Structure of the Mouse Basigin Gene, a Unique Member of the Immunoglobulin Superfamily

Miyauchi, Terukatsu; Jimma, Fumie; Igakura, Tadahiko; Yu, Shyr-Shen; Ozawa, Masayuki; Muramatsu, Takashi

doi:10.1093/oxfordjournals.jbchem.a124971

Cited by 26 publications

(13 citation statements)

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“…Our results are in agreement with previous studies that detected Na,K-ATPase (6, 48), Glut-1 (49, 50), monocarboxylate transporter (11), carbonic anhydrase (51), basigin (52,53), EBP50 (46,47), the vitronectin receptor (54), and the chloride intracellular channel 6 (55) in the RPE apical microvilli. However, proteins such as peropsin, Kir7.1, and organic anion transport protein 2, known to localize to RPE microvilli, were not identified in our study.…”

Section: Peptides Matched Functionsupporting

confidence: 93%

Proteomic Characterization of Isolated Retinal Pigment Epithelium Microvilli

Bonilha

Bhattacharya

West

et al. 2004

Molecular & Cellular Proteomics

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Polarized epithelial cells are characterized by displaying compartmentalized functions associated with differential distribution of transporters, structural proteins, and signaling molecules on their apical and basolateral surfaces. Their apical surfaces frequently elaborate microvilli, which vary in structure according to the specific type and function of each epithelium. The molecular basis of this heterogeneity is poorly understood. However, differences in function will undoubtedly be reflected in the specific molecular composition of the apical surface in each epithelial subtype. We have exploited a method for isolating microvilli from the mouse eye using wheat germ agglutinin (WGA)-agarose beads to begin to understand the specific molecular composition of apical microvilli of the retinal pigment epithelium (RPE) and expand our knowledge of the potential function of this interface. Initially, apical RPE plasma membranes bound to WGA beads were processed for morphological analysis using known apical and basolateral surface markers. The protein composition of the apical microvilli was then established using proteomic analysis. Over 200 proteins were identified, including a number of proteins previously known to be localized to RPE microvilli, as well as others not known to be present at this surface. Localization of novel proteins identified with proteomics was confirmed by immunohistochemistry in both mouse and rat eye tissue. The data generated provides new information on the protein composition of the RPE apical microvilli. The isolation technique used should be amenable for isolating microvilli in other epithelia as well, allowing new insights into additional functions of this important epithelial compartment. Molecular & Cellular Proteomics 3:1119 -1127, 2004.Epithelial cells are characterized by the asymmetric distribution of proteins and lipids in their plasma membrane: a basic feature referred to as polarity. The functional polarity of epithelial cells is dependent on the asymmetric distribution of specific enzymes, signaling molecules, and transport proteins between their apical and basolateral surface membranes (1). The apical surface of cuboidal and columnar epithelial cells commonly faces a luminal cavity and is characterized by the presence of numerous surface membrane elaborations referred to as microvilli. Microvilli greatly increase the apical surface area and, consequently, the number of transport and signaling proteins it contains, thereby enhancing the epithelial functional capacity. Absorptive epithelia such as kidney and intestine have their apical surface decorated with highly organized apical microvilli of uniform length and width. More dynamic and less organized structures are present in the epithelial cells of the placenta and the retinal pigment epithelium (RPE), 1 which perform endocytosis and phagocytosis, respectively. The basis of this morphological heterogeneity is poorly understood and is likely to be related to the specialized function and specific molecular composition of the ...

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Section: Peptides Matched Functionsupporting

confidence: 93%

Proteomic Characterization of Isolated Retinal Pigment Epithelium Microvilli

Bonilha

Bhattacharya

West

et al. 2004

Molecular & Cellular Proteomics

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“…CD147 was identified independently in various species and are referenced throughout the literature as EMMPRIN (Extracellular Matrix Metalloproteinase-Inducer), M6 (Human) (Kasinrerk et al 1992), Neurothelin, 5A11 and HT7 (chicken) (Seulberger et al 1992;Fadool et al 1993;Schlosshauer et al 1995), OX47 and CE9 (rat) (Fossum et al 1991;Nehme et al 1995), and Basigin, gp42 (human and mouse) (Altruda et al 1989;Miyauchi et al 1991;Miyauchi et al 1995). The CD147 gene, designated BSG for basigin, is located on chromosome 19p13.3 and encodes a 29 kD protein, though migration on SDS-PAGE usually occurs between 35-65 kD, depending on the degree of glycosylation (Kasinrerk et al 1992;Kirsch et al 1997;Kasinrerk et al 1999).…”

Section: Structural Organizationmentioning

confidence: 99%

CD147 immunoglobulin superfamily receptor function and role in pathology

Iacono

Brown

Greene

et al. 2007

Experimental and Molecular Pathology

243

206

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The immunoglobulin superfamily member CD147 plays an important role in fetal, neuronal, lymphocyte and extracellular matrix development. Here we review the current understanding of CD147 expression and protein interactions with regard to CD147 function and its role in pathologic conditions including heart disease, Alzheimer's disease, stroke and cancer. A model linking hypoxic conditions found within the tumor microenvironment to up-regulation of CD147 expression and tumor progression is introduced.

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“…Characterization of the 5A11 antigen showed that it is identical to the HT7 antigen, an inducible marker on endothelial cells of the blood-brain barrier [4] . Other homologous proteins in this family include M6 or EMMPRIN in human [5,6] ; OX-47, CD-147, CE-9, or PE-2 in rat [7][8][9] ; RPE7 in bovine retina [10] , and Basigin or gp42 in mouse [11][12][13] . For each of the 5A11/Basigin homologues, a transcript of ~1.2 kb has been cloned, which codes for a nascent polypeptide of ~30 kDa [3][4][5][6][7][8][9][10][11][12][13] .…”

Section: A11/basigin and 5a11/basigin-2 Are Members Of The Immunoglomentioning

confidence: 99%

5A11/Basigin Gene Products Are Necessary for Proper Maturation and Function of the Retina

Ochrietor¹,

Linser²

2004

Dev Neurosci

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5A11/Basigin gene products are important membrane glycoproteins for development and maturation of the retina. The gene encodes two immunoglobulin-like, membrane-bound glycoproteins as a result of splice variation. The smaller protein product, named 5A11/Basigin, is expressed by many tissues within the mouse, whereas the larger protein product, named 5A11/Basigin-2, is expressed only by the photoreceptor cells (PCs) of the retina. Mice in which the gene for 5A11/Basigin has been deleted have several abnormalities, including blindness from the time of eye opening with subsequent degeneration of the PCs. Studies by this laboratory suggest that a developmental deficiency is the underlying cause of the blindness. However, definitive biological functions for 5A11/Basigin and 5A11/Basigin-2 have yet to be defined. It is known that 5A11/Basigin is multifunctional and can interact with several different proteins. Preliminary studies indicate that 5A11/Basigin-2 may be multifunctional as well. Studies by this laboratory and others have demonstrated that 5A11/Basigin (and probably 5A11/Basigin-2) acts as a chaperone for monocarboxylate transporter-1 (MCT-1) translocation to the cell membrane. We have proposed that a lactate metabolon exists within the retina and functions to shuttle lactate, an energy source, from glial cells to the PCs. This metabolon is not present within 5A11/Basigin null mouse retinas, which may be the underlying cause of the retinal dysfunction and subsequent degeneration. Further studies will be necessary to determine which of the functions are critical for proper development of the retina.

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Structure of the Mouse Basigin Gene, a Unique Member of the Immunoglobulin Superfamily

Cited by 26 publications

References 0 publications

Proteomic Characterization of Isolated Retinal Pigment Epithelium Microvilli

Proteomic Characterization of Isolated Retinal Pigment Epithelium Microvilli

CD147 immunoglobulin superfamily receptor function and role in pathology

5A11/Basigin Gene Products Are Necessary for Proper Maturation and Function of the Retina

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