Regulation of the Tec family of non-receptor tyrosine kinases in cardiovascular disease

Yin, Zeyu; Zou, Yuanming; Wang, Dong; Huang, Xinyue; Xiong, Shengjun; Cao, Liu; Zhang, Ying; Sun, Yingxian; Zhang, Naijin

doi:10.1038/s41420-022-00927-4

Cited by 17 publications

(18 citation statements)

References 97 publications

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“…Changes in the expression of fucosylated oligosaccharides have been observed in pathological processes such as atherosclerosis [ 149 ]. In addition, the phosphorylation modification of tyrosine is related to the formation of esters, which may also be involved in lipid metabolism and the occurrence and progression of diseases [ 150 ].…”

Section: Resultsmentioning

confidence: 99%

Changes to Urinary Proteome in High-Fat-Diet ApoE−/− Mice

et al. 2022

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Cardiovascular disease is currently the leading cause of death worldwide. Atherosclerosis is an important pathological basis of cardiovascular disease, and its early diagnosis is of great significance. Urine bears no need nor mechanism to be stable, so it accumulates many small changes and is therefore a good source of biomarkers in the early stages of disease. In this study, ApoE-/- mice were fed a high-fat diet for 5 months. Urine samples from the experimental group and control group (C57BL/6 mice fed a normal diet) were collected at seven time points. Proteomic analysis was used for comparison within the experimental group and for comparison between the experimental group and the control group. The results of the comparison within the experimental group showed a significant difference in the urinary proteome before and after a one-week high-fat diet, and several of the differential proteins have been reported to be associated with atherosclerosis and/or as biomarker candidates. The results of the comparison between the experimental group and the control group indicated that the biological processes enriched by the GO analysis of the differential proteins correspond to the progression of atherosclerosis. The differences in chemical modifications of urinary proteins have also been reported to be associated with the disease. This study demonstrates that urinary proteomics has the potential to sensitively monitor changes in the body and provides the possibility of identifying early biomarkers of atherosclerosis.

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Section: Resultsmentioning

confidence: 99%

Changes to Urinary Proteome in High-Fat-Diet ApoE−/− Mice

et al. 2022

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“…BTK belongs to a sub-family of non-receptor protein tyrosine kinases (TEC kinases) and plays an essential role in the proliferation, differentiation, and survival of B cells. BTK also plays a role in the function of innate cells and T cells and mediates Toll-like receptor signaling and NLRP3 inflammasome activation 1 . BTKis have revolutionized landscape therapy of B cell malignancies such as chronic lymphocytic leukemia, diffuse large B-cell lymphoma, mantle cell lymphoma, and Waldenstrom macroglobulinemia.…”

Section: Discussionmentioning

confidence: 99%

Disseminated Fungal Infection in a Patient Receiving Zanubrutinib

Walsh

Sánchez

et al. 2023

Preprint

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“… 49 According to whether PTK is a cell membrane receptor, PTKs can be divided into nonreceptor type and membrane receptor type. 50 Receptor‐type tyrosine kinases include EGFR, VEGFR, and FGFR. Abnormal activation of these kinases is related to angiogenesis, tumor invasion, and metastasis.…”

Section: Phosphorylationmentioning

confidence: 99%

Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

Zhong

Xiao

Xie

et al. 2023

MedComm

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Protein posttranslational modifications (PTMs) refer to the breaking or generation of covalent bonds on the backbones or amino acid side chains of proteins and expand the diversity of proteins, which provides the basis for the emergence of organismal complexity. To date, more than 650 types of protein modifications, such as the most well‐known phosphorylation, ubiquitination, glycosylation, methylation, SUMOylation, short‐chain and long‐chain acylation modifications, redox modifications, and irreversible modifications, have been described, and the inventory is still increasing. By changing the protein conformation, localization, activity, stability, charges, and interactions with other biomolecules, PTMs ultimately alter the phenotypes and biological processes of cells. The homeostasis of protein modifications is important to human health. Abnormal PTMs may cause changes in protein properties and loss of protein functions, which are closely related to the occurrence and development of various diseases. In this review, we systematically introduce the characteristics, regulatory mechanisms, and functions of various PTMs in health and diseases. In addition, the therapeutic prospects in various diseases by targeting PTMs and associated regulatory enzymes are also summarized. This work will deepen the understanding of protein modifications in health and diseases and promote the discovery of diagnostic and prognostic markers and drug targets for diseases.

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Regulation of the Tec family of non-receptor tyrosine kinases in cardiovascular disease

Cited by 17 publications

References 97 publications

Changes to Urinary Proteome in High-Fat-Diet ApoE−/− Mice

Changes to Urinary Proteome in High-Fat-Diet ApoE−/− Mice

Disseminated Fungal Infection in a Patient Receiving Zanubrutinib

Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

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