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Matrix Metalloproteinases (MMPs) belong to a family of metal-dependent
endopeptidases which contain a series of conserved pro-peptide domains and catalytic
domains. MMPs have been widely found in plants, animals, and microorganisms.
MMPs are involved in regulating numerous physiological processes, pathological
processes, and immune responses. In addition, MMPs play a key role in disease
occurrence, including tumors, cardiovascular diseases, and other diseases. Compared
with invertebrate MMPs, vertebrate MMPs have diverse subtypes and complex
functions. Therefore, it is difficult to study the function of MMPs in vertebrates.
However, it is relatively easy to study invertebrate MMPs because there are fewer
subtypes of MMPs in invertebrates. In the present review, the structure and function
of MMPs in invertebrates were summarized, which will provide a theoretical basis for
investigating the regulatory mechanism of MMPs in invertebrates.
Apoptosis, also named programmed cell death, is a highly conserved physiological mechanism. Apoptosis plays crucial roles in many life processes, such as tissue development, organ formation, homeostasis maintenance, resistance against external aggression, and immune responses. Apoptosis is regulated by many genes, among which Apoptosis Inhibitor-5 (API5) is an effective inhibitor, though the structure of API5 is completely different from the other known Inhibitors Of Apoptosis Proteins (IAPs). Due to its high expression in many types of tumors, API5 has received extensive attention, and may be an effective target for cancer treatment. In order to comprehensively and systematically understand the biological roles of API5, we summarized the evolution and structure of API5 and its roles in anti-apoptosis in this review.
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