Intercellular adhesion molecule 1: Recent findings and new concepts involved in mammalian spermatogenesis

Mruk, Dolores D.; Xiao, Xiang; Lydka, Marta; Li, Michelle W.M.; Bilińska, Barbara; Cheng, C. Yan

doi:10.1016/j.semcdb.2013.07.003

Cited by 19 publications

(27 citation statements)

References 217 publications

(174 reference statements)

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“…Sertoli cells possess a basolateral membrane that faces the outside of the tubule that is exposed to nutrients from the blood, and an apical membrane that is in contact with germ cells Caballero et al, 2012;Franca et al, 2012;Mruk et al, 2013). It is the primary job of Sertoli cells to nurture and protect the developing germ cells (Kato et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

Localization of Multidrug Resistance-Associated Proteins along the Blood-Testis Barrier in Rat, Macaque, and Human Testis

2013

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The blood-testis barrier (BTB) prevents the entry of many drugs into seminiferous tubules, which can be beneficial for therapy not intended for the testis but may decrease drug efficacy for medications requiring entry to the testis. Previous data have shown that some of the transporters in the multidrug resistance-associated protein (MRP) family (ABCC) are expressed in the testis. By determining the subcellular localization of these transporters, their physiologic function and effect on drug disposition may be better predicted. Using immunohistochemistry (IHC), we determined the site of expression of the MRP transporters expressed in the testis, namely, MRP1, MRP4, MRP5, and MRP8, from immature and mature rats, rhesus macaques, and adult humans. We determined that in all species MRP1 was restricted to the basolateral membrane of Sertoli cells, MRP5 is located in Leydig cells, and MRP8 is located in round spermatids, whereas MRP4 showed speciesspecific localization. MRP4 is expressed on the basolateral membrane of Sertoli cells in human and nonhuman primates, but on the apical membrane of Sertoli cells in immature and mature rats, representing a potential caution when using rat models as a means for studying drug disposition across the BTB. These data suggest that MRP1 may limit drug disposition into seminiferous tubules, as may MRP4 in human and nonhuman primates but not in rats. These data also suggest that MRP5 and MRP8 may not have a major impact on the penetration of drugs across the BTB.

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Section: Introductionmentioning

confidence: 99%

Localization of Multidrug Resistance-Associated Proteins along the Blood-Testis Barrier in Rat, Macaque, and Human Testis

2013

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“…In order to allow germ cells to move from the basal to the adluminal compartment, BTB junctions rapidly disassemble and reassemble in a very dynamic way. BTB restructuring allows germ cells progression to the adluminal compartment and involves peculiar changes in structural proteins of tight junctions, such as claudin-11 and occludin, and of adherens junctions, such as N -cadherin (Mruk et al, 2014). …”

Section: Discussionmentioning

confidence: 99%

“…In this way, fully developed spermatozoa can be released into the tubular lumen at the end of spermiogenesis (Lui et al, 2003; Mruk et al, 2014). …”

Section: Discussionmentioning

confidence: 99%

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Polydeoxyribonucleotide, an Adenosine-A2A Receptor Agonist, Preserves Blood Testis Barrier from Cadmium-Induced Injury

et al. 2017

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Cadmium (Cd) impairs blood-testis barrier (BTB). Polydeoxyribonucleotide (PDRN), an adenosine A2A agonist, has positive effects on male reproductive system. We investigated the effects of PDRN on the morphological and functional changes induced by Cd in mice testes. Adult Swiss mice were divided into four groups: controls administered with 0.9% NaCl (1 ml/kg, i.p., daily) or with PDRN (8 mg/kg, i.p. daily), animals challenged with Cd chloride (CdCl2; 2 mg/kg, i.p, daily) and animals challenged with CdCl2 (2 mg/kg, i.p., daily) and treated with PDRN (8 mg/kg, i.p., daily). Experiments lasted 14 days. Testes were processed for biochemical, structural, and ultrastructural evaluation and hormones were assayed in serum. CdCl2 increased pERK 1/2 expression and Follicle Stimulating Hormone (FSH) and Luteinizing Hormone (LH) levels; it decreased testosterone (TE) and inhibin-B levels and induced structural damages in extratubular compartment and in seminiferous epithelium, with ultrastructural features of BTB disruption. Many TUNEL-positive germ cells were present. CdCl2 increased tubular TGF-β3 immunoreactivity and reduced claudin-11, occludin, and N-cadherin immunoreactivity. PDRN administration reduced pERK 1/2 expression, FSH, and LH levels; it increased TE and inhibin-B levels, ameliorated germinal epithelium changes and protected BTB ultrastructure. Few TUNEL-positive germ cells were present and the extratubular compartment was preserved. Furthermore, PDRN decreased TGF-β3 immunoreactivity and enhanced claudin-11, occludin, and N-cadherin immunoreactivity. We demonstrate a protective effect of PDRN on Cd-induced damages of BTB and suggest that PDRN may play an important role against Cd, particularly against its harmful effects on gametogenesis.

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“…Foxc2 inhibited ICAM-1 expression in HUVECs. ICAM-1 has been reported to directly interact with molecules on the surface of monocytes to influence cell adhesion (Mruk et al, 2014). The effects of Foxc2 on the adhesion of fluorescence-labeled THP-1 monocytes to LPS-treated HUVECs were tested using Foxc2 siRNA and recombinant plasmids overexpressing Foxc2.…”

Section: Foxc2 Was Involved In Regulating Lps-induced Adhesion Of Thpmentioning

confidence: 99%

Forkhead Box C2 Attenuates Lipopolysaccharide-Induced Cell Adhesion via Suppression of Intercellular Adhesion Molecule-1 Expression in Human Umbilical Vein Endothelial Cells

Zheng

et al. 2019

DNA and Cell Biology

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Atherosclerosis is a chronic vascular inflammatory disease that involves diverse cell types and circulating regulatory factors, including intercellular adhesion molecule (ICAM)-1, a proinflammatory cytokine. Lipopolysaccharides (LPS) increase ICAM-1 expression and promote cell adhesion, but the mechanism is not clear. We found that LPS induced time-and dose-regulated upregulation of ICAM-1 expression and downregulation of forkhead box protein C2 (Foxc2) expression in human umbilical vein endothelial cells (HUVECs). Overexpression of Foxc2 significantly inhibited both LPS-induced ICAM-1 expression in HUVECs and LPS-induced adhesion of THP-1 cells to HUVECs. Foxc2 siRNA dramatically increased both LPS-induced ICAM-1 expression and LPS-induced adhesion of THP-1 human monocytes cells to HUVECs. We conclude that Foxc2 inhibited LPS-induced adhesion of THP-1 cells to HUVECs by suppressing ICAM-1 expression in HUVECs.

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Intercellular adhesion molecule 1: Recent findings and new concepts involved in mammalian spermatogenesis

Cited by 19 publications

References 217 publications

Localization of Multidrug Resistance-Associated Proteins along the Blood-Testis Barrier in Rat, Macaque, and Human Testis

Localization of Multidrug Resistance-Associated Proteins along the Blood-Testis Barrier in Rat, Macaque, and Human Testis

Polydeoxyribonucleotide, an Adenosine-A2A Receptor Agonist, Preserves Blood Testis Barrier from Cadmium-Induced Injury

Forkhead Box C2 Attenuates Lipopolysaccharide-Induced Cell Adhesion via Suppression of Intercellular Adhesion Molecule-1 Expression in Human Umbilical Vein Endothelial Cells

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