Functional Implications of Cathelicidin Antimicrobial Protein in Breast Cancer and Tumor-Associated Macrophage Microenvironment

Chen, Jiawei; Shin, Vivian Y.; Ho, John W.; Siu, Michelle K.Y.; Cheuk, Isabella Wai-Yin; Kwong, Ava

doi:10.3390/biom10050688

Cited by 14 publications

(14 citation statements)

References 64 publications

(74 reference statements)

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“…Paradoxically, LL-37 promotes tumorigenesis in breast cancer, ovarian cancer, malignant melanoma, lung cancer, prostate cancer, pancreatic cancer and squamous cell carcinoma of the skin [ 256 ]. For instance, LL-37 was found to be highly expressed in breast cancer [ 257 ], and promoted the migration and metastasis of breast cancer cells [ 258 ]. In ovarian cancer, it enhances the proliferation, migration and invasion of ovarian cancer cells [ 247 ].…”

Section: Activity Of Ampsmentioning

confidence: 99%

Antimicrobial peptides: mechanism of action, activity and clinical potential

et al. 2021

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The management of bacterial infections is becoming a major clinical challenge due to the rapid evolution of antibiotic resistant bacteria. As an excellent candidate to overcome antibiotic resistance, antimicrobial peptides (AMPs) that are produced from the synthetic and natural sources demonstrate a broad-spectrum antimicrobial activity with the high specificity and low toxicity. These peptides possess distinctive structures and functions by employing sophisticated mechanisms of action. This comprehensive review provides a broad overview of AMPs from the origin, structural characteristics, mechanisms of action, biological activities to clinical applications. We finally discuss the strategies to optimize and develop AMP-based treatment as the potential antimicrobial and anticancer therapeutics.

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Section: Activity Of Ampsmentioning

confidence: 99%

Antimicrobial peptides: mechanism of action, activity and clinical potential

et al. 2021

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“…В случае рака молочной железы было показано, что уровень Hp повышен не только в крови, но и в опухолевых тканях. Причём неожиданно оказалось существование функциональной связи между Hp и гликолитическими ферментами, такими как глюкозо-6-фосфатизомераза и гексокиназа [96].…”

Section: гаптоглобин и его протеоформы как потенциальные биомаркеры заболеванийunclassified

Haptoglobin as a biomarker

Naryzhny

Legina

2021

BIOMED KHIM

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Haptoglobin (Hp) is a blood plasma glycoprotein that binds free hemoglobin (Hb) and plays a critical role in tissue protection and the prevention of oxidative damage. In addition, it has a number of regulatory functions. Haptoglobin is an acute phase protein, its concentration in plasma changes in pathology, and the test for its concentration is part of normal clinical practice. Haptoglobin is a conservative protein synthesized mainly in the liver and lungs and is the subject of research as a potential biomarker of many diseases, including various forms of malignant neoplasms. Haptoglobin has several unique biophysical characteristics. Only in humans, the Hp gene is polymorphic, has three structural alleles that control the synthesis of three major phenotypes of Hp, homozygous Hp1-1 and Hp2-2, and heterozygous Hp2-1, determined by a combination of allelic variants that are inherited. Numerous studies indicate that the phenotype of haptoglobin can be used to judge the individual's predisposition to various diseases. In addition, Hp undergoes various post-translational modifications (PTMs). These are structural transformations (removal of the signal peptide, cutting of the Pre-Hp precursor molecule into two subunits, α and β, limited proteolysis of α-chains, formation of disulfide bonds, multimerization), as well as chemical modifications of α-chains and glycosylation of the β-chain. Glycosylation of the β-chain of haptoglobin at four Asn sites is the most important variable PTM that regulates the structure and function of the glycoprotein. The study of modified oligosaccharides of the Hp β-chain has become the main direction in the study of pathological processes, including malignant neoplasms. Many studies are focused on the identification of PTM and changes in the level of the α2-chain of this protein in pathology. These characteristics of Hp indicate the possibility of the existence of this protein as different proteoforms, probably with different functions. This review is devoted to the description of the structural and functional diversity of Hp and its potential use as a biomarker of various pathologies.

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“…In the case of breast cancer, it has been shown that the level of Hp is increased not only in the blood but also in tumor tissues. Moreover, it was unexpectedly found that there is a functional relationship between Hp and glycolytic enzymes, such as glucose-6-phosphate isomerase and hexokinase [ 96 ]. Another disease recently found to have elevated plasma Hp levels is acute myocardial infarction in young adults [ 97 ].…”

Section: Haptoglobin and Its Proteoforms As Potential Biomarkers Of Diseasesmentioning

confidence: 99%

Haptoglobin as a Biomarker

Naryzny

Legina

2021

Biochem. Moscow Suppl. Ser. B

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— Haptoglobin (Hp) is a glycoprotein that binds free hemoglobin (Hb) in plasma and plays a critical role in tissue protection and prevention of oxidative damage. Besides, it has some regulatory functions. Haptoglobin is an acute-phase protein, its concentration in plasma changes in pathology, and the test for its concentration is part of normal clinical practice. Haptoglobin is a conservative protein synthesized mainly in the liver and lungs and is the subject of research as a potential biomarker of many diseases, including various forms of malignant neoplasms. Haptoglobin has several unique biophysical characteristics. The human Нр gene is polymorphic, has three structural alleles that control the synthesis of three major phenotypes of haptoglobin: homozygous Нр1-1 and Нр2-2, and heterozygous Нр2-1, determined by a combination of allelic variants that are inherited. Numerous studies indicate that the phenotype of haptoglobin can be used to judge the individual predisposition of a person to various diseases. In addition, Hp undergoes various post-translational modifications (PTMs). These are structural transformations (removal of the signal peptide, cutting off the Pre-Hp precursor molecule into two subunits, α and β, limited proteolysis of α-chains, formation of disulfide bonds, multimerization), as well as chemical modifications of α-chains and glycosylation of the β-chain. Glycosylation of the β-chain of haptoglobin at four Asn sites is the most important variable PTM that regulates the structure and function of the glycoprotein. The study of modified oligosaccharides of the β-chain of Hp has become the main direction in the study of pathological processes, including malignant neoplasms. These characteristics indicate the possibility of the existence of Hp in the form of a multitude of proteoforms, probably performing different functions. This review is devoted to the description of the structural and functional diversity and the potential use of Hp as a biomarker of various pathologies.

show abstract

Functional Implications of Cathelicidin Antimicrobial Protein in Breast Cancer and Tumor-Associated Macrophage Microenvironment

Cited by 14 publications

References 64 publications

Antimicrobial peptides: mechanism of action, activity and clinical potential

Antimicrobial peptides: mechanism of action, activity and clinical potential

Haptoglobin as a biomarker

Haptoglobin as a Biomarker

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