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  • 1
    Electronic Resource
    Electronic Resource
    Distribution of basement membrane type IV collagen α chains in ameloblastoma: an immunofluorescence study (2002)
    Oxford, UK : Munksgaard International Publishers
    Journal of oral pathology & medicine 31 (2002), S. 0 
    Details
    ISSN: 1600-0714
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Background:  Type IV collagen, a heterotrimeric molecule that exists in six genetically distinct forms, α1(IV)–α6(IV) is a major structural component of basement membrane (BM) and acts as a scaffold for other BM constituents.Methods:  Indirect immunofluorescence using α chain-specific monoclonal antibodies was employed to clarify basement membrane (BM) collagen IV distribution in two ameloblastoma, and for comparison, on oral mucosa and tooth germ.Results:  Ameloblastoma BM expressed five of six genetically distinct forms of collagen IV: α1(IV), α2(IV), α5(IV) and α6(IV) chains occurred as intense linear stainings without disruption around neoplastic epithelium, and this expression pattern was fundamentally similar to oral mucosa BM; α4(IV) expression was rare and occurred around nests of primitive tumor cells or potentially invasive sites. The tooth germ demonstrated a stage- and position-specific collagen IV distribution: the inner enamel epithelium BM expressed α1(IV), α2(IV), and α4(IV) except in the cuspal predentine region; and the outer enamel epithelium BM expressed α1(IV), α2(IV), α5(IV), and α6(IV) chains.Conclusions:  Results suggest that collagen IV α chain distribution in ameloblastoma BM plays an important role in tumor cytodifferentiation and progression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1600-0714.2002.00162.x
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  • 2
    Electronic Resource
    Electronic Resource
    Glomerular basement membrane type IV collagen antigens in Goodpasture's and Alport's syndromes (1998)
    Springer
    Clinical and experimental nephrology 2 (1998), S. 282-288 
    Details
    ISSN: 1437-7799
    Keywords: type IV collagen ; Goodpasture's syndrome ; Alport's syndrome ; glomerular basement membrane ; immunohistochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Type IV collagen, the main constituent of the renal glomerular basement membrane, is involved in Goodpasture's syndrome, and autoimmune disease, and in Alport's syndrome, a genetic disease. There are 6 alpha chains, α1(IV) through α6(IV), in type IV collagen in mammals. Immunohistochemical studies, using α-chain-specific monoclonal antibodies on tissue specimens from healthy people and patients with Alport's syndrome, have shown that there are 3 forms of type IV collagen molecules in mammalian basement membranes, namely α1/α1/α2, α3/α4/α5, and α5/α5/α6. Antibody specificity analysis of sera from patients with Goodpasture's syndrome show that all sera have autoantibody, with the highest titer against α3(IV)NC1, although they also have titers against the other 5α chains. This indicates that α3(IV)NC1 is the major target antigen of the disease, although the glomerular basement membrane contains the α1 through α5 chains. Experimental glomerulonephritis in rats, induced by the injection of 6 recombinant α(IV)NC1s with an adjuvant, has shown that α3(IV)NC1 and α4(IV)NC1 are nephritogenic. The lack of, or very poor, nephritogenicity of the other 4 α(IV)NC1s can be explained by the high immunologic tolerance against these chains, which are distributed widely in basement membranes of the whole body.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02480455
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  • 3
    Electronic Resource
    Electronic Resource
    Renal distribution of collagen type IV α chains in autosomal-dominant Alport syndrome (1998)
    Springer
    Clinical and experimental nephrology 2 (1998), S. 58-63 
    Details
    ISSN: 1437-7799
    Keywords: Alport syndrome ; type IV collagen ; hereditary nephritis ; immunohistochemistry ; monoclonal antibody ; antigen retrieval
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Background Autosomal-dominant Alport syndrome is a recognized, but relatively uncommon, form of Alport syndrome. Recently, mutations in theCOL4A3 andCOL4A4 genes, which encode collagen type IV α3 and α4 chains, respectively, have been shown to cause the disease. However, the distribution of α(IV) chains has yet to be determined. Methods To clarify the renal distribution of α(IV) chains, immunohistochemistry of α1(IV) to α6(IV) chains was performed, using chain-specific monoclonal antibodies, raised by us, and an antigen retrieval procedure. Paraffin-embedded renal sections, obtained from 8 patients from 3 families with the disease, were examined. Results The distribution of all 6 α(IV) chains was not significantly different between the 8 patients and the controls. Collagen type IV α1 and α2 chains were ubiquitously expressed, while α3 to α6 chains were detected in the basement membranes of the glomerulus and Bowman's capsule, and/or part of the tubular basement membranes. Conclusions Our findings contrast with those of X-linked and autosomal-recessive Alport syndrome. The distribution pattern of α(IV) chains may provide a useful means of distinguishing the different forms of Alport syndrome.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02480625
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  • 4
    Electronic Resource
    Electronic Resource
    Diffuse mesangial sclerosis associated with Kawasaki disease: an analysis of alpha chains (α1–α6) of human type IV collagen in the renal basement membrane (1997)
    Springer
    Virchows Archiv 430 (1997), S. 489-494 
    Details
    ISSN: 1432-2307
    Keywords: Key words Infantile nephrotic syndrome ; Diffuse mesangial sclerosis ; Kawasaki disease ; Type IV collagen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  A case of diffuse mesangial sclerosis (DMS) associated with Kawasaki disease is reported. A previously healthy Japanese girl, aged 4 months, presented with clinical features of Kawasaki disease. At week 10 of the illness, she developed the nephrotic syndrome, which was refractory to steroid therapy. Renal biopsy demonstrated a diffuse mesangial proliferative glomerulonephritis with microcystic tubular dilatation and, ultrastructurally, marked thinning of the lamina densa in the glomerular basement membrane (GBM) and the tubular basement membrane (TBM) of the proximal tubule. She went into chronic renal failure and died at the age of 11 months. At autopsy, the kidney revealed DMS. Histologically, we found Finnish microcystic disease in its early stages in the biopsy. Using a newly developed monoclonal antibody, we analysed the alpha chains (α1–α6) of type IV collagen in the GBM and TBM. There was no defective constitution of alpha chains on the thin GBM, but the thin TBM of the microcystic proximal tubule showed a weak or discontinuous reactivity for α1 and α2 chains, suggesting faulty formation of the basement membrane. The sclerosing glomeruli of the DMS did not depend on collapse of the GBM, which was positive for α3–α5 chains, but mainly on the proliferation of mesangial matrix, which was positive for α1 and α2 chains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004280050059
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  • 5
    Electronic Resource
    Electronic Resource
    Establishment by the rat lymph node method of epitope-defined monoclonal antibodies recognizing the six different α chains of human type IV collagen (1995)
    Springer
    Histochemistry and cell biology 104 (1995), S. 267-275 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract A group of rat monoclonal antibodies recognizing the six different α chains of human type IV collagen have been established by our novel method. The method is designated the rat lymph node method in which enlarged medial iliac lymph nodes of a rat injected with an antigen emulsion via hind footpads are used as a source of B cells for cell fusion to produce hybridomas. The immunogens used were synthetic peptides having non-consensus amino acid sequences near the carboxyl termini of type IV collagen α chains. Hybridomas were screened both by ELISA with synthetic peptides and by indirect immunofluorescence with cryostat sections of human kidneys. Because the epitopes of all antibodies were determined by multipin-peptide scanning, they were confirmed to be isoform-specific. They are useful for identification of α chains of type IV collagen at the protein level in normal and abnormal conditions. The combined use of synthetic peptides as immunogens, the rat lymph node method as making monoclonal antibodies, and the multipin-peptide scanning as epitope mapping is found to be a strong tool for identification of peptides and proteins whose amino acid sequences are known or have been deduced.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01464322
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  • 6
    Electronic Resource
    Electronic Resource
    Differential expression of type IV collagen isoforms, α5(IV) and α6(IV) chains, in basement membranes surrounding smooth muscle cells (1998)
    Springer
    Histochemistry and cell biology 110 (1998), S. 359-366 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Smooth muscle is composed of cigar-shaped, non-striated cells, each of which is encapsulated by a basement membrane and forms the contractile portion of tubular organs such as the gastrointestinal tract, pulmonary tract, genitourinary tract, and vasculature, in which slow and sustained contractions are needed. We examined basement membranes produced by smooth muscle cells and, using α(IV) chain-specific monoclonal antibodies, analyzed type IV collagens in these organs. Detailed distribution analysis of the α chains in normal and Alport cases by use of specific antibodies indicated that there are at least three molecular forms of type IV collagen, [α1(IV)]2α2(IV), α3(IV)α4(IV)α5(IV), and α5(IV)/α6(IV). Smooth muscle cells in the urinary bladder and uterus were enclosed by basement membranes composed of α1, α2, α5, and α6 chains. The same α chains were present around smooth muscle cells in the muscular layer of the fundus of the stomach, whereas those in the antrum and further distal side of the gastrointestinal tract expressed mostly α1 and α2 chains. In addition, immunostaining analysis of the vasculature also showed that most of the smooth muscle cells were positive for α1 and α2 chains; however, α5 and α6 chains were also expressed by smooth muscle cells in the aorta and some arteries where blood pressure changes significantly. These results suggest that the smooth muscle cells enclosed by α5/α6-containing basement membranes might have some particular function related to mechanical stress or tensile strength during the characteristic contractile activity of tubular organs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180050296
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  • 7
    Electronic Resource
    Electronic Resource
    Expression of type IV collagen in the developing human kidney (1998)
    Springer
    Pediatric nephrology 12 (1998), S. 554-558 
    Details
    ISSN: 1432-198X
    Keywords: Key words: Type IV collagen ; α6 Chain ; Human renal development ; Glomerular basement membrane ; Transient expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract. The distribution of α1–6 chains of type IV collagen (α1–6(IV)) in human fetal kidneys was examined by indirect immunofluorescence. By 11 weeks of gestation, α1, 2, 3, 4, and 6(IV) were already present, but α5(IV) appeared relatively late, at 21 weeks. α1(IV) and α2(IV) were present in all basement membranes, α3(IV) and α4(IV) were restricted to the glomerular basement membrane and parts of the tubular basement membrane. α5(IV) was distributed in the glomerular basement membrane, Bowman’s capsule, and parts of the tubular basement membrane. α6(IV) was present in the Bowman’s capsule, parts of the tubular basement membrane, and occurred in parts of the glomerular basement membrane at the early capillary loop stage, but disappeared during the later capillary loop stage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004670050503
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  • 8
    Electronic Resource
    Electronic Resource
    Absence of α6(IV) collagen in kidney and skin of X-linked Alport syndrome patients (1996)
    Springer
    Pediatric nephrology 10 (1996), S. 742-744 
    Details
    ISSN: 1432-198X
    Keywords: Key words: Alport syndrome   ;   Type IV collagen   ;   Basement membrane
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Ab stract. To identify the abnormalities of the type IV collagen α6 chain, α6(IV), in Alport syndrome, we examined renal and skin tissue using rat monoclonal antibodies against non-consensus amino acid sequences of α6(IV). Immunofluorescence of normal human kidney and skin tissue revealed linear α6(IV) staining in the basement membrane (BM) of Bowman’s capsule, in some tubules, and also in the epidermal BM. Renal specimens from five male patients of four families with X-linked Alport syndrome showed no reactivity for α6(IV) in Bowman’s capsules and tubules. In these patients, α1(IV) and α2(IV) were normal, whereas α3(IV), α4(IV), and α5(IV) were absent from the BMs of the kidney. In skin tissue of male patients, neither α5(IV) nor α6(IV) were detected. The epidermal BM of female heterozygotes with X-linked Alport syndrome showed a mosaic staining for α5(IV) and α6(IV). These findings indicate that, in addition to a disturbed α3(IV)-α4(IV)-α5(IV) network, patients with X-linked Alport syndrome have abnormalities in α6(IV) of the renal and epidermal BMs at the protein level.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004670050206
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  • 9
    Electronic Resource
    Electronic Resource
    Immunohistochemical localization of glomerular basement membrane antigens in various renal diseases (1986)
    Springer
    Virchows Archiv 408 (1986), S. 403-419 
    Details
    ISSN: 1432-2307
    Keywords: GBM antigens ; Renal diseases ; Immunohistochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The immunofluorescent localization of glomerular basement membrane (GBM) antigens was examined in 52 specimens from normal kidneys and in various renal diseases using antisera to human GBM HGBM), IV type collagen (IV Col) and P3 antigen, a rat nephritogen. Anti-HGBM serum normally stained the GBM and the mesangium in a restrictive pattern, anti-IV Col serum stained the GBM and the mesangium in a wider pattern and anti-P3 serum stained only the GBM. In mesangial proliferative glomerulonephritis, including IgA nephropathy pathy and Henoch-Schönlein nephritis, the widened mesangial areas were stained with anti-HGBM and anti-IV Col sera. In membranous nephropathy, the punched-out lesions of thickened GBM were demonstrated with the three antisera in moderate cases and a double linear distribution with fine granulation with anti-HGBM and anti-IV Col sera were revealed in one severe case. In membranoproliferative glomerulonephritis, the expanded mesangium and thickened capillary walls were stained with anti-HGBM and anti-IV Col sera, while the outer line of glomerular capillary walls was only positive with anti-P3 serum. In crescentic glomerulonephritis, the collapsed glomerular tufts were stained normally with anti-HGBM and anti-P3 sera and weakly with anti-IV Col serum. In diabetic nephropathy, anti-HGBM serum stained the GBM in a double linear distribution without reacting with the expanded mesangium; anti-IV Col serum stained the mesangium and the GBM in a less clear double linear fashion while anti-P3 serum stained the GBM as single line. Thin membrane disease and Alport's syndrome had normal reactivity with all antisera. However, in one case of Alport's syndrome anti-HGBM and anti-P3 sera stained the GBM in a focal and segmental pattern, while normal staining with anti-IV Col serum was found. In lesions with adhesions and crescents the staining was positive for HGBM and IV Col and negative for P3; obsolescent glomeruli were stained with anti-HGBM and anti-P3 sera, and had diminished staining with anti-IV Col serum. The identification of the various structural glomerular antigens is useful in the classification of certain types of glomerular diseases. Further insight into the mechanisms underlying these conditions may be obtained in this way.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00707698
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  • 10
    Electronic Resource
    Electronic Resource
    Differential expression of α1(IV), α2(IV), α5(IV) and α6(IV) collagen chains in the basement membrane of basal cell carcinoma (1997)
    Springer
    Journal of molecular histology 29 (1997), S. 563-570 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Type IV collagen, the major component of basement membrane, consists primarily of α1(IV) and α2(IV) chains. Recently, other types of collagen IV chains, i.e. α3(IV), α4(IV), α5(IV) and α6(IV) chains, have been identified by protein chemistry and molecular cloning. We have examined the diversity of the assembly of α(IV) chains of the basement membrane surrounding tumour nests of basal cell carcinomas, in tissues from 11 patients, by immunohistochemical analysis using specific monoclonal antibodies to six α(IV) chain. The immunostaining profile of each chain differed with respect to the histological subtypes of basal cell carcinoma. In the morphea-like subtype, which was more invasive, α1(IV) and α2(IV) chains were discontinuously stained, and α5(IV) and α6(IV) chains were entirely absent. However, in the superficial subtype, which was non-aggressive, α1(IV), α2(IV), α5(IV) and α6(IV) chains were well stained compared with the other subtypes of basal cell carcinoma. In addition, in the solid subtype, which showed slow growth and ulceration, α1(IV) and α2(IV) chains were continuously stained, and α5(IV) and α6(IV) chains were discontinuous or absent. The assembly of α5(IV) and α6(IV) chains into the basement membrane was inhibited in the solid and morphea subtypes of BCC. This differential expression of type IV collagen chains seems to be associated with the invasive potential of basal cell carcinoma
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026428010104
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