Quantifying the Matrix Metalloproteinase 2 (MMP2) Spatially in Tissues by Probe via MALDI Imaging Mass Spectrometry

Yu, Daojiang; Peng, Lai; Yan, Tao; Fang, Kai; Chen, Lei; Zhang, Shuyu

doi:10.3389/fchem.2021.786283

Cited by 1 publication

(4 citation statements)

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“…To address this challenge, Yu et al developed a specific sensor for spatial detection of MMP-2 in tissues using MALDI MS (Figure 13a). [85] The sensor is a peptide containing MMP-2 enzyme cleavage sequence. The peptide has a chlorine atom on the Tyr of the peptide end, which make it has ability to provide two isotopes to improve the detection accuracy.…”

Section: Ms Sensorsmentioning

confidence: 99%

“…[158] This sensing system was able to detect three biomarkers, including MMP-9, ADAM-10, and ADAM-17 in simulated serum samples, demonstrating the potential of this sensing system for the diagnosis of up to five cancer types, including breast cancer, stomach, lung, colorectal, and prostate cancer. [85] Copyright 2021, Frontiers Media. b) A mass spectrometric biosensing strategy for MMP-2 and MMP-7 detection.…”

Section: Dual-target Detection Platformmentioning

confidence: 99%

Section: Enzymatic Activity‐based Sensorsmentioning

confidence: 99%

mentioning

confidence: 99%

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Recent Development and Applications of Sensors for the Detection of Matrix Metalloproteinases

Zhang

et al. 2023

Adv Materials Technologies

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of ECM cleavage. As the number of identified MMPs types increased, researchers began to classify the MMPs according to the protein structure. [3] Despite some structural differences, most of the structural modules of MMPs are still conservative, including i) an amino-terminal peptide which can leads MMPs to the endoplasmic reticulum, ii) a propeptide region (companying with a zinc-interacting thiol group) and a zinc-binding site which can maintains MMPs as inactive zymogens or as a catalytic domain, iii) a linker region of varying residue length that may determine the substrates to which the MMPs can accommodate, and iv) a hemopexin-like domain. [4] With the application of engineered genetic models these years, more biological roles of MMPs have been revealed in recently years. For example, through investigating MMPs' substrates of other proteins, such as pro-proteases, chemokines, antimicrobial peptides, cell surface proteins, coagulation factors, adhesion molecules, cryptic growth factors, and cytokines, [5] it has been revealed that the MMPs have a broad and dramatic impact on physiological processes, for example, immunity, [6] tissue repair, [7,8] cell differentiation, [9,10] and cell invasion. [11] In these physiological processes, MMPs are secreted as zymogens. [12] The cysteine (Cys) residues of MMPs' propeptide regions are able to interact with Zn 2+ of the catalytic domains. The formation of the thiols-Zn 2+ bonds play important roles in maintaining the inactivity of MMPs, i.e., MMPs' activations are achieved by breaking these bonds. It is conceivable that MMPs can be activated by a variety of endogenous or exogenous substances, such as mercurial compounds and chaotropic agents. [4] To regulate the activity of MMPs, organisms have evolved a family of two-domain proteins (TIMPs) as the endogenous inhibitors. [13] Most MMPs are ubiquitously secreted in mammalian organisms. The level of MMPs' expression is generally low under normal physiological conditions, while the abnormally elevated expression and activity levels are often associated with diseases. For example, as of the positive roles of MMPs in tumor growth and angiogenesis, [14] recent studies revealed that MMPs overexpression is implicated in a variety of cancers. [15] MMP-2 and MMP-9 are overexpressed in breast cancer, [16] cervical cancer, [17] etc., while MMP-7 are correlated with colorectal cancer (CRC). [18] Moreover, the prognostic value of MMPs has also been well demonstrated in treatment of different cancers. [19,20] For example, patients with high levels of MMP-2 and MMP-9 were clinically defined as a poor prognosis. [21] Therefore, MMPs' Matrix metalloproteinases (MMPs) are a class of zinc-dependent endopeptidases that play important roles in disease progression. High expression of MMPs is associated with various diseases, including cancer, cardiovascular diseases, neurological diseases, and inflammatory diseases. For better understanding the roles of MMPs in these diseases' development and the potential in early diagnosis and treatment m...

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Section: Ms Sensorsmentioning

confidence: 99%

Section: Dual-target Detection Platformmentioning

confidence: 99%