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Journal articles on the topic 'Basiglio'

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Author: Grafiati

Published: 10 March 2023

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1

Bianconi, M., L. Ferraro, G. C. Traina, G. Zanoli, T. Antonelli, A. Guberti, R. Ricci, and L. Massari. "Pharmacokinetics and efficacy of ropivacaine continuous wound instillation after joint replacement surgery † †Declaration of interest. This work was supported by AstraZeneca, Basiglio, Milano, Italy. Presented in part at the Third European Congress of Orthopaedic Anaesthesia, 31 May–2 June 2001, London, UK." British Journal of Anaesthesia 91, no. 6 (December 2003): 830–35. http://dx.doi.org/10.1093/bja/aeg277.

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2

Chen, Li, Jiajia Bi, Masaaki Nakai, David Bunick, John F. Couse, Kenneth S. Korach, and Romana A. Nowak. "Expression of basigin in reproductive tissues of estrogen receptor-α or -β null mice." REPRODUCTION 139, no. 6 (June 2010): 1057–66. http://dx.doi.org/10.1530/rep-10-0069.

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Basigin plays important roles in both male and female reproduction because basigin (Bsg) null male and female mice are infertile. The aim of the present study was to determine whether basigin expression in reproductive organs requires estrogen receptor-α (ESR1, ERα) or -β (ESR2, ERβ). Expression of basigin protein in the testis, ovary, and male and female reproductive tracts was studied in adult wild-type (WT),Esr1-null (αERKO), andEsr2-null (βERKO) mice by immunohistochemistry and immunoblotting. Basigin mRNA levels in ovary and uterus were examined by quantitative RT-PCR. In females, basigin protein expression was observed mainly in granulosa and interstitial cells of the ovary and epithelial cells of the proximal oviduct in all genotypes. Basigin protein was also expressed in the uterine epithelium at proestrus and estrus in WT and βERKO mice but not in αERKO mice. However, a higher level of basigin mRNA was observed in uteri of αERKO mice compared with WT and βERKO mice. In males, basigin was expressed in Leydig cells and all germ cells except spermatogonia in all genotypes. Basigin was present in epithelial cells lining the efferent ductules in WT and βERKO mice, but expression was greatly reduced in αERKO mice. In epididymal ducts, basigin expression was observed in epithelial cells in the caput and cauda in all genotypes. These data suggest that expression of basigin protein requires ESR1, but not ESR2, in the uterus and efferent ductules, but is independent of estrogen receptor in the ovary, oviduct, testis, and epididymis.

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3

Ding, Nai-Zheng, Cheng-Qiang He, and Zeng-Ming Yang. "Quantification of basigin mRNA in mouse oocytes and preimplantation embryos by competitive RT-PCR." Zygote 10, no. 3 (August 2002): 239–43. http://dx.doi.org/10.1017/s0967199402002319.

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Basigin is a member of the immunoglobulin superfamily and a key molecule related to mouse blastocyst implantation. Whether preimplantation mouse embryos express basigin mRNA is still unknown. The aim of this study was to use a quantitative competitive polymerase chain reaction to assess quantitatively the levels of basigin mRNA in mouse oocyte and preimplantation embryos. Basigin mRNA was detected in the oocyte and all the stages of preimplantation embryos. The levels of basigin mRNA were 0.0606 ± 0.0282 in the oocyte, 0.0102 ± 0.0036 in the zygote, 0.0007 ± 0.0003 in the 2-cell embryo, 0.0031 ± 0.0017 in the 4-cell embryo, 0.0084 ± 0.0024 in the 8-cell embryo, 0.0537 ± 0.0121 in the morula and 0.0392 ± 0.0161 attomoles in the blastocyst, respectively. The levels of basigin mRNA in the oocyte, morula and blastocyst were significantly higher than those in the zygote and embryos at the 2-cell, 4-cell and 8-cell stages. The high level of basigin expression in the blastocyst may play a role during embryo implantation.

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4

Albrechtsen, Reidar, Nicolai Wewer Albrechtsen, Sebastian Gnosa, Jeanette Schwarz, Lars Dyrskjøt, and Marie Kveiborg. "Identification of ADAM12 as a Novel Basigin Sheddase." International Journal of Molecular Sciences 20, no. 8 (April 22, 2019): 1957. http://dx.doi.org/10.3390/ijms20081957.

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The transmembrane glycoprotein basigin, a member of the immunoglobulin superfamily, stimulates matrix metalloproteinase (MMP)-mediated extracellular matrix (ECM) degradation and thereby drives cancer cell invasion. Basigin is proteolytically shed from the cell surface and high concentrations of soluble basigin in the blood dictates poor prognosis in cancer patients. A positive correlation between basigin and a disintegrin and metalloproteinase (ADAM)-12 in serum from prostate cancer patients has been reported. Yet, the functional relevance of this correlation is unknown. Here, we show that ADAM12 interacts with basigin and cleaves it in the juxtamembrane region. Specifically, overexpression of ADAM12 increases ectodomain shedding of an alkaline phosphatase-tagged basigin reporter protein from the cell surface. Moreover, CRISPR/Cas9-mediated knockout of ADAM12 in human HeLa carcinoma cells results in reduced shedding of the basigin reporter, which can be rescued by ADAM12 re-expression. We detected endogenous basigin fragments, corresponding to the expected size of the ADAM12-generated ectodomain, in conditioned media from ADAM12 expressing cancer cell-lines, as well as serum samples from a healthy pregnant donor and five bladder cancer patients, known to contain high ADAM12 levels. Supporting the cancer relevance of our findings, we identified several cancer-associated mutations in the basigin membrane proximal region. Subsequent in vitro expression showed that some of these mutants are more prone to ADAM12-mediated shedding and that the shed ectodomain can enhance gelatin degradation by cancer cells. In conclusion, we identified ADAM12 as a novel basigin sheddase with a potential implication in cancer.

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5

Li, Kailiang, and Romana A. Nowak. "The role of basigin in reproduction." Reproduction 159, no. 2 (February 2020): R97—R109. http://dx.doi.org/10.1530/rep-19-0268.

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Basigin is a highly glycosylated transmembrane protein that was originally identified as a product of tumor cells. Basigin is a potent inducer of matrix metalloproteinases (MMPs) and angiogenic factors such as vascular endothelial growth factor (VEGF). Basigin is also a chaperone protein for specific metabolite transporters in the plasma cell membrane such as the monocarboxylate transporters and is an important regulator of cell metabolism. Studies in reproductive model systems have demonstrated that basigin is expressed in the testis, ovary, uterus and placenta and is necessary for normal fertility in both males and females. Overexpression of basigin is associated with reproductive diseases including uterine leiomyomas and endometriosis. This review presents an overview of the literature regarding the physiological role of basigin in reproductive tissues and the mechanistic pathways involved in its actions.

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6

Chen, Li, Robert J. Belton, and Romana A. Nowak. "Basigin-Mediated Gene Expression Changes in Mouse Uterine Stromal Cells During Implantation." Endocrinology 150, no. 2 (February 1, 2009): 966–76. http://dx.doi.org/10.1210/en.2008-0571.

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Implantation of mouse embryos is dependent on the proliferation and differentiation of uterine stromal cells in a process called decidualization. Decidualization both supports and limits the invasion of the implanting embryo and is regulated in part by the expression of matrix metalloproteinases (MMPs) and their inhibitors, the tissue inhibitors of metalloproteinases (TIMPs). Molecules that alter the balance between MMP and TIMP expression could prevent implantation of the embryo. The membrane glycoprotein basigin (CD147/EMMPRIN), a known inducer of MMPs, is necessary for normal implantation in the mouse. The purpose of this study was to investigate the potential roles of basigin during implantation in the mouse. Using an in vitro stromal cell culture system, we found that recombinant human basigin protein (rBSG) increases MMP-3 and MMP-9 expression without altering TIMP-3 expression. Our results also showed rBSG induces expression of cytokines IL-1α/β and leukocyte chemoattractants, CCL3, CCL20, CXCL2, and CXCL5. More importantly, rBSG significantly suppressed stromal cell decidualization as shown by the inhibition of alkaline phosphatase-2 expression and activity by rBSG. However, rBSG did not affect stromal cell proliferation. Taken together, our data indicate that basigin mediates gene expression changes in mouse uterine stromal cells and suggests that temporal and spatial regulation of basigin expression may be involved in the recruitment of leukocytes to the mouse uterus during early pregnancy. The role of basigin during embryo implantation in mice is examined. Basigin regulates matrix metalloproteinase, IL-1, and leukocyte chemoattractant production by uterine stromal cells.

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7

Köpnick, Anna-Lena, Annika Jansen, Katharina Geistlinger, Nathan Hugo Epalle, and Eric Beitz. "Basigin drives intracellular accumulation of l-lactate by harvesting protons and substrate anions." PLOS ONE 16, no. 3 (March 26, 2021): e0249110. http://dx.doi.org/10.1371/journal.pone.0249110.

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Transmembrane transport of l-lactate by members of the monocarboxylate transporter family, MCT, is vital in human physiology and a malignancy factor in cancer. Interaction with an accessory protein, typically basigin, is required to deliver the MCT to the plasma membrane. It is unknown whether basigin additionally exerts direct effects on the transmembrane l-lactate transport of MCT1. Here, we show that the presence of basigin leads to an intracellular accumulation of l-lactate 4.5-fold above the substrate/proton concentrations provided by the external buffer. Using basigin truncations we localized the effect to arise from the extracellular Ig-I domain. Identification of surface patches of condensed opposite electrostatic potential, and experimental analysis of charge-affecting Ig-I mutants indicated a bivalent harvesting antenna functionality for both, protons and substrate anions. From these data, and determinations of the cytosolic pH with a fluorescent probe, we conclude that the basigin Ig-I domain drives lactate uptake by locally increasing the proton and substrate concentration at the extracellular MCT entry site. The biophysical properties are physiologically relevant as cell growth on lactate media was strongly promoted in the presence of the Ig-I domain. Lack of the domain due to shedding, or misfolding due to breakage of a stabilizing disulfide bridge reversed the effect. Tumor progression according to classical or reverse Warburg effects depends on the transmembrane l-lactate distribution, and this study shows that the basigin Ig-I domain is a pivotal determinant.

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8

Belton, Robert J., Li Chen, Fernando S. Mesquita, and Romana A. Nowak. "Basigin-2 Is a Cell Surface Receptor for Soluble Basigin Ligand." Journal of Biological Chemistry 283, no. 26 (April 22, 2008): 17805–14. http://dx.doi.org/10.1074/jbc.m801876200.

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9

Ovens, Matthew J., Christine Manoharan, Marieangela C. Wilson, Clarey M. Murray, and Andrew P. Halestrap. "The inhibition of monocarboxylate transporter 2 (MCT2) by AR-C155858 is modulated by the associated ancillary protein." Biochemical Journal 431, no. 2 (September 28, 2010): 217–25. http://dx.doi.org/10.1042/bj20100890.

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In mammalian cells, MCTs (monocarboxylate transporters) require association with an ancillary protein to enable plasma membrane expression of the active transporter. Basigin is the preferred binding partner for MCT1, MCT3 and MCT4, and embigin for MCT2. In rat and rabbit erythrocytes, MCT1 is associated with embigin and basigin respectively, but its sensitivity to inhibition by AR-C155858 was found to be identical. Using RT (reverse transcription)–PCR, we have shown that Xenopus laevis oocytes contain endogenous basigin, but not embigin. Co-expression of exogenous embigin was without effect on either the expression of MCT1 or its inhibition by AR-C155858. In contrast, expression of active MCT2 at the plasma membrane of oocytes was significantly enhanced by co-expression of exogenous embigin. This additional transport activity was insensitive to inhibition by AR-C155858 unlike that by MCT2 expressed with endogenous basigin that was potently inhibited by AR-C155858. Chimaeras and C-terminal truncations of MCT1 and MCT2 were also expressed in oocytes in the presence and absence of exogenous embigin. L-Lactate Km values for these constructs were determined and revealed that the TM (transmembrane) domains of an MCT, most probably TM7–TM12, but not the C-terminus, are the major determinants of L-lactate affinity, whereas the associated ancillary protein has little or no effect. Inhibitor titrations of lactate transport by these constructs indicated that embigin modulates MCT2 sensitivity to AR-C155858 through interactions with both the intracellular C-terminus and TMs 3 and 6 of MCT2. The C-terminus of MCT2 was found to be essential for its expression with endogenous basigin.

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10

Sakuragi, Takaharu, Ryuta Kanai, Akihisa Tsutsumi, Hirotaka Narita, Eriko Onishi, Kohei Nishino, Takuya Miyazaki, et al. "The tertiary structure of the human Xkr8–Basigin complex that scrambles phospholipids at plasma membranes." Nature Structural & Molecular Biology 28, no. 10 (October 2021): 825–34. http://dx.doi.org/10.1038/s41594-021-00665-8.

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AbstractXkr8–Basigin is a plasma membrane phospholipid scramblase activated by kinases or caspases. We combined cryo-EM and X-ray crystallography to investigate its structure at an overall resolution of 3.8 Å. Its membrane-spanning region carrying 22 charged amino acids adopts a cuboid-like structure stabilized by salt bridges between hydrophilic residues in transmembrane helices. Phosphatidylcholine binding was observed in a hydrophobic cleft on the surface exposed to the outer leaflet of the plasma membrane. Six charged residues placed from top to bottom inside the molecule were essential for scrambling phospholipids in inward and outward directions, apparently providing a pathway for their translocation. A tryptophan residue was present between the head group of phosphatidylcholine and the extracellular end of the path. Its mutation to alanine made the Xkr8–Basigin complex constitutively active, indicating that it plays a vital role in regulating its scramblase activity. The structure of Xkr8–Basigin provides insights into the molecular mechanisms underlying phospholipid scrambling.

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11

Tabolacci, Claudio, Martina Cordella, Sabrina Mariotti, Stefania Rossi, Cinzia Senatore, Carla Lintas, Lauretta Levati, et al. "Melanoma Cell Resistance to Vemurafenib Modifies Inter-Cellular Communication Signals." Biomedicines 9, no. 1 (January 15, 2021): 79. http://dx.doi.org/10.3390/biomedicines9010079.

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The therapeutic success of BRAF inhibitors (BRAFi) and MEK inhibitors (MEKi) in BRAF-mutant melanoma is limited by the emergence of drug resistance, and several lines of evidence suggest that changes in the tumor microenvironment can play a pivotal role in acquired resistance. The present study focused on secretome profiling of melanoma cells sensitive or resistant to the BRAFi vemurafenib. Proteomic and cytokine/chemokine secretion analyses were performed in order to better understand the interplay between vemurafenib-resistant melanoma cells and the tumor microenvironment. We found that vemurafenib-resistant melanoma cells can influence dendritic cell (DC) maturation by modulating their activation and cytokine production. In particular, human DCs exposed to conditioned medium (CM) from vemurafenib-resistant melanoma cells produced higher levels of pro-inflammatory cytokines—that potentially facilitate melanoma growth—than DCs exposed to CM derived from parental drug-sensitive cells. Bioinformatic analysis performed on proteins identified by mass spectrometry in the culture medium from vemurafenib-sensitive and vemurafenib-resistant melanoma cells suggests a possible involvement of the proteasome pathway. Moreover, our data confirm that BRAFi-resistant cells display a more aggressive phenotype compared to parental ones, with a significantly increased production of interferon-γ, interleukin-8, vascular-endothelial growth factor, CD147/basigin, and metalloproteinase 2 (MMP-2). Plasma levels of CD147/basigin and MMP-2 were also measured before the start of therapy and at disease progression in a small group of melanoma patients treated with vemurafenib or vemurafenib plus cobimetinib. A significant increment in CD147/basigin and MMP-2 was observed in all patients at the time of treatment failure, strengthening the hypothesis that CD147/basigin might play a role in BRAFi resistance.

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12

Zenonos, Zenon A., Sara K. Dummler, Nicole Müller-Sienerth, Jianzhu Chen, Peter R. Preiser, Julian C. Rayner, and Gavin J. Wright. "Basigin is a druggable target for host-oriented antimalarial interventions." Journal of Experimental Medicine 212, no. 8 (July 20, 2015): 1145–51. http://dx.doi.org/10.1084/jem.20150032.

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Plasmodium falciparum is the parasite responsible for the most lethal form of malaria, an infectious disease that causes a large proportion of childhood deaths and poses a significant barrier to socioeconomic development in many countries. Although antimalarial drugs exist, the repeated emergence and spread of drug-resistant parasites limit their useful lifespan. An alternative strategy that could limit the evolution of drug-resistant parasites is to target host factors that are essential and universally required for parasite growth. Host-targeted therapeutics have been successfully applied in other infectious diseases but have never been attempted for malaria. Here, we report the development of a recombinant chimeric antibody (Ab-1) against basigin, an erythrocyte receptor necessary for parasite invasion as a putative antimalarial therapeutic. Ab-1 inhibited the PfRH5-basigin interaction and potently blocked erythrocyte invasion by all parasite strains tested. Importantly, Ab-1 rapidly cleared an established P. falciparum blood-stage infection with no overt toxicity in an in vivo infection model. Collectively, our data demonstrate that antibodies or other therapeutics targeting host basigin could be an effective treatment for patients infected with multi-drug resistant P. falciparum.

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13

van Ooij, Christiaan. "Basigin opens the door to malaria." Nature Reviews Microbiology 10, no. 1 (November 28, 2011): 3. http://dx.doi.org/10.1038/nrmicro2715.

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14

Bornhauser, Beat C., Jeannette Boutter, Peter Horvath, Martin Stanulla, and Jean-Pierre Bourquin. "Image-Based RNA Interference Screening Identifies Microenvironmental Signals Supporting Primary Acute Lymphoblastic Leukemia Cell Survival." Blood 120, no. 21 (November 16, 2012): 2348. http://dx.doi.org/10.1182/blood.v120.21.2348.2348.

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Abstract Abstract 2348 Leukemia cells are critically dependent upon interactions with the microenvironment in the bone marrow and at extramedullary sanctuary sites, which is likely to provide a protective mechanism to escape chemotherapy. In vitro, co-culture of primary ALL cells on human bone marrow derived mesenchymal stromal cells (MSCs) provides survival cues allowing long-term cultures. In contrast, primary ALL cells rapidly undergo cell death when cultured without stromal support. We developed an automated microscopy-based approach to identify pro-survival signals by RNA interference of candidate genes in MSCs and subsequent evaluation of leukemia cell survival, enabling us to functionally profile primary leukemia cells. We took advantage of our leukemia xenograft system as a renewable source of well characterized samples derived from cases with very high risk (VHR) ALL, which were selected based on clinical resistance to chemotherapy. Based on gene expression and cell surface proteomic data that we had obtained from both cellular compartments, we generated a customized siRNA library for 110 candidate genes with a potential function in stromal support. Primary ALL cells were seeded on reversely transfected MSC cells and ALL cell viability was assessed with a fluorescent vital dye after 6 days. Image analysis and machine learning algorithms were developed for quantification of surviving ALL cells on top of MSC. Evaluating three VHR-ALL cases we observed a strong decrease of viability when interfering with the expression of 14 candidate genes in 2 out of 3 patients. Interestingly, in validation studies with 7 additional cases, the pattern of dependence on the genes tested were confirmed to be only partially overlapping between patients, indicating the existence of functional differences in distinct subsets. As a proof of concept, we could show that down-regulation of VCAM1 or the VEGF pathway in MSCs decreased ALL survival supporting earlier studies. Concomitantly, inhibitors of VEGF signalling recapitulated ALL cell viability decrease for patients that showed to be dependent on VEGFC expression in MSCs. One of the strongest effects on ALL survival was achieved by down-regulation of the membrane protein Basigin (CD147). Specifically, 13 out of 17 ALL cases were affected by the modulation of Basigin on MSC level. Basigin has been implicated in cell signalling, in interactions with extracellular matrix and serves as chaperone to different membrane carrier proteins. Among putative Basigin interactors we identified the heteromeric amino acid transporter SLC3A2 (CD98) to be required for ALL survival in the same set of ALL cases. The down-regulation of Basigin, SLC3A2 or both together in MSC cells induces an increase in ROS in ALL cells resulting in apoptotic cell death, which indicates that Basigin/SLC3A2 function is important for the integrity of ALL cell metabolism in this model of the leukemia niche. We are now investigating which metabolites are implicated in the mechanism of action. Taken together, we have established a robust platform for systematic functional investigation of primary ALL survival in a 2-D model of the microenvironment and obtained evidence for patient-specific dependence of leukemia cell survival on stromal support. Critical interactions between ALL cells and bone marrow stromal cells can be identified with this approach, which will be useful for unbiased higher throughput screening and combinatorial testing. This platform will also be of great interest for preclinical drug profiling on clinically relevant patients samples in the context of protective bone marrow signals. Disclosures: No relevant conflicts of interest to declare.

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15

Hérubel, François, Saïd El Mouatassim, Pierre Guérin, René Frydman, and Yves Ménézo. "Genetic expression of monocarboxylate transporters during human and murine oocyte maturation and early embryonic development." Zygote 10, no. 2 (May 2002): 175–81. http://dx.doi.org/10.1017/s096719940200223x.

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During the early preimplantation stages of human embryos, pyruvate and lactate, but not glucose, are the preferred energy substrates. Transport of these monocarboxylates is mediated, in mammalian cells, by a family of transporters, designated as monocarboxylate transporters (MCTs). Human and mouse genetic expression of MCT members 1, 2, 3, 4 and basigin, a chaperone protein of MCT1 and MCT4, was qualitatively analysed using the reverse transcription nested polymerase chain reaction (RT-nested PCR) in immature oocytes (germinal vesicle stage; GV), in non-fertilised metaphase II (MII) oocytes and in embryos from 2-cell stage to blastocysts. Transcripts encoding for MCT1 and MCT2 were present, under a polyadenylated form, in the majority of the human and mouse oocytes and early embryos. MCT3 transcripts were not detected in either human or mouse. MCT4 mRNA was not detected in human oocytes and embryos, but was present in mouse oocytes and embryos. This fact could imply differences in lactate transport and regulation of intracellular pH between human and murine early embryos. Basigin transcripts were present in mouse and human MII oocytes and preimplantation embryos, but were not detected at GV stage. However, using 3' end-specific primers in the RT reaction instead of Oligo(dT)12-18 primers, transcripts encoding for this protein were then detected at GV stage in both species. This result suggests that a regulated polyadenylation process occurs during oocyte maturation for these transcripts. Thus, basigin mRNA can be considered as a marker of oocyte cytoplasmic maturation in human and mouse species.

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16

Chambers, Patrick William. "Basigin Binds Spike S on SARS-CoV2." OALib 08, no. 11 (2021): 1–7. http://dx.doi.org/10.4236/oalib.1108064.

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17

Zhu, Xuejiao, Libin Wen, Wei Wang, Qi Xiao, and Kongwang He. "Basigin-CyP elevated porcine circovirus type2 replication." Virus Research 289 (November 2020): 198152. http://dx.doi.org/10.1016/j.virusres.2020.198152.

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18

Betsuyaku, Tomoko, Kenji Kadomatsu, Gail L. Griffin, Takashi Muramatsu, and Robert M. Senior. "Increased Basigin in Bleomycin-Induced Lung Injury." American Journal of Respiratory Cell and Molecular Biology 28, no. 5 (May 2003): 600–606. http://dx.doi.org/10.1165/rcmb.2002-0059oc.

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19

Finch, NiCole A., Paul J. Linser, and Judith D. Ochrietor. "Hydrophobic Interactions Stabilize the Basigin-MCT1 Complex." Protein Journal 28, no. 7-8 (September 17, 2009): 362–68. http://dx.doi.org/10.1007/s10930-009-9202-3.

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20

Liao, C. G., L. M. Kong, F. Song, J. L. Xing, L. X. Wang, Z. J. Sun, H. Tang, et al. "Characterization of Basigin Isoforms and the Inhibitory Function of Basigin-3 in Human Hepatocellular Carcinoma Proliferation and Invasion." Molecular and Cellular Biology 31, no. 13 (May 2, 2011): 2591–604. http://dx.doi.org/10.1128/mcb.05160-11.

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21

Clamp, Michael F., Judith D. Ochrietor, Tatiana P. Moroz, and Paul J. Linser. "Developmental analyses of 5A11/Basigin, 5A11/Basigin-2 and their putative binding partner MCT1 in the mouse eye." Experimental Eye Research 78, no. 4 (April 2004): 777–89. http://dx.doi.org/10.1016/j.exer.2003.12.004.

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22

Okubo, Aoi, Youhei Uchida, Yuko Higashi, Takuya Sato, Youichi Ogawa, Akihiro Ryuge, Kenji Kadomatsu, and Takuro Kanekura. "CD147 Is Essential for the Development of Psoriasis via the Induction of Th17 Cell Differentiation." International Journal of Molecular Sciences 23, no. 1 (December 24, 2021): 177. http://dx.doi.org/10.3390/ijms23010177.

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Th17 cells play an important role in psoriasis. The differentiation of naïve CD4+ T cells into Th17 cells depends on glycolysis as the energy source. CD147/basigin, an integral transmembrane protein belonging to the immunoglobulin superfamily, regulates glycolysis in association with monocarboxylate transporters (MCTs)-1 and -4 in cancer cells and T cells. We examined whether CD147/basigin is involved in the pathogenesis of psoriasis in humans and psoriasis-model mice. The serum level of CD147 was increased in patients with psoriasis, and the expression of CD147 and MCT-1 was elevated in their dermal CD4+ RORγt+ T cells. In vitro, the potential of naïve CD4+ T cells to differentiate into Th17 cells was abrogated in CD147−/− T cells. Imiquimod (IMQ)-induced psoriatic dermatitis was significantly milder in CD147−/− mice and bone marrow chimeric mice lacking CD147 in the hematopoietic cells of myeloid lineage. These findings demonstrate that CD147 is essential for the development of psoriasis via the induction of Th17 cell differentiation.

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23

Alizzi, Rebecca A., Derek Xu, Conrad M. Tenenbaum, Wei Wang, and Elizabeth R. Gavis. "The ELAV/Hu protein Found in neurons regulates cytoskeletal and ECM adhesion inputs for space-filling dendrite growth." PLOS Genetics 16, no. 12 (December 28, 2020): e1009235. http://dx.doi.org/10.1371/journal.pgen.1009235.

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Dendritic arbor morphology influences how neurons receive and integrate extracellular signals. We show that the ELAV/Hu family RNA-binding protein Found in neurons (Fne) is required for space-filling dendrite growth to generate highly branched arbors of Drosophila larval class IV dendritic arborization neurons. Dendrites of fne mutant neurons are shorter and more dynamic than in wild-type, leading to decreased arbor coverage. These defects result from both a decrease in stable microtubules and loss of dendrite-substrate interactions within the arbor. Identification of transcripts encoding cytoskeletal regulators and cell-cell and cell-ECM interacting proteins as Fne targets using TRIBE further supports these results. Analysis of one target, encoding the cell adhesion protein Basigin, indicates that the cytoskeletal defects contributing to branch instability in fne mutant neurons are due in part to decreased Basigin expression. The ability of Fne to coordinately regulate the cytoskeleton and dendrite-substrate interactions in neurons may shed light on the behavior of cancer cells ectopically expressing ELAV/Hu proteins.

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24

Francesco Calvisi, Diego. "CD147/Basigin: a Warburg oncogene in hepatocellular carcinoma?" Chinese Journal of Cancer Research 28, no. 3 (2016): 377–79. http://dx.doi.org/10.21147/j.issn.1000-9604.2016.03.13.

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25

Najyb, Ouafa, Louise Brissette, and Eric Rassart. "Apolipoprotein D Internalization Is a Basigin-dependent Mechanism." Journal of Biological Chemistry 290, no. 26 (April 27, 2015): 16077–87. http://dx.doi.org/10.1074/jbc.m115.644302.

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26

Lee, A., A. P. Rode, A. J. Nicoll, L. Lim, S. Lim, P. Angus, I. Kronborg, et al. "1057 BASIGIN PREDICTS ADVANCED DISEASE IN HEPATOCELLULAR CARCINOMA." Journal of Hepatology 56 (April 2012): S414. http://dx.doi.org/10.1016/s0168-8278(12)61069-1.

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27

Chen, Xiang, Takuro Kanekura, Shinichro Tsuyama, Fusayoshi Murata, and Tamotsu Kanzaki. "Ultrastructural localization of basigin in normal human epidermis." Histochemistry and Cell Biology 115, no. 6 (June 2001): 465–70. http://dx.doi.org/10.1007/s004180100282.

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28

Guindolet, Damien, and Eric E. Gabison. "Role of CD147 (EMMPRIN/Basigin) in Tissue Remodeling." Anatomical Record 303, no. 6 (March 15, 2019): 1584–89. http://dx.doi.org/10.1002/ar.24089.

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29

Yoshioka, Tomoki, Tomoki Kosugi, Yoshiko Mori, Kayaho Maeda, Seiichi Matsuo, and Shoichi Maruyama. "SP050THE ROLE OF BASIGIN IN THE DEVELOPMENT OF PROTEINURIA." Nephrology Dialysis Transplantation 31, suppl_1 (May 2016): i103. http://dx.doi.org/10.1093/ndt/gfw157.11.

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30

Kato, Noritoshi, Tomoki Kosugi, Waichi Sato, Takuji Ishimoto, Hiroshi Kojima, Yuka Sato, Kazuma Sakamoto, et al. "Basigin/CD147 Promotes Renal Fibrosis after Unilateral Ureteral Obstruction." American Journal of Pathology 178, no. 2 (February 2011): 572–79. http://dx.doi.org/10.1016/j.ajpath.2010.10.009.

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31

Wu, Xiao-Dong, Meng-Yao Zhang, Ya-Tong Chen, Hui Yao, Qing Zhang, Wen-Jing Wang, Da-Fu Fu, et al. "Generation and Characterization of Fibroblast-Specific Basigin Knockout Mice." Molecular Biotechnology 61, no. 2 (December 11, 2018): 111–21. http://dx.doi.org/10.1007/s12033-018-0141-0.

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32

Li, Rongsong, Lei Huang, Huiming Guo, and Bryan P. Toole. "Basigin (murine EMMPRIN) stimulates matrix metalloproteinase production by fibroblasts." Journal of Cellular Physiology 186, no. 3 (2001): 371–79. http://dx.doi.org/10.1002/1097-4652(2000)9999:999<000::aid-jcp1042>3.0.co;2-8.

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33

Zhao, Shu-Hua, Yu Wang, Li Wen, Zhen-Bo Zhai, Zhen-Hua Ai, Nian-Ling Yao, Li Wang, et al. "Basigin-2 is the predominant basigin isoform that promotes tumor cell migration and invasion and correlates with poor prognosis in epithelial ovarian cancer." Journal of Translational Medicine 11, no. 1 (2013): 92. http://dx.doi.org/10.1186/1479-5876-11-92.

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34

Priego-Hernández, Víctor D., Adán Arizmendi-Izazaga, Diana G. Soto-Flores, Norma Santiago-Ramón, Milagros D. Feria-Valadez, Napoleón Navarro-Tito, Hilda Jiménez-Wences, et al. "Expression of HIF-1α and Genes Involved in Glucose Metabolism Is Increased in Cervical Cancer and HPV-16-Positive Cell Lines." Pathogens 12, no. 1 (December 25, 2022): 33. http://dx.doi.org/10.3390/pathogens12010033.

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Cervical cancer (CC) is the most common cancer in women in the lower genital tract. The main risk factor for developing CC is persistent infection with HPV 16. The E6 and E7 oncoproteins of HPV 16 have been related to metabolic reprogramming in cancer through the regulation of the expression and stability of HIF-1α and consequently of the expression of its target genes, such as HIF1A (HIF-1α), SLC2A1 (GLUT1), LDHA, CA9 (CAIX), SLC16A3 (MCT4), and BSG (Basigin or CD147), which are involved in glucose metabolism. This work aimed to evaluate the expression of HIF-1α, GLUT1, LDHA, CAIX, MCT4, and Basigin in patient samples and CC cell lines. To evaluate the expression level of HIF1A, SLC2A1, LDHA, CA9, SLC16A3, and BSG genes in tissue from patients with CC and normal tissue, the TCGA dataset was used. To evaluate the expression level of these genes by RT-qPCR in CC cell lines, HPV-negative (C-33A) and HPV-16-positive (SiHa and Ca Ski) cell lines were used. Increased expression of HIF1A, SLC2A1, LDHA, SLC16A3, and BSG was found in Ca Ski and CA9 in SiHa compared to C-33A. Similar results were observed in CC tissues compared to normal tissue obtained by bioinformatics analysis. In conclusion, the expression of HIF-1α, GLUT1, LDHA, CAIX, MCT4, and BSG genes is increased in CC and HPV-16-positive cell lines.

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35

Hernán, Pérez Camacho, Suhevic Jorge, Malcervelli Daniela, Fischman María Laura, Cisale Humberto, and Mundo Silvia. "Evidence of the Expression of Basigin in Mature Porcine Sperm." Archives of Urology 1, no. 1 (2018): 17–21. http://dx.doi.org/10.22259/2638-5228.0101004.

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36

Lee, Cheuk-Lun, Maggie P. Y. Lam, Kevin K. W. Lam, Carmen O. N. Leung, Ronald T. K. Pang, Ivan K. Chu, Tiffany H. L. Wan, Joyce Chai, William S. B. Yeung, and Philip C. N. Chiu. "Identification of CD147 (basigin) as a mediator of trophoblast functions." Human Reproduction 28, no. 11 (September 5, 2013): 2920–29. http://dx.doi.org/10.1093/humrep/det355.

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37

Wightman, Samantha M., Robert J. Belton, Johnathan E. Lawrence, and Robert J. Winn. "CBIO-43ROLE OF BASIGIN-3 IN MMP EXPRESSION IN GBM." Neuro-Oncology 17, suppl 5 (November 2015): v63.5—v64. http://dx.doi.org/10.1093/neuonc/nov209.43.

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38

Curtin, K. D. "Basigin (EMMPRIN/CD147) interacts with integrin to affect cellular architecture." Journal of Cell Science 118, no. 12 (June 15, 2005): 2649–60. http://dx.doi.org/10.1242/jcs.02408.

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39

Muramatsu, Takashi. "Basigin (CD147), a multifunctional transmembrane glycoprotein with various binding partners." Journal of Biochemistry 159, no. 5 (December 18, 2015): 481–90. http://dx.doi.org/10.1093/jb/mvv127.

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40

Kanekura, Takuro, and Xiang Chen. "CD147/basigin promotes progression of malignant melanoma and other cancers." Journal of Dermatological Science 57, no. 3 (March 2010): 149–54. http://dx.doi.org/10.1016/j.jdermsci.2009.12.008.

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41

Munro, Michelle, Yazan Akkam, and Kathryn D. Curtin. "Mutational analysis of Drosophila basigin function in the visual system." Gene 449, no. 1-2 (January 2010): 50–58. http://dx.doi.org/10.1016/j.gene.2009.09.004.

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42

Luo, Zhongling, Xu Zhang, Weiqi Zeng, Juan Su, Keda Yang, Lixia Lu, Chuan Bian Lim, et al. "TRAF6 regulates melanoma invasion and metastasis through ubiquitination of Basigin." Oncotarget 7, no. 6 (January 12, 2016): 7179–92. http://dx.doi.org/10.18632/oncotarget.6886.

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43

Mannowetz, Nadja, Petra Wandernoth, and Gunther Wennemuth. "Basigin interacts with both MCT1 and MCT2 in murine spermatozoa." Journal of Cellular Physiology 227, no. 5 (January 23, 2012): 2154–62. http://dx.doi.org/10.1002/jcp.22949.

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44

Nakai, Masaaki, Li Chen, and Romana A. Nowak. "Tissue distribution of basigin and monocarboxylate transporter 1 in the adult male mouse: A study using the wild-type and basigin gene knockout mice." Anatomical Record Part A: Discoveries in Molecular, Cellular, and Evolutionary Biology 288A, no. 5 (2006): 527–35. http://dx.doi.org/10.1002/ar.a.20320.

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45

Reddy, K. Sony, Alok K. Pandey, Hina Singh, Tajali Sahar, Amlabu Emmanuel, Chetan E. Chitnis, Virander S. Chauhan, and Deepak Gaur. "Bacterially Expressed Full-Length Recombinant Plasmodium falciparum RH5 Protein Binds Erythrocytes and Elicits Potent Strain-Transcending Parasite-Neutralizing Antibodies." Infection and Immunity 82, no. 1 (October 14, 2013): 152–64. http://dx.doi.org/10.1128/iai.00970-13.

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ABSTRACTPlasmodium falciparumreticulocyte binding-like homologous protein 5 (PfRH5) is an essential merozoite ligand that binds with its erythrocyte receptor, basigin. PfRH5 is an attractive malaria vaccine candidate, as it is expressed by a wide number ofP. falciparumstrains, cannot be genetically disrupted, and exhibits limited sequence polymorphisms. Viral vector-induced PfRH5 antibodies potently inhibited erythrocyte invasion. However, it has been a challenge to generate full-length recombinant PfRH5 in a bacterial-cell-based expression system. In this study, we have produced full-length recombinant PfRH5 inEscherichia colithat exhibits specific erythrocyte binding similar to that of the native PfRH5 parasite protein and also, importantly, elicits potent invasion-inhibitory antibodies against a number ofP. falciparumstrains. Antibasigin antibodies blocked the erythrocyte binding of both native and recombinant PfRH5, further confirming that they bind with basigin. We have thus successfully produced full-length PfRH5 as a functionally active erythrocyte binding recombinant protein with a conformational integrity that mimics that of the native parasite protein and elicits potent strain-transcending parasite-neutralizing antibodies.P. falciparumhas the capability to develop immune escape mechanisms, and thus, blood-stage malaria vaccines that target multiple antigens or pathways may prove to be highly efficacious. In this regard, antibody combinations targeting PfRH5 and other key merozoite antigens produced potent additive inhibition against multiple worldwideP. falciparumstrains. PfRH5 was immunogenic when immunized with other antigens, eliciting potent invasion-inhibitory antibody responses with no immune interference. Our results strongly support the development of PfRH5 as a component of a combination blood-stage malaria vaccine.

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Ganusov, Vitaly V., and Aram Bejnood. "Innate immunity does not contribute to the resistance of mice from different vendors to P. yoelii infection." Journal of Immunology 198, no. 1_Supplement (May 1, 2017): 57.9. http://dx.doi.org/10.4049/jimmunol.198.supp.57.9.

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Abstract Nearly 500,000 individuals die annually from Plasmodium infections. Factors contributing to susceptibility to Plasmodium infections remain poorly understood. It was recently observed that C57BL/6 mice from different vendors (NCI, Harlem, Taconic, Jackson) have different susceptibility to Plasmodium yoelii infection: Jackson/Taconic mice generally have lower peak parasitemia in the blood and better survival than NIC/Harlem mice (Villarino et al. PNAS 2016). Bioinformatic analysis suggested that high mortality of susceptible mice could arise due to a higher expression of basigin, a protein required by Plasmodium falciparum to invade red blood cells in humans (Stough et al. Front Microbiol 2017). We applied a series of mathematical models of different levels of complexity to experimental data on P. yoelii dynamics in mice from these 4 vendors. Our analysis suggests that there are no statistically significant differences in the P. yoelii dynamics during the first 10–14 days post infection, and that the estimated rates of parasite replication were independent of the vendor type. In contrast, we found large differences in parameters for Plasmodium-specific adaptive immune response suggesting that resistant mice mounted a faster and a more efficient response. Our results thus suggest that higher expression of basigin is unlikely to explain higher susceptibility of NCI/Harlem mice to P. yoelii infection and that innate immunity controlling parasite replication during the first 2 weeks of infection unlikely to be different between susceptible and resistant mice. In contrast, a faster generation of the adaptive immunity in resistant mice was likely to be responsible for better parasite control.

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Hiraishi, Katsuya, Tatsuo Ide, Fumie Jimma, Hiroshi Ohi, Fumiko Inokuchi, Teruo Miyauchi, and Keiji Suzuki. "Immunohistochemical Distribution of Human Basigin by Using a Novel Monoclonal Antibody." ACTA HISTOCHEMICA ET CYTOCHEMICA 36, no. 2 (2003): 135–44. http://dx.doi.org/10.1267/ahc.36.135.

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Toyama, Y., M. Maekawa, K. Kadomatsu, T. Miyauchi, T. Muramatsu, and S. Yuasa. "Histological Characterization of Defective Spermatogenesis in Mice Lacking the Basigin Gene." Anatomia, Histologia, Embryologia: Journal of Veterinary Medicine Series C 28, no. 3 (June 1999): 205–13. http://dx.doi.org/10.1046/j.1439-0264.1999.00194.x.

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49

Crosnier, Cécile, Leyla Y. Bustamante, S. Josefin Bartholdson, Amy K. Bei, Michel Theron, Makoto Uchikawa, Souleymane Mboup, et al. "Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum." Nature 480, no. 7378 (November 9, 2011): 534–37. http://dx.doi.org/10.1038/nature10606.

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50

Kaname, T., T. Miyauchi, A. Kuwano, Y. Matsuda, T. Muramatsu, and T. Kajii. "Mapping basigin (BSG), a member of the immunoglobulin superfamily, to 19p13.3." Cytogenetic and Genome Research 64, no. 3-4 (1993): 195–97. http://dx.doi.org/10.1159/000133573.

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