c113449564529d7cff7961909ee49084 pmc_10221039.pdf 8dfc5679e31ea2695777a0ad9a8a438799196875 pmc_10221039.pdf 4e268a7d7a720f8bbad6e648525d5677211cb4417bd9a73d2f829b0d925070e7 pmc_10221039.pdf Title: Marine Invertebrates: A Promissory Still Unexplored Source of Inhibitors of Biomedically Relevant Metallo Aminopeptidases Belonging to the M1 and M17 Families Subject: Proteolytic enzymes, also known as peptidases, are critical in all living organisms. Peptidases control the cleavage, activation, turnover, and synthesis of proteins and regulate many biochemical and physiological processes. They are also involved in several pathophysiological processes. Among peptidases, aminopeptidases catalyze the cleavage of the N-terminal amino acids of proteins or peptide substrates. They are distributed in many phyla and play critical roles in physiology and pathophysiology. Many of them are metallopeptidases belonging to the M1 and M17 families, among others. Some, such as M1 aminopeptidases N and A, thyrotropin-releasing hormone-degrading ectoenzyme, and M17 leucyl aminopeptidase, are targets for the development of therapeutic agents for human diseases, including cancer, hypertension, central nervous system disorders, inflammation, immune system disorders, skin pathologies, and infectious diseases, such as malaria. The relevance of aminopeptidases has driven the search and identification of potent and selective inhibitors as major tools to control proteolysis with an impact in biochemistry, biotechnology, and biomedicine. The present contribution focuses on marine invertebrate biodiversity as an important and promising source of inhibitors of metalloaminopeptidases from M1 and M17 families, with foreseen biomedical applications in human diseases. The results reviewed in the present contribution support and encourage further studies with inhibitors isolated from marine invertebrates in different biomedical models associated with the activity of these families of exopeptidases. Keywords: aminopeptidase; aminopeptidase N; aminopeptidase A; TRH-degrading ectoenzyme; leucyl aminopeptidase; enzyme inhibitors; drug-oriented inhibitors; marine invertebrates Author: Isel Pascual Alonso, Fabiola Almeida García, Mario Ernesto Valdés Tresanco, Yarini Arrebola Sánchez, Daniel Ojeda del Sol, Belinda Sánchez Ramírez, Isabelle Florent, Marjorie Schmitt and Francesc Xavier Avilés Creator: LaTeX with hyperref Producer: pdfTeX-1.40.21 CreationDate: Thu May 4 02:04:05 2023 CEST ModDate: Thu May 4 03:15:46 2023 CEST Tagged: no UserProperties: no Suspects: no Form: none JavaScript: no Pages: 37 Encrypted: no Page size: 595.276 x 841.89 pts (A4) Page rot: 0 File size: 17355176 bytes Optimized: no PDF version: 1.7 name type encoding emb sub uni object ID ------------------------------------ ----------------- ---------------- --- --- --- --------- HCRKXL+VnURWPalladioL Type 1 Custom yes yes no 10 0 LJYLSL+URWPalladioL-Bold Type 1 Custom yes yes no 15 0 VTHRUQ+URWPalladioL-Roma Type 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and valid SignatureMatches: PDF-hul MIMEtype: application/pdf PDFMetadata: Objects: 1100 FreeObjects: 1 IncrementalUpdates: 0 DocumentCatalog: PageLayout: SinglePage PageMode: UseNone Outlines: Item: Title: Introduction Destination: section.1 Item: Title: M1 and M17 Metalloexopeptidase Inhibitors Isolated from Marine Invertebrates Destination: section.2 Children: Item: Title: Metallopeptidases: General Characteristics and Classification Destination: subsection.2.1 Item: Title: Clan MA: Subclan MA (E) Destination: subsection.2.2 Item: Title: M1 Family of Metalloaminopeptidases Destination: subsection.2.3 Item: Title: Inhibitors of M1 Family Isolated from Marine Invertebrates Destination: subsection.2.4 Children: Item: Title: A Specific Inhibitor of Thyrotropin-Releasing Hormone-Degrading Ectoenzyme/Pyroglutamyl Aminopeptidase II Isolated from a Marine Organism Destination: subsubsection.2.4.1 Item: Title: Inhibitors of Aminopeptidase N Isolated from Marine Organisms Destination: subsubsection.2.4.2 Item: Title: Clan MF: Family M17 Destination: subsection.2.5 Item: Title: Inhibitors of M17 Leucyl Aminopeptidases from Marine Organisms Destination: subsection.2.6 Item: Title: Conclusions Destination: section.3 Item: Title: References Destination: section.4 Info: Title: Marine Invertebrates: A Promissory Still Unexplored Source of Inhibitors of Biomedically Relevant Metallo Aminopeptidases Belonging to the M1 and M17 Families Author: Isel Pascual Alonso, Fabiola Almeida García, Mario Ernesto Valdés Tresanco, Yarini Arrebola Sánchez, Daniel Ojeda del Sol, Belinda Sánchez Ramírez, Isabelle Florent, Marjorie Schmitt and Francesc Xavier Avilés Subject: Proteolytic enzymes, also known as peptidases, are critical in all living organisms. Peptidases control the cleavage, activation, turnover, and synthesis of proteins and regulate many biochemical and physiological processes. They are also involved in several pathophysiological processes. Among peptidases, aminopeptidases catalyze the cleavage of the N-terminal amino acids of proteins or peptide substrates. They are distributed in many phyla and play critical roles in physiology and pathophysiology. Many of them are metallopeptidases belonging to the M1 and M17 families, among others. Some, such as M1 aminopeptidases N and A, thyrotropin-releasing hormone-degrading ectoenzyme, and M17 leucyl aminopeptidase, are targets for the development of therapeutic agents for human diseases, including cancer, hypertension, central nervous system disorders, inflammation, immune system disorders, skin pathologies, and infectious diseases, such as malaria. The relevance of aminopeptidases has driven the search and identification of potent and selective inhibitors as major tools to control proteolysis with an impact in biochemistry, biotechnology, and biomedicine. The present contribution focuses on marine invertebrate biodiversity as an important and promising source of inhibitors of metalloaminopeptidases from M1 and M17 families, with foreseen biomedical applications in human diseases. The results reviewed in the present contribution support and encourage further studies with inhibitors isolated from marine invertebrates in different biomedical models associated with the activity of these families of exopeptidases. 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