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• W72383048 abstract "The 1990s have been an exciting and productive decade for the molecular dissection of the etiology of Alport syndrome. Alport syndrome is a hereditary glomerulonephritis accompanied usually by sensorineural deafness, frequently by ocular abnormalities, and rarely by diffuse leiomyomatosis (DL), which is characterized by benign nodular smooth muscle tumors of esophagus, tracheo-bronchial tree, and genital tract. The primary mode of inheritance of Alport syndrome is X-linked-dominant, though there are also autosomal-recessive and autosomal-dominant forms, and its overall prevalence is estimated to be 1 in 5000. The only treatments for the nephropathy at end stage are dialysis and renal transplantation.1Reeders ST Molecular genetics of hereditary nephritis.Kidney Int. 1992; 42: 783-792Crossref PubMed Scopus (28) Google Scholar, 2Kashtan CE Michael AF Alport syndrome: from bedside to genome to bedside.Am J Kidney Dis. 1993; 22: 627-640PubMed Scopus (39) Google Scholar, 3Tryggvason K Zhou J Hostikka SL Shows TB Molecular genetics of Alport syndrome.Kidney Int. 1993; 43: 38-44Crossref PubMed Scopus (154) Google Scholar, 4Gubler M-C Antignac C Deschenes G Knebelmann B Hors-Cayla MC Grunfeld J-P Broyer M Habib R Genetic, clinical, and morphologic heterogeneity in Alport's syndrome.Adv Nephrol. 1993; 22: 15-35PubMed Google Scholar, 5Antignac C Molecular genetics of basement membranes: the paradigm of Alport syndrome.Kidney Int. 1995; 47: S29-S33Google Scholar, 6Kashtan CE Alport syndrome.Kidney Int. 1997; 51: S69-S71PubMed Google Scholar Alport syndrome is a basement membrane disease involving type IV collagen. Collagen IV is a major component of all basement membranes. It is composed of α chains that trimerize to form long triple helical protomers. Protomers are secreted by cells and associate with each other in the extracellular matrix to form a chicken-wire-like network.7Hudson BG Wieslander J Wisdom Jr., BJ Noelken ME Biology of disease: Goodpasture syndrome: molecular architecture and function of basement membrane antigen.Lab Invest. 1989; 61: 256-269PubMed Google Scholar This serves as the scaffold for assembly of the basement membrane, which also contains laminin, entactin/nidogen, and sulfated proteoglycans.8Timpl R Brown JC Supramolecular assembly of basement membranes.BioEssays. 1996; 18: 123-132Crossref PubMed Scopus (585) Google Scholar, 9Timpl R Macromolecular organization of basement membranes.Curr Opin Cell Biol. 1996; 8: 618-624Crossref PubMed Scopus (554) Google Scholar There are six genetically distinct collagen IV α chains, α1(IV)-α6(IV). The collagen α1(IV) and α2(IV) chains are the classical chains and are essentially ubiquitous in basement membranes. Mutations in COL4A1 and COL4A2 have not been found in mammals and would likely be embryonically lethal. In contrast, the underlying genetic defect in Alport syndrome is a mutation in any one of three genes encoding what have been termed novel type IV collagen chains. These chains have a restricted tissue distribution. Importantly, they are all major components of the glomerular basement membrane (GBM), which is characteristically thinned, thickened, and split in Alport syndrome. X-linked Alport syndrome is caused by mutations in the collagen α5(IV) chain gene COL4A5, and mutations in COL4A3 and COL4A4, which are linked head-to-head on chromosome 2, are responsible for the autosomal forms of the disease.10Barker DF Hostikka SL Zhou J Chow LT Oliphant AR Gerken SC Gregory MC Skolnick MH Atkin CL Tryggvason K Identification of mutations in the COL4A5 collagen gene in Alport syndrome.Science. 1990; 248: 1224-1227Crossref PubMed Scopus (666) Google Scholar, 11Lemmink HH Mochizuki T van den Heuvel PWJ Schroder CH Barrientos A Monnens LAH van Oost BA Brunner HG Reeders ST Smeets HJM Mutations in the type IV collagen α3 (COL4A3) gene in autosomal recessive Alport syndrome.Hum Mol Genet. 1994; 3: 1269-1273Crossref PubMed Scopus (198) Google Scholar, 12Mochizuki T Lemmink HH Mariyama M Antignac C Gubler M-C Pirson Y Verellen-Dumoulin C Chan B Schroder CH Smeets HJ Reeders ST Identification of mutations in the α3(IV) and α4(IV) collagen genes in autosomal recessive Alport syndrome.Nat Genet. 1994; 8: 77-82Crossref PubMed Scopus (441) Google Scholar A molecular hallmark of the severe forms of Alport syndrome is that mutations affecting only one of the COL4A3-COL4A5 genes result in the absence all three gene products from the GBM. This has been used as circumstantial evidence to suggest a model in which the α3-α5(IV) chains coassemble in a manner that requires all three chains.13Hudson BG Reeders ST Tryggvason K Type IV collagen: structure, gene organization, and role in human diseases.J Biol Chem. 1993; 268: 26033-26036Abstract Full Text PDF PubMed Google Scholar In this model, the nonmutated genes would be transcribed and translated normally, but the chains they encode would be degraded on failing to assemble due to the absence of a normal third chain. This model is attractive, because it is consistent with the inherent trimeric structure of collagen IV protomers. Alternatively, the defect in assembly could be at the level of protomer:protomer interactions in the extracellular matrix. Good evidence for transcriptional down-regulation of the nonmutated genes in a canine model of Alport syndrome has been presented. These data show that the lack of collagen α5(IV) protein due to COL4A5 mutation was associated with a decrease in α3(IV) and α4(IV) steady-state mRNA levels.14Thorner PS Zheng K Kalluri R Jacobs R Hudson BG Coordinate gene expression of the α3, α4, and α5 chains of collagen type IV: evidence from a canine model of X-linked nephritis with a COL4A5 gene mutation.J Biol Chem. 1996; 271: 13821-13828Abstract Full Text Full Text PDF PubMed Scopus (56) Google Scholar This could explain in part the absence of the α3(IV) and α4(IV) chains in mutant dog kidney basement membranes. However, RNA studies in humans and in the two mouse models of Alport syndrome did not find such a down-regulation in steady-state mRNA levels and thus do not support such a transcriptional mechanism.15Nakanishi K Yoshikawa N Iijima K Nakamura H Expression of type IV collagen α3 and α4 chain mRNA in X-linked Alport syndrome.J Am Soc Nephrol. 1996; 7: 938-945Crossref PubMed Google Scholar, 16Miner JH Sanes JR Molecular and functional defects in kidneys of mice lacking collagen α3(IV): implications for Alport syndrome.J Cell Biol. 1996; 135: 1403-1413Crossref PubMed Scopus (255) Google Scholar, 17Cosgrove D Meehan DT Grunkemeyer JA Kornak JM Sayers R Hunter WJ Samuelson GC Collagen COL4A3 knockout: a mouse model for autosomal Alport syndrome.Genes Dev. 1996; 10: 2981-2992Crossref PubMed Scopus (297) Google Scholar The collagen α6(IV) chain is unique in that it has a restricted tissue distribution but is not deposited in the GBM. It is found in basement membranes associated with Bowman's capsule, epidermis, and a subset of smooth muscle cells.18Ninomiya Y Kagawa M Iyama K Naito I Kishiro Y Seyer JM Sugimoto M Oohashi T Sado Y Differential expression of two basement membrane collagen genes, COL4A6 and COL4A5, demonstrated by immunofluorescence staining using peptide-specific monoclonal antibodies.J Cell Biol. 1995; 130: 1219-1229Crossref PubMed Scopus (266) Google Scholar, 19Peissel B Gene L Kalluri R Kashtan C Rennke HG Gallo GR Yoshioka K Sun MJ Hudson BG Neilson EG Zhou J Comparative distribution of the α1(IV), α5(IV), and α6(IV) collagen chains in normal human adult and fetal tissues and in kidneys from X-linked Alport syndrome patients.J Clin Invest. 1995; 96: 1948-1957Crossref PubMed Scopus (121) Google Scholar Consistent with its absence from GBM, mutations that affect only COL4A6 have not been found in Alport patients.20Lemmink HH Schroder CH Monnens LA Smeets HJ The clinical spectrum of type IV collagen mutations.Hum Mutat. 1997; 9: 477-499Crossref PubMed Scopus (145) Google Scholar However, COL4A6 is located on the X chromosome head-to-head with COL4A5 and some COL4A5 deletion mutations that cause Alport syndrome extend into COL4A6.21Zhou J Mochizuki T Smeets H Antignac C Laurila P de Paepe A Tryggvason K Reeders ST Deletion of the paired α5(IV) and α6(IV) collagen genes in inherited smooth muscle tumors.Science. 1993; 261: 1167-1169Crossref PubMed Scopus (241) Google Scholar, 22Heidet L Dahan K Zhou J Xu Z Cochat P Gould JDM Leppig KA Proesmans W Guyot C Guillot M Roussel B Tryggvason K Grunfeld J-P Gubler M-C Antignac C Deletions of both α5(IV) and α6(IV) collagen genes in Alport syndrome and in Alport syndrome associated with smooth muscle tumours.Hum Mol Genet. 1995; 4: 99-108Crossref PubMed Scopus (102) Google Scholar, 23Heidet L Cohen-Solal L Boye E Thorner P Kemper MJ David A Larget Piet L Zhou J Flinter F Zhang X Gubler MC Antignac C Novel COL4A5/COL4A6 deletions, and further characterization of the diffuse leiomyomatosis-Alport syndrome (DL-AS) locus define the DL critical region.Cytogenet Cell Genet. 1997; 78: 240-246Crossref PubMed Scopus (46) Google Scholar Thus, the 5′ ends of both genes are affected. Cases of Alport syndrome associated with diffuse leiomyomatosis always fall into this category, but the extent of the deletion into COL4A6 is limited to the alternative exons 1 and 1′, intron 1, exon 2, and part of the very large intron 2. Interestingly, if the deletion extends into exon 3, then diffuse leiomyomatosis is not observed.22Heidet L Dahan K Zhou J Xu Z Cochat P Gould JDM Leppig KA Proesmans W Guyot C Guillot M Roussel B Tryggvason K Grunfeld J-P Gubler M-C Antignac C Deletions of both α5(IV) and α6(IV) collagen genes in Alport syndrome and in Alport syndrome associated with smooth muscle tumours.Hum Mol Genet. 1995; 4: 99-108Crossref PubMed Scopus (102) Google Scholar, 23Heidet L Cohen-Solal L Boye E Thorner P Kemper MJ David A Larget Piet L Zhou J Flinter F Zhang X Gubler MC Antignac C Novel COL4A5/COL4A6 deletions, and further characterization of the diffuse leiomyomatosis-Alport syndrome (DL-AS) locus define the DL critical region.Cytogenet Cell Genet. 1997; 78: 240-246Crossref PubMed Scopus (46) Google Scholar This leads to the question of how and why some deletions that affect COL4A6 result in diffuse leiomyomatosis, whereas the most extensive ones do not. It has been hypothesized that the more restricted deletions may allow production of a truncated α6(IV) protein in smooth muscle that might be capable of aberrant signaling and lead to the observed benign tumors.22Heidet L Dahan K Zhou J Xu Z Cochat P Gould JDM Leppig KA Proesmans W Guyot C Guillot M Roussel B Tryggvason K Grunfeld J-P Gubler M-C Antignac C Deletions of both α5(IV) and α6(IV) collagen genes in Alport syndrome and in Alport syndrome associated with smooth muscle tumours.Hum Mol Genet. 1995; 4: 99-108Crossref PubMed Scopus (102) Google Scholar However, no stable integration of any α6(IV) protein into esophageal tumor basement membranes from appropriate patients was observed.24Heidet L Cai Y Sado Y Ninomiya Y Thorner P Guicharnaud L Boye E Chauvet V Solal LC Beziau A Torres RG Antignac C Gubler MC Diffuse leiomyomatosis associated with X-linked Alport syndrome: extracellular matrix study using immunohistochemistry and in situ hybridization.Lab Invest. 1997; 76: 233-243PubMed Google Scholar Another possibility is that there is a gene, which may or may not encode a protein, embedded in the large second intron of COL4A6 that is somehow transformed into a dominant promoter of smooth muscle cell proliferation by the deletions that cause Alport syndrome with diffuse leiomyomatosis.22Heidet L Dahan K Zhou J Xu Z Cochat P Gould JDM Leppig KA Proesmans W Guyot C Guillot M Roussel B Tryggvason K Grunfeld J-P Gubler M-C Antignac C Deletions of both α5(IV) and α6(IV) collagen genes in Alport syndrome and in Alport syndrome associated with smooth muscle tumours.Hum Mol Genet. 1995; 4: 99-108Crossref PubMed Scopus (102) Google Scholar Further studies of the ∼140-kb second intron of COL4A6 will be necessary to test this hypothesis. COL4A5-specific mutations lead to the absence of collagen α6(IV) in renal and epidermal basement membranes,18Ninomiya Y Kagawa M Iyama K Naito I Kishiro Y Seyer JM Sugimoto M Oohashi T Sado Y Differential expression of two basement membrane collagen genes, COL4A6 and COL4A5, demonstrated by immunofluorescence staining using peptide-specific monoclonal antibodies.J Cell Biol. 1995; 130: 1219-1229Crossref PubMed Scopus (266) Google Scholar, 19Peissel B Gene L Kalluri R Kashtan C Rennke HG Gallo GR Yoshioka K Sun MJ Hudson BG Neilson EG Zhou J Comparative distribution of the α1(IV), α5(IV), and α6(IV) collagen chains in normal human adult and fetal tissues and in kidneys from X-linked Alport syndrome patients.J Clin Invest. 1995; 96: 1948-1957Crossref PubMed Scopus (121) Google Scholar, 25Hino S Takemura T Sado Y Kagawa M Oohashi T Ninomiya Y Yoshioka K Absence of α6(IV) collagen in kidney and skin of X-linked Alport syndrome patients.Pediatr Nephrol. 1996; 10: 742-744Crossref PubMed Scopus (16) Google Scholar suggesting that the α6(IV) chain cannot assemble into these basement membranes without the α5(IV) chain. One important issue that has not been addressed is the status of collagen α6(IV) protein in the smooth muscle basement membranes of such Alport patients, who do not have deletions extending into COL4A6 and who do not develop leiomyomata. The formal possibility exists that, despite its absence from kidney and skin basement membranes, these patients maintain a somewhat normal complement of α6(IV) protein in their smooth muscle basement membranes. This might play some role in preventing overproliferation of smooth muscle cells. However, if true, then it would be difficult to explain the absence of tumors when COL4A6 deletions extend into exon 3. Nevertheless, whether COL4A5-specific mutations lead to an absence of α6(IV) in smooth muscle basement membranes is certainly worth investigating. The article by Zheng et al26Zheng K Harvey S Sado Y Naito I Ninomiya Y Jacobs R Thorner PS Absence of the α6(IV) chain of collagen type IV in Alport syndrome is related to a failure at the protein assembly level and does not result in diffuse leiomyomatosis.Am J Pathol. 1999; 154: 1883-1891Abstract Full Text Full Text PDF PubMed Scopus (18) Google Scholar published in this issue of The Americal Journal of Pathology finally addresses this and other important points using a canine model of X-linked Alport syndrome. Paul Thorner and colleagues have previously studied this family of Samoyed dogs in depth; they have identified a single base non-sense mutation in COL4A5 and have shown that the affected dogs exhibit many of the characteristics observed in human Alport syndrome.27Thorner P Jansen B Baumal R Valli VE Goldberger A Samoyed hereditary glomerulopathy. Immunohistochemical staining of basement membranes of kidney for laminin, collagen type IV, fibronectin, and Goodpasture antigen, and correlation with electron microscopy of glomerular capillary basement membranes.Lab Invest. 1987; 56: 435-443PubMed Google Scholar, 28Thorner P Baumal R Valli VE Mahuran D McInnes R Marrano P Abnormalities in the NC1 domain of collagen type IV in GBM in canine hereditary nephritis.Kidney Int. 1989; 35: 843-850Crossref PubMed Scopus (12) Google Scholar, 29Baumal R Thorner P Valli VE McInnes R Marrano P Jacobs R Binnington A Bloedow AG Renal disease in carrier female dogs with X-linked hereditary nephritis: implications for female patients with this disease.Am J Pathol. 1991; 139: 751-764PubMed Google Scholar, 30Zheng K Thorner PS Marrano P Baumal R McInnes RR Canine X chromosome-linked hereditary nephritis: a genetic model for human X-linked hereditary nephritis resulting from a single base mutation in the gene encoding the α5 chain of collagen type IV.Proc Natl Acad Sci USA. 1994; 91: 3989-3993Crossref PubMed Scopus (103) Google Scholar In this issue of the Journal they report the cloning and sequencing of DNA adjacent to the 5′ end of canine COL4A5 and show that dog has a COL4A6 gene with many similarities to the human gene, including the tightly linked, head-to-head arrangement with COL4A5. This is the first cross-species comparison of this region, and it shows that although exon 1 is very conserved between human and dog, exon 1′ is not. The authors rightly question the functionality of this exon in dog. Indeed, by Northern blot analysis, they show that COL4A6 mRNAs from bladder smooth muscle contain exon 1 but not exon 1′. The authors use immunohistochemistry to show that the collagen α6(IV) chain is present in bladder smooth muscle basement membranes from a normal dog but is completely absent from the COL4A5 mutant dog smooth muscle. Moreover, despite the absence of α6(IV) protein, α6(IV) mRNA levels in bladder smooth muscle are nearly normal. Finally, leiomyomata have never been observed in this family of dogs. These results reveal important new information regarding the biology of type IV collagen and the etiology of Alport syndrome with diffuse leiomyomatosis. First, a point mutation in COL4A5 is sufficient to prevent incorporation of the collagen α6(IV) chain into smooth muscle basement membranes, independent of a reduction in α6(IV) mRNA levels. This provides further evidence for requisite coassembly of the α5 and α6(IV) chains, in agreement with the observed absence of α6(IV) from renal and epidermal basement membranes in Alport patients with COL4A5-specific mutations.18Ninomiya Y Kagawa M Iyama K Naito I Kishiro Y Seyer JM Sugimoto M Oohashi T Sado Y Differential expression of two basement membrane collagen genes, COL4A6 and COL4A5, demonstrated by immunofluorescence staining using peptide-specific monoclonal antibodies.J Cell Biol. 1995; 130: 1219-1229Crossref PubMed Scopus (266) Google Scholar, 19Peissel B Gene L Kalluri R Kashtan C Rennke HG Gallo GR Yoshioka K Sun MJ Hudson BG Neilson EG Zhou J Comparative distribution of the α1(IV), α5(IV), and α6(IV) collagen chains in normal human adult and fetal tissues and in kidneys from X-linked Alport syndrome patients.J Clin Invest. 1995; 96: 1948-1957Crossref PubMed Scopus (121) Google Scholar, 25Hino S Takemura T Sado Y Kagawa M Oohashi T Ninomiya Y Yoshioka K Absence of α6(IV) collagen in kidney and skin of X-linked Alport syndrome patients.Pediatr Nephrol. 1996; 10: 742-744Crossref PubMed Scopus (16) Google Scholar However, it contrasts with the transcriptional mechanisms previously proposed as negative regulators of expression of the α3 and α4(IV) chains in COL4A5 mutant dog kidney.14Thorner PS Zheng K Kalluri R Jacobs R Hudson BG Coordinate gene expression of the α3, α4, and α5 chains of collagen type IV: evidence from a canine model of X-linked nephritis with a COL4A5 gene mutation.J Biol Chem. 1996; 271: 13821-13828Abstract Full Text Full Text PDF PubMed Scopus (56) Google Scholar Second, the mere absence of α6(IV) from dog smooth muscle is not sufficient to cause diffuse leiomyomatosis. By analogy, based on these studies of dog, human Alport patients with COL4A5 mutations would lack the α6(IV) chain in smooth muscle, but only those with the additional appropriate COL4A6 deletions would develop leiomyomata. Thus, these deletions are likely affecting something other than expression of α6(IV) and its incorporation into basement membranes. Determining what this something really is will solve an important mystery and could force revisions in our understanding of gene structure, regulation of cell proliferation, and development of tumors and perhaps cancer." @default.
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• W72383048 title "Alport Syndrome with Diffuse Leiomyomatosis" @default.
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• W72383048 cites W1983027730 @default.
• W72383048 cites W1989038991 @default.
• W72383048 cites W1989520310 @default.
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