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  • 1
    Electronic Resource
    Electronic Resource
    Differential distribution and expressions of collagens in the cerebral aneurysmal wall (1997)
    Springer
    Acta neuropathologica 94 (1997), S. 197-206 
    Details
    ISSN: 1432-0533
    Keywords: Key words Cerebral aneurysm ; Immunohistology ; In situ hybridization ; Smooth muscle cells ; Collagen types I ; III ; VI
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract To investigate the role of collagens in the formation and rupture of cerebral aneurysms, we examined the distribution and synthesis of vascular collagens in the wall of normal human cerebral main trunks and of cerebral aneurysms using immunohistochemistry and in situ hybridization techniques. Fifteen cerebral aneurysmal walls were resected at operation; control cerebral main trunks were obtained from seven autopsy cases. Semiserial sections from the specimens were subjected to immunofluorescence and immunohistochemical staining with antibodies to collagen types I, III, IV, V, VI, desmin and α-smooth muscle actin. In addition, type III collagen mRNA was examined by in situ hybridization. Immunohistochemical study showed that all collagen types were grossly preserved in the aneurysmal wall, although the distribution patterns were different for each collagen. The distribution of major fibrillar collagen types I and III was more diffuse and homogeneous in the luminal layer of the aneurysmal wall than the media of the control artery, although the intensity of immunohistochemical staining was weaker in the abluminal layer of the aneurysmal wall than the adventitia of the control artery. Collagen types IV and V were distributed more sparsely in the luminal layer of the aneurysmal wall than the media of the control artery. Collagen type VI was noted in the luminal as well as the abluminal layer of the aneurysmal wall, whereas it was located exclusively in the adventitia of the control artery. In situ hybridization showed that the signal for collagen type III mRNA on fibroblastic and smooth muscle cells was higher in the aneurysmal walls than the control arteries, suggesting up-regulation of type III collagen transcription in the cerebral aneurysmal wall. The study of the distribution and synthetic regulation of various types of collagen in the aneurysmal wall may be essential for understanding the formation of the aneurysmal wall and its protection against enlargement or rupture.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004010050694
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  • 2
    Electronic Resource
    Electronic Resource
    Differential expression of CCAAT enhancer binding protein family in rat alveolar epithelial cell proliferation and in acute lung injury (1999)
    Springer
    Cell & tissue research 297 (1999), S. 261-270 
    Details
    ISSN: 1432-0878
    Keywords: Key words Acute lung injury ; Bleomycin ; CCAAT enhancer binding protein ; Lipopolysaccharide ; Wound healing ; Rat (F 344)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Although alveolar reorganization after acute lung injury depends on regeneration of alveolar epithelial cells, there is little knowledge of regulation of pulmonary healing process. Transcription factors may play key roles in this regulation. To investigate whether the CCAAT enhancer binding protein (C/EBP) family, α, β, and δ, were involved in alveolar reorganization after injury, we examined expression of C/EBP proteins and mRNAs in lung injuries induced by lipopolysaccharide (LPS) or bleomycin (Bleo) and in cell proliferation by keratinocyte growth factor (KGF). By immunohistochemistry, we demonstrated that C/EBPα and C/EBPβ were expressed in alveolar type II cells and alveolar macrophages, but C/EBPδ was expressed restrictedly in some of alveolar type II cells in a spatial pattern in the control lungs. Further, these three C/EBP family members were differentially expressed in alveolar cell proliferation and in acute lung injury, in which, interestingly, C/EBPα and C/EBPδ were reciprocally expressed in alveolar type II cell proliferation and in pulmonary fibrosis. However, expressions of their mRNAs by in situ hybridization were dramatically increased in the affected lesions of the lungs by LPS and Bleo, and Northern blot analysis showed an increased abundance of the mRNA for C/EBPβ in LPS-treated lungs and for C/EBPδ in Bleo-treated lungs, compared with those in the control lungs. Thus, differential expression of the C/EBP family may be required to maintain and reorganize the basic integrity of alveolar structure during pathological states, which suggests an important role for the C/EBP family in maintaining normal alveolar architecture and function and in repairing the damaged epithelium after injury.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004410051354
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  • 3
    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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  • 4
    Electronic Resource
    Electronic Resource
    Immunohistochemical Localization of Arginase II and Other Enzymes of Arginine Metabolism in Rat Kidney and Liver (1998)
    Springer
    Journal of molecular histology 30 (1998), S. 741-751 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Arginine is a precursor for the synthesis of urea, polyamines, creatine phosphate, nitric oxide and proteins. It is synthesized from ornithine by argininosuccinate synthetase and argininosuccinate lyase and is degraded by arginase, which consists of a liver-type (arginase I) and a non-hepatic type (arginase II). Recently, cDNAs for human and rat arginase II have been isolated. In this study, immunocytochemical analysis showed that human arginase II expressed in COS-7 cells was localized in the mitochondria. Arginase II mRNA was abundant in the rat small intestine and kidney. In the kidney, argininosuccinate synthetase and lyase were immunostained in the cortex, intensely in proximal tubules and much less intensely in distal tubules. In contrast, arginase II was stained intensely in the outer stripes of the outer medulla, presumably in the proximal straight tubules, and in a subpopulation of the proximal tubules in the cortex. Immunostaining of serial sections of the kidney showed that argininosuccinate synthetase and arginase II were collocalized in a subpopulation of proximal tubules in the cortex, whereas only the synthetase, but not arginase II, was present in another subpopulation of proximal tubules. In the liver, all the enzymes of the urea cycle, i.e. carbamylphosphate synthetase I, ornithine transcarbamylase, argininosuccinate synthetase and lyase and arginase I, showed similar zonation patterns with staining more intense in periportal hepatocytes than in pericentral hepatocytes, although zonation of ornithine transcarbamylase was much less prominent. The implications of these results are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1003468726969
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  • 5
    Electronic Resource
    Electronic Resource
    Developmental pattern of expression of the mouse α1(XI) collagen gene (Col11a1) (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Developmental Dynamics 204 (1995), S. 41-47 
    Details
    ISSN: 1058-8388
    Keywords: Type XI collagen ; Extracellular matrix ; Gene expression ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Fibrillar networks are intimately involved in several morphogenetic processes which underlie the harmonious development of the vertebrate embryo. Recent genetic evidence has demonstrated that the minor types V and XI collagen are key regulators of types I and II fibrillogenesis in non-cartilaginous and cartilaginous matrices, respectively. A comprehensive understanding of the expression and regulation of the genes coding for the chains of the minor collagen types is therefore relevant to animal morphogenesis and development. The present study was undertaken to elucidate the embryonic pattern of expression of the gene coding for the mouse α1 chain of type XI colagen (Col11α1) using the technique of in situ hybridization. Transcripts of the Col11α1 gene were detected as early as 11 days of gestation. The α1(XI) transcripts were found to accumulate mostly in cartilaginous tissues, such as the chondrocranium and the developing limbs. Like the major cartilage-specific collagen (type II), Col11α1 expression was also noted in the neuro-epithelium of the brain. However, α1(XI) transcripts accumulated in several other non-cartilaginous sites. They include odontoblasts, trabecular bones, atrioventricular valve of the heart, the tongue, the intestine, and the otic vesicle. Altogether, the data confirm that Col11α1 has a broader spectrum of expression than previously thought. This finding raises the possibility that the α1(XI) chain may participate in the formation of stage- and tissue-specific trimers with distinct functional properties. © 1995 wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aja.1002040106
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