Defensins: Natural component of human innate immunity

Jarczak, Justyna; Kościuczuk, Ewa M.; Lisowski, Paweł; Strzałkowska, N.; Jóźwik, Artur; Horbańczuk, J.O.; Krzyżewski, J.; Zwierzchowski, L.; Bagnicka, Emilia

doi:10.1016/j.humimm.2013.05.008

Cited by 173 publications

(161 citation statements)

References 84 publications

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“…The tear fluid contains several prototypic AMPs such as defensins, dermcidin and LL-37 cathelicidin [74,85,101,102]. Defensins are small cationic peptides produced by epithelial cells with cysteine rich sequences forming a very stable 3D structure [103]. The two subfamilies of defensins (α-and β-defensins) show broad antimicrobial as well as antifungal and antiviral activities [95,104].…”

Section: The Chemical Barrier Of the Tears As A Possible Source For Bmentioning

confidence: 99%

Diabetic retinopathy: Proteomic approaches to help the differential diagnosis and to understand the underlying molecular mechanisms

Csősz

Deák

Kalló

et al. 2017

Journal of Proteomics

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a b s t r a c t a r t i c l e i n f oDiabetic retinopathy is the most common diabetic eye disease and a leading cause of blindness among patients with diabetes. The appearance and the severity of the symptoms correlate with the duration of diabetes and poor blood glucose level management. Diabetic retinopathy is also categorized as a chronic low-level inflammatory disease; the high blood glucose level promotes the accumulation of the advanced glycation end products and leads to the stimulation of monocytes and macrophages. Examination of protein level alterations in tears using state-of the art proteomics techniques have identified several proteins as possible biomarkers for the different stages of the diabetic retinopathy. Some of the differentially expressed tear proteins have a role in the barrier function of tears linking the diabetic retinopathy with another eye complication of diabetes, namely the diabetic keratopathy resulting in impaired wound healing. Understanding the molecular events leading to the eye complications caused by hyperglycemia may help the identification of novel biomarkers as well as therapeutic targets in order to improve quality of life of diabetic patients. Biological significance: Diabetic retinopathy (DR), the leading cause of blindness among diabetic patients can develop without any serious symptoms therefore the early detection is crucial. Because of the increasing prevalence there is a high need for improved screening methods able to diagnose DR as soon as possible. The non-invasive collection and the relatively high protein concentration make the tear fluid a good source for biomarker discovery helping the early diagnosis. In this work we have reviewed the administration of advanced proteomics techniques used in tear biomarker studies and the identified biomarkers with potential to improve the already existing screening methods for DR detection.

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Section: The Chemical Barrier Of the Tears As A Possible Source For Bmentioning

confidence: 99%

Diabetic retinopathy: Proteomic approaches to help the differential diagnosis and to understand the underlying molecular mechanisms

Csősz

Deák

Kalló

et al. 2017

Journal of Proteomics

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“…Moreover, some defensins are known to act as chemokines that activate the adaptive immune response [2][3][4][5]. The mammalian defensins are characterized by six cysteine residues forming three intramolecular disulfide bridges, and are divided into two subfamilies, α-and β-defensins, based on the amino acid sequence similarities and the linkages of the disulfide bonds [3][4][5].…”

Section: Introductionmentioning

confidence: 99%

“…The α-defensins are cationic, amphipathic 3-4 kDa peptides [5]. They were first isolated from myeloid cells and later identified in intestinal Paneth cells.…”

Section: Introductionmentioning

confidence: 99%

“…Structurally, α-defensins are characterized by a triple-stranded β-sheet structure that is constrained by three invariant disulfide bonds between Cys I -Cys VI , Cys II -Cys IV , and Cys III -Cys V . This characteristic pattern of disulfide bridges is considered to be crucial for maintenance of the three-dimensional structure and proteolytic stability of these peptides [5]. Moreover, α-defensins have conserved biochemical features including a canonical Arg-Glu salt 5 bridge, a conserved Gly residue at Cys III＋8 , and high content of Arg relative to that of Lys.…”

Section: Introductionmentioning

confidence: 99%

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Efficient production of a correctly folded mouse α-defensin, cryptdin-4, by refolding during inclusion body solubilization

Tomisawa

Sato

Kamiya

et al. 2015

Protein Expression and Purification

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Mammalian α-defensins contribute to innate immunity by exerting antimicrobial activity against various pathogens. To perform structural and functional analysis of α-defensins, large amounts of α-defensins are essential. Although many expression systems for the production of recombinant α-defensins have been developed, attempts to obtain large amounts of α-defensins have been only moderately successful. Therefore, in this study, we applied a previously developed aggregation-prone protein coexpression method for the production of mouse α-defensin cryptdin-4 (Crp4) in order to enhance the formation of inclusion bodies in E. coli expression system. By using this method, we succeeded in obtaining a large amount of Crp4 in the form of inclusion bodies.Moreover, we attempted to refold Crp4 directly during the inclusion-body solubilization step under oxidative conditions. Surprisingly, even without any purification, Crp4 was efficiently refolded during the solubilization step of inclusion bodies, and the yield was better than that of the conventional refolding method. NMR spectra of purified Crp4 suggested that it was folded into its correct tertiary structure. Therefore, the method described in this study not only enhances the expression of α-defensin as inclusion bodies, but also eliminates the cumbersome and time-consuming refolding step.3

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“…Имеется множество типов дефензинов альфа и бета (a-def-1; a-def-3; a-def-4; a-def-6; b-def-1; b-def-2; b-def-4 и т.п. ), которые в многоклеточном организме, в целом, выполняют более или менее сходные антибиотические функции: они обладают широким спектром бактерицидного действия, направленного против бактерий, грибов и даже некоторых вирусов [10][11][12][13].…”

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Defensins – natural peptide antibiotics of higher eucariotes

Grishin

Соколов

2014

BIOMED KHIM

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The goal of this review is to characterize defensins representing an evolutionary the most ancient family of antimicrobial peptides. It gives general information on functional and structural features of defensins as the main components of the first-line defense of higher eukaryote organisms against infectious agents. The review considers not only current situation in the defensin research but also perspectives of creation of recombinant antimicrobial peptides of biomedical application.

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Defensins: Natural component of human innate immunity

Cited by 173 publications

References 84 publications

Diabetic retinopathy: Proteomic approaches to help the differential diagnosis and to understand the underlying molecular mechanisms

Diabetic retinopathy: Proteomic approaches to help the differential diagnosis and to understand the underlying molecular mechanisms

Efficient production of a correctly folded mouse α-defensin, cryptdin-4, by refolding during inclusion body solubilization

Defensins – natural peptide antibiotics of higher eucariotes

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