Retinal Degeneration Following Failed Photoreceptor Maturation in 5A11/Basigin Null Mice

Ochrietor, Judith D.; Moroz, Tatiana M.; Kadomatsu, Kenji; Muramatsu, Takashi; Linser, Paul J.

doi:10.1006/exer.2000.0974

Cited by 28 publications

(23 citation statements)

References 31 publications

(44 reference statements)

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“…For example, rod cells in the Bsg knockout mouse retina exhibit gross morphological differences, having smaller outer segments (Ochrietor et al, 2001). Mouse basigin is expressed in both retinal neurons and Müller cell glia (Ochrietor et al, 2003).…”

Section: Mouse Basigin and D-basiginmentioning

confidence: 99%

Basigin (EMMPRIN/CD147) interacts with integrin to affect cellular architecture

Curtin

Meinertzhagen

Wyman

2005

Journal of Cell Science

111

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Basigin, an IgG family glycoprotein found on the surface of human metastatic tumors, stimulates fibroblasts to secrete matrix metalloproteases that remodel the extracellular matrix. Using Drosophila melanogaster we identify intracellular, matrix metalloprotease-independent, roles for basigin. Specifically, we found that basigin, interacting with integrin, is required for normal cell architecture in some cell types. Basigin promotes cytoskeletal rearrangements and the formation of lamellipodia in cultured insect cells. Loss of basigin from photoreceptors leads to misplaced nuclei, rough ER and mitochondria, as well as to swollen axon terminals. These changes in intracellular structure suggest cytoskeletal disruptions. These defects can be rescued by either fly or mouse basigin. Basigin and integrin colocalize to cultured cells and to the visual system. Basigin-mediated changes in the architecture of cultured cells require integrin binding activity. Basigin and integrin interact genetically to affect cell structure in the animal, possibly by forming complexes at cell contacts that help organize internal cell structure.

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Section: Mouse Basigin and D-basiginmentioning

confidence: 99%

Basigin (EMMPRIN/CD147) interacts with integrin to affect cellular architecture

Curtin

Meinertzhagen

Wyman

2005

Journal of Cell Science

111

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“…Only the testes express greater amounts of 5A11/Basigin transcript than the retina [17] . Within the eye, 5A11/Basigin is expressed on the surface of MCs, the RPE, and blood vessel endothelial cells [17,20,21] . We have also seen 5A11/Basigin immunoreactivity on the ciliary apparatus and ciliary pigmented epithelium, as well as the lens epithelium and the anterior portion of the lens [22] .…”

Section: A11/basigin and 5a11/basigin-2 Have Different Patterns Of Ementioning

confidence: 99%

“…This strain of mice exhibits severely depressed electroretinogram recordings from the time of eye opening, despite a normal retinal architecture [1] . The fi rst sign of abnormality is observed at postnatal day 18, when PC outer segments of null mice appear less dense, and perhaps shorter, than those of control littermates [21] . Later, at about 8 weeks of age, degeneration of the PCs begins [20,21] .…”

Section: The 5a11/basigin Null Mouse Has a Novel Form Of Retinal Dystmentioning

confidence: 99%

“…The fi rst sign of abnormality is observed at postnatal day 18, when PC outer segments of null mice appear less dense, and perhaps shorter, than those of control littermates [21] . Later, at about 8 weeks of age, degeneration of the PCs begins [20,21] . The outer nuclear layer is completely degenerated by 8 months of age [20] .…”

Section: The 5a11/basigin Null Mouse Has a Novel Form Of Retinal Dystmentioning

confidence: 99%

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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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“…CD147, a type I membrane protein and a member of the immunoglobulin superfamily (Stockinger et al, 1997), has been independently cloned from different species and is also referred to as human EMMPRIN/M6 (Biswas et al, 1995), mouse basigin (Miyauchi et al, 1990), chicken 5A11 (Fadool and Linser, 1993a), avian HT7 (Seulberger et al, 1992), and rat CE-9 (Nehme et al, 1993). Mice with targeted disruption of the CD147 gene are blind starting 5 weeks after birth (Hori et al, 2000) because of deficient photoreceptor development and retinal degeneration (Ochrietor et al, 2001(Ochrietor et al, , 2002. Significantly, CD147 has a strong expression level in the retina, especially in the RPE (Neill and Barnstable, 1990;Fan et al, 1998;Philp et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

The Basolateral Targeting Signal of CD147 (EMMPRIN) Consists of a Single Leucine and Is Not Recognized by Retinal Pigment Epithelium

Deora

Gravotta

Kreitzer

et al. 2004

MBoC

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CD147, a type I integral membrane protein of the immunoglobulin superfamily, exhibits reversed polarity in retinal pigment epithelium (RPE). CD147 is apical in RPE in contrast to its basolateral localization in extraocular epithelia. This elicited our interest in understanding the basolateral sorting signals of CD147 in prototypic Madin-Darby canine kidney (MDCK) cells. The cytoplasmic domain of CD147 has basolateral sorting information but is devoid of well-characterized basolateral signals, such as tyrosine and di-leucine motifs. Hence, we carried out systematic site-directed mutagenesis to delineate basolateral targeting information in CD147. Our detailed analysis identified a single leucine (252) as the basolateral targeting motif in the cytoplasmic tail of CD147. Four amino acids (243-246) N-terminal to leucine 252 are also critical basolateral determinants of CD147, because deletion of these amino acids leads to mistargeting of CD147 to the apical membranes. We ruled out the involvement of adaptor complex 1B (AP1B) in the basolateral trafficking of CD147, because LLC-PK1 cells lacking AP1B, target CD147 basolaterally. At variance with MDCK cells, the human RPE cell line ARPE-19 does not distinguish between CD147 (WT) and CD147 with leucine 252 mutated to alanine and targets both proteins apically. Thus, our study identifies an atypical basolateral motif of CD147, which comprises a single leucine and is not recognized by RPE cells. This unusual basolateral sorting signal will be useful in unraveling the specialized sorting machinery of RPE cells. INTRODUCTIONEpithelial cells have distinct apical and basolateral membrane domains with different protein and lipid compositions. The asymmetry is essential for the multiple vectorial functions they perform (Rodriguez-Boulan and Nelson, 1989;Yeaman et al., 1999). The polarized protein distribution results from sorting mechanisms operating in the biosynthetic and recycling pathways that recognize specific sorting signals in plasma membrane proteins. Structural features believed to operate as apical sorting signals include glycosylphophatidylinositol anchors (Lisanti et al., 1989), N-glycans (Scheiffele et al., 1995), O-glycans (Yeaman et al., 1997;Jacob et al., 2000), and protein sequences in the transmembrane (Kundu et al., 1996;Lin et al., 1998), or cytoplasmic domains (Chuang and Sung, 1998;Rodriguez-Boulan and Gonzalez, 1999;Nelson and Yeaman, 2001). On the other hand, basolateral signals are formed by short peptide sequences usually found in the protein domain facing the cytosol (Le Gall et al., 1995;Yeaman et al., 1999;Mostov et al., 2000). They mainly include tyrosine motifs (consensus motif NPXY or YXXF) as well as di-leucine and di-hydrophobic residues (Matter et al., 1992;Aroeti et al., 1993;Hunziker and Fumey, 1994;Simonsen et al., 1997;Bonifacino and Dell'Angelica, 1999;Rodionov et al., 2000).Different types of epithelial cells vary widely in the final distribution of plasma membrane proteins or in the pathways that these proteins follow to the cell surf...

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Retinal Degeneration Following Failed Photoreceptor Maturation in 5A11/Basigin Null Mice

Cited by 28 publications

References 31 publications

Basigin (EMMPRIN/CD147) interacts with integrin to affect cellular architecture

Basigin (EMMPRIN/CD147) interacts with integrin to affect cellular architecture

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

The Basolateral Targeting Signal of CD147 (EMMPRIN) Consists of a Single Leucine and Is Not Recognized by Retinal Pigment Epithelium

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