Contribution of activated beta3 integrin in the PDI release from endothelial cells

Ponamarczuk, Halszka; Popielarski, Marcin; Stasiak, Marta; Bednarek, Radosław; Studzian, Maciej; Pułaski, Łukasz; Babińska, Anna; Świątkowska, Maria

doi:10.2741/4663

Cited by 14 publications

(6 citation statements)

References 22 publications

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“…Furthermore, during vascular injury, secreted PDI is captured on the surface of platelets and endothelial cells through its direct interaction with the β3 integrin (Cho et al, 2012). The reversible disulfide interaction between PDI and β3 integrin is also reported to contribute to the secretion of PDI from endothelial cells (Ponamarczuk et al, 2018).…”

Section: Cells Referencementioning

confidence: 99%

Pathophysiological roles of cell surface and extracellular protein disulfide isomerase and their molecular mechanisms

Chiu

Chen

et al. 2021

British J Pharmacology

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Protein disulfide isomerase (PDI) is the prototypic member of the thiol isomerase family that catalyses disulfide bond rearrangement. Initially identified in the endoplasmic reticulum as folding catalysts, PDI and other members in its family have also been widely reported to reside on the cell surface and in the extracellular matrix. Although how PDI is exported and retained on the cell surface remains a subject of debate, this unique pool of PDI is developing into an important mechanism underlying the redox regulation of protein sulfhydryls that are critical for the cellular activities under various disease conditions. This review aims to provide an overview of the pathophysiological roles of surface and extracellular PDI and their underlying molecular mechanisms.Understanding the involvement of extracellular PDI in these diseases will advance our knowledge in the molecular aetiology to facilitate the development of novel pharmacological strategies by specifically targeting PDI in extracellular compartments.

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Section: Cells Referencementioning

confidence: 99%

Pathophysiological roles of cell surface and extracellular protein disulfide isomerase and their molecular mechanisms

Chiu

Chen

et al. 2021

British J Pharmacology

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“…As such, it is possible that the intracellular proteins calreticulin and PDI were released from cells during the extraction process, where they then associated with the mature fibrillin microfibrils. Another explanation for the presence of PDI in the extracellular space is the recent evidence of its secretion from cells via an activation of αvβ3 integrin ( 75 ). In either case, the co-purification of calreticulin and PDI supports their proposed roles in microfibril assembly.…”

Section: Resultsmentioning

confidence: 99%

Structural and compositional diversity of fibrillin microfibrils in human tissues

Eckersley¹,

Mellody²,

Pilkington³

et al. 2018

Journal of Biological Chemistry

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Elastic fibers comprising fibrillin microfibrils and elastin are present in many tissues, including the skin, lungs, and arteries, where they confer elasticity and resilience. Although fibrillin microfibrils play distinct and tissue-specific functional roles, it is unclear whether their ultrastructure and composition differ between elastin-rich (skin) and elastin-poor (ciliary body and zonule) organs or after in vitro synthesis by cultured cells. Here, we used atomic force microscopy, which revealed that the bead morphology of fibrillin microfibrils isolated from the human eye differs from those isolated from the skin. Using newly developed pre-MS preparation methods and LC-MS/MS, we detected tissue-specific regions of the fibrillin-1 primary structure that were differentially susceptible to proteolytic extraction. Comparing tissue- and culture-derived microfibrils, we found that dermis- and dermal fibroblast–derived fibrillin microfibrils differ in both bead morphology and periodicity and also exhibit regional differences in fibrillin-1 proteolytic susceptibility. In contrast, collagen VI microfibrils from the same dermal or fibroblast samples were invariant in ultrastructure (periodicity) and protease susceptibility. Finally, we observed that skin- and eye-derived microfibril suspensions were enriched in elastic fiber– and basement membrane–associated proteins, respectively. LC-MS/MS also identified proteins (such as calreticulin and protein-disulfide isomerase) that are potentially fundamental to fibrillin microfibril biology, regardless of their tissue source. Fibrillin microfibrils synthesized in cell culture lacked some of these key proteins (MFAP2 and -4 and fibrillin-2). These results showcase the structural diversity of these key extracellular matrix assemblies, which may relate to their distinct roles in the tissues where they reside.

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“…P4HB in these regions can interact with proteins such as integrins, which was closely associated with the actin cytoskeleton ( Kong et al, 2020 ). Therefore, P4HB in the cytoplasm can convey extracellular signals and trigger subsequent cascade reactions such as protein phosphorylation and cytoskeletal reorganization ( Ponamarczuk et al, 2018 ). Spermatogonia and spermatocytes are in the early stages of spermatogenesis and actively engage in cell proliferation and differentiation.…”

Section: Discussionmentioning

confidence: 99%

Expression, localization, and function of P4HB in the spermatogenesis of Chinese mitten crab (Eriocheir sinensis)

Tang¹,

Ni²,

Li³

et al. 2023

PeerJ

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Background The sperm of Chinese mitten crab (Eriocheir sinensis) have special noncondensed nuclei. The formation and stability of the special nuclei are closely related to the correct folding of proteins during spermatogenesis. P4HB plays a key role in protein folding, but its expression and role in the spermatogenesis of E. sinensis are unclear. Objective To investigate the expression and distribution characteristics of P4HB in the spermatogenesis of E. sinensis as well as its possible role. Methods The testis tissues of adult and juvenile E. sinensis were used as materials. We utilized a variety of techniques, including homology modeling, phylogenetic analysis, RT-qPCR, western blotting, and immunofluorescence staining to predict the protein structure and sequence homology of P4HB, analyze its expression in the testis tissues, and localize and semi-quantitatively assess its expression in different male germ cells. Results The sequence of P4HB protein in E. sinensis shared a high similarity of 58.09% with the human protein disulfide isomerase, and the phylogenetic tree analysis indicated that the protein sequence was highly conserved among crustaceans, arthropods, and other animals species. P4HB was found to be expressed in both juvenile and adult E. sinensis testis tissues, with different localization patterns observed all over the developmental stages of male germ cells. It was higher expressed in the spermatogonia, spermatocytes, and stage I spermatids, followed by the mature sperm than in the stage II and III spermatids. The subcellular localization analysis revealed that P4HB was predominantly expressed in the cytoplasm, cell membrane, and extracellular matrix in the spermatogonia, spermatocytes, stage I and stage II spermatids, with some present in specific regions of the nuclei in the spermatogonia. In contrast, P4HB was mainly localized in the nuclei of stage III spermatids and sperm, with little expression observed in the cytoplasm. Conclusion P4HB was expressed in the testis tissues of both adult and juvenile E. sinensis, but the expression and localization were different in male germ cells at various developmental stages. The observed differences in the expression and localization of P4HB may be an essential factor in maintaining the cell morphology and structure of diverse male germ cells in E. sinensis. Additionally, P4HB expressed in the nuclei of spermatogonia, late spermatids, and sperm may play an indispensable role in maintaining the stability of the noncondensed spermatozoal nuclei in E. sinensis.

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Contribution of activated beta3 integrin in the PDI release from endothelial cells

Cited by 14 publications

References 22 publications

Pathophysiological roles of cell surface and extracellular protein disulfide isomerase and their molecular mechanisms

Pathophysiological roles of cell surface and extracellular protein disulfide isomerase and their molecular mechanisms

Structural and compositional diversity of fibrillin microfibrils in human tissues

Expression, localization, and function of P4HB in the spermatogenesis of Chinese mitten crab (Eriocheir sinensis)

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