriosis (HSCORE = 31) versus eutopic endometrium (HSCORE = 91) and adenomyosis (HSCORE = 149), but significantly increased in adenomyosis (HSCORE = 149) compared to eutopic endometrium (HSCORE = 91). Similarly, analysis of the levels of MT1-MMP using enzyme-linked immune assays (ELISAs) demonstrated a significant increase in the concentrations of MT1-MMP in the serum of endometriosis patients (1.3 ± 0.8) versus controls (0.7 ± 0.2), but not in the endocervical mucus. Furthermore, MT1-MMP levels in the endocervical mucus of patients with endometriosis were notably reduced in patients using contraception (3.2 ± 0.4) versus those without contraception (3.8 ± 0.2). Conclusions: Taken together, our findings showed an opposite regulation of MT1-MMP in the tissue of ovarian endometriosis and adenomyosis compared to eutopic endometrium without endometriosis but increased serum levels in patients with endometriosis. Full article
(This article belongs to the Special Issue 10th Anniversary of Biomedicines—Advances in Proteinases and Proteinase Inhibitors)
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18 pages, 2535 KiB  
Article
Maquiberry Cystatins: Recombinant Expression, Characterization, and Use to Protect Tooth Dentin and Enamel
by Eduardo Pereira de Souza, Milene Ferro, Vinicius Taioqui Pelá, Thais Fernanda-Carlos, Cecília Guimarães Giannico Borges, Even Akemi Taira, Talita Mendes Oliveira Ventura, Ariel Domingo Arencibia, Marília Afonso Rabelo Buzalaf and Flávio Henrique-Silva
Biomedicines 2023, 11(5), 1360; https://0-doi-org.brum.beds.ac.uk/10.3390/biomedicines11051360 - 04 May 2023
Viewed by 1378
Abstract
Phytocystatins are proteinaceous competitive inhibitors of cysteine peptidases involved in physiological and defensive roles in plants. Their application as potential therapeutics for human disorders has been suggested, and the hunt for novel cystatin variants in different plants, such as maqui (Aristotelia chilensis [...] Read more.
Phytocystatins are proteinaceous competitive inhibitors of cysteine peptidases involved in physiological and defensive roles in plants. Their application as potential therapeutics for human disorders has been suggested, and the hunt for novel cystatin variants in different plants, such as maqui (Aristotelia chilensis), is pertinent. Being an understudied species, the biotechnological potential of maqui proteins is little understood. In the present study, we constructed a transcriptome of maqui plantlets using next-generation sequencing, in which we found six cystatin sequences. Five of them were cloned and recombinantly expressed. Inhibition assays were performed against papain and human cathepsins B and L. Maquicystatins can inhibit the proteases in nanomolar order, except MaquiCPIs 4 and 5, which inhibit cathepsin B in micromolar order. This suggests maquicystatins’ potential use for treating human diseases. In addition, since we previously demonstrated the efficacy of a sugarcane-derived cystatin to protect dental enamel, we tested the ability of MaquiCPI-3 to protect both dentin and enamel. Both were protected by this protein (by One-way ANOVA and Tukey’s Multiple Comparisons Test, p < 0.05), suggesting its potential usage in dental products. Full article
(This article belongs to the Special Issue 10th Anniversary of Biomedicines—Advances in Proteinases and Proteinase Inhibitors)
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17 pages, 9145 KiB  
Article
Screening MT1-MMP Activity and Inhibition in Three-Dimensional Tumor Spheroids
by Anna M. Knapinska, Gary Drotleff, Cedric Chai, Destiny Twohill, Alexa Ernce, Dorota Tokmina-Roszyk, Isabella Grande, Michelle Rodriguez, Brad Larson and Gregg B. Fields
Biomedicines 2023, 11(2), 562; https://0-doi-org.brum.beds.ac.uk/10.3390/biomedicines11020562 - 15 Feb 2023
Cited by 1 | Viewed by 2459
Abstract
Membrane type 1 matrix metalloproteinase (MT1-MMP) has been shown to be crucial for tumor angiogenesis, invasion, and metastasis, and thus MT1-MMP is a high priority target for potential cancer therapies. To properly evaluate MT1-MMP inhibitors, a screening protocol is desired by which enzyme [...] Read more.
Membrane type 1 matrix metalloproteinase (MT1-MMP) has been shown to be crucial for tumor angiogenesis, invasion, and metastasis, and thus MT1-MMP is a high priority target for potential cancer therapies. To properly evaluate MT1-MMP inhibitors, a screening protocol is desired by which enzyme activity can be quantified in a tumor microenvironment-like model system. In the present study, we applied a fluorogenic, collagen model triple-helical substrate to quantify MT1-MMP activity for tumor spheroids embedded in a collagen hydrogel. The substrate was designed to be MT1-MMP selective and to possess fluorescent properties compatible with cell-based assays. The proteolysis of the substrate correlated to glioma spheroid invasion. In turn, the application of either small molecule or protein-based MMP inhibitors reduced proteolytic activity and glioma spheroid invasion. The presence of MT1-MMP in glioma spheroids was confirmed by western blotting. Thus, spheroid invasion was dependent on MT1-MMP activity, and inhibitors of MT1-MMP and invasion could be conveniently screened in a high-throughput format. The combination of the fluorogenic, triple-helical substrate, the three-dimensional tumor spheroids embedded in collagen, and Hit-Pick software resulted in an easily adaptable in vivo-like tumor microenvironment for rapidly processing inhibitor potential for anti-cancer use. Full article
(This article belongs to the Special Issue 10th Anniversary of Biomedicines—Advances in Proteinases and Proteinase Inhibitors)
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18 pages, 2771 KiB  
Article
Aminopeptidase Activities Interact Asymmetrically between Brain, Plasma and Systolic Blood Pressure in Hypertensive Rats Unilaterally Depleted of Dopamine
by Inmaculada Banegas, Isabel Prieto, Ana Belén Segarra, Francisco Vives, Magdalena Martínez-Cañamero, Raquel Durán, Juan de Dios Luna, Germán Domínguez-Vías and Manuel Ramírez-Sánchez
Biomedicines 2022, 10(10), 2457; https://0-doi-org.brum.beds.ac.uk/10.3390/biomedicines10102457 - 01 Oct 2022
Viewed by 1343
Abstract
Brain dopamine, in relation to the limbic system, is involved in cognition and emotion. These functions are asymmetrically processed. Hypertension not only alters such functions but also their asymmetric brain pattern as well as their bilateral pattern of neurovisceral integration. The central and [...] Read more.
Brain dopamine, in relation to the limbic system, is involved in cognition and emotion. These functions are asymmetrically processed. Hypertension not only alters such functions but also their asymmetric brain pattern as well as their bilateral pattern of neurovisceral integration. The central and peripheral renin-angiotensin systems, particularly the aminopeptidases involved in its enzymatic cascade, play an important role in blood pressure control. In the present study, we report how these aminopeptidases from left and right cortico-limbic locations, plasma and systolic blood pressure interact among them in spontaneously hypertensive rats (SHR) unilaterally depleted of dopamine. The study comprises left and right sham and left and right lesioned (dopamine-depleted) rats as research groups. Results revealed important differences in the bilateral behavior comparing sham left versus sham right, lesioned left versus lesioned right, and sham versus lesioned animals. Results also suggest an important role for the asymmetrical functioning of the amygdala in cardiovascular control and an asymmetrical behavior in the interaction between the medial prefrontal cortex, hippocampus and amygdala with plasma, depending on the left or right depletion of dopamine. Compared with previous results of a similar study in Wistar-Kyoto (WKY) normotensive rats, the asymmetrical behaviors differ significantly between both WKY and SHR strains. Full article
(This article belongs to the Special Issue 10th Anniversary of Biomedicines—Advances in Proteinases and Proteinase Inhibitors)
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16 pages, 1571 KiB  
Article
Differential Distribution and Activity Profile of Acylpeptide Hydrolase in the Rat Seminiferous Epithelium
by Alejandra A. Covarrubias, Erwin De la Fuente-Ortega, Gabriela Rossi, Ennio Cocca, Mosè Rossi, Gianna Palmieri and Floria C. Pancetti
Biomedicines 2022, 10(7), 1591; https://0-doi-org.brum.beds.ac.uk/10.3390/biomedicines10071591 - 04 Jul 2022
Viewed by 1780
Abstract
Acylpeptide hydrolase (APEH) is a serine protease involved in amino acid recycling from acylated peptides (exopeptidase activity) and degradation of oxidized proteins (endoproteinase activity). This enzyme is inhibited by dichlorvos (DDVP), an organophosphate compound used as an insecticide. The role of APEH in [...] Read more.
Acylpeptide hydrolase (APEH) is a serine protease involved in amino acid recycling from acylated peptides (exopeptidase activity) and degradation of oxidized proteins (endoproteinase activity). This enzyme is inhibited by dichlorvos (DDVP), an organophosphate compound used as an insecticide. The role of APEH in spermatogenesis has not been established; therefore, the aim of this study was to characterize the distribution and activity profile of APEH during this process. For this purpose, cryosections of male reproductive tissues (testis and epididymis) and isolated cells (Sertoli cells, germ cells, and spermatozoa) were obtained from adult rats in order to analyze the intracellular localization of APEH by indirect immunofluorescence. In addition, the catalytic activity profiles of APEH in the different male reproductive tissues and isolated cells were quantified. Our results show that APEH is homogeneously distributed in Sertoli cells and early germ cells (spermatocytes and round spermatids), but this pattern changes during spermiogenesis. Specifically, in elongated spermatids and spermatozoa, APEH was localized in the acrosome and the principal piece. The exopeptidase activity was higher in the germ cell pool, compared to sperm and Sertoli cells, while the endoproteinase activity in epididymal homogenates was higher compared to testis homogenates at 24 h of incubation. In isolated cells, this activity was increased in Sertoli and germ cell pools, compared to spermatozoa. Taken together, these results indicate that APEH is differentially distributed in the testicular epithelium and undergoes re-localization during spermiogenesis. A possible role of APEH as a component of a protection system against oxidative stress and during sperm capacitation is discussed. Full article
(This article belongs to the Special Issue 10th Anniversary of Biomedicines—Advances in Proteinases and Proteinase Inhibitors)
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11 pages, 948 KiB  
Review
Matrix Metalloproteinases in Oral Health—Special Attention on MMP-8
by Tsvetelina Atanasova, Teodora Stankova, Anelia Bivolarska and Tatyana Vlaykova
Biomedicines 2023, 11(6), 1514; https://0-doi-org.brum.beds.ac.uk/10.3390/biomedicines11061514 - 23 May 2023
Cited by 5 | Viewed by 1709
Abstract
Matrix metalloproteinases (MMPs) are a large family of Ca2+ and Zn2+ dependent proteolytic enzymes, able to cleave the various components of the extracellular matrix (ECM), as well as a range of other regulatory molecules. Several reports have proven the important role [...] Read more.
Matrix metalloproteinases (MMPs) are a large family of Ca2+ and Zn2+ dependent proteolytic enzymes, able to cleave the various components of the extracellular matrix (ECM), as well as a range of other regulatory molecules. Several reports have proven the important role of both MMPs and their endogenous inhibitors, TIPMs, in oral health, the initial development of the tooth, and during enamel maturation. In this mini-review, we aim to summarize the literature information about the functions of MMPs, paying more attention to MMP-8 (collagenase-2 or neutrophil collagenase) in the development and progression of periodontitis, peri-implantitis, and carious lesions. We also emphasize the role of particular gene variants in MMP8 as predisposing factors for some oral diseases. Full article
(This article belongs to the Special Issue 10th Anniversary of Biomedicines—Advances in Proteinases and Proteinase Inhibitors)
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21 pages, 904 KiB  
Review
The Role of the Ectopeptidase APN/CD13 in Cancer
by Uwe Lendeckel, Farzaneh Karimi, Ruba Al Abdulla and Carmen Wolke
Biomedicines 2023, 11(3), 724; https://0-doi-org.brum.beds.ac.uk/10.3390/biomedicines11030724 - 28 Feb 2023
Cited by 2 | Viewed by 8260
Abstract
APN/CD13 is expressed in a variety of cells/tissues and is therefore associated with diverse physiological functions, including proliferation, differentiation, migration, angiogenesis, invasion, metastasis, vasoconstriction, and the regulation of normal and impaired immune function. Increased expression or activity of APN/CD13 has been described for [...] Read more.
APN/CD13 is expressed in a variety of cells/tissues and is therefore associated with diverse physiological functions, including proliferation, differentiation, migration, angiogenesis, invasion, metastasis, vasoconstriction, and the regulation of normal and impaired immune function. Increased expression or activity of APN/CD13 has been described for various tumors, such that APN/CD13 is in most cases associated with reduced disease-free and overall survival. The mechanisms that mediate these cellular effects of APN/CD13 have been largely determined and are described here. APN/CD13-regulated signaling pathways include integrin recycling, the regulation of small GTPase activities, cell–ECM interactions, and Erk1/2, PI3K, and Wnt signaling. APN/CD13 is a neo-angiogenesis marker that is not found on normal endothelia, but it is found on neo-angiogenetically active endothelia. Therefore, APN/CD13 represents a specific receptor for so-called “tumor-homing peptides” (NRG peptides). Peptides containing the NRG motif show high-affinity binding to APN/CD13. APN/CD13 thus represents a versatile target for the inhibition of tumor-induced angiogenesis through the tumor-selective administration of, e.g., cytotoxic substances. Furthermore, it enables the molecular imaging of tumor masses and the assessment of (neo)angiogenesis in animal models and in patients. Pharmacological inhibitors of APN/CD13 have been proven to reduce tumor growth and tumor progression in various APN/CD13-positive tumors. Full article
(This article belongs to the Special Issue 10th Anniversary of Biomedicines—Advances in Proteinases and Proteinase Inhibitors)
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