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  • 1
    Keywords: Human Physiology ; Human physiology ; Biochemistry ; Medical biochemistry. ; Brain Diseases, Metabolic, Inborn pathology ; Genetic Diseases, Inborn pathology ; Biochemical Phenomena ; Case Reports
    Description / Table of Contents: Part 1 Metabolic Disorders. Citrin deficiency” -- Homocystinuria No Acquaintance -- Phenylketonuria -- Urea cycle disorders (such as defects of OTCD)” -- Wilson disease -- Diabetes Mellitus type I -- Lipid storage disorder, namely Niemann-Pick C1 disease -- Gaucher disease -- Fabry disease -- Mitochondrial disease (such as defects of MELAS) -- Heme oxygenase deficiency -- Collagen metabolism (such as OI) -- Organic acid metabolism disorders -- Part 2 Genetic Disorders. Glucose 6-Phosphate Dehydrogenase Deficiency -- Familial Hypercholesterolemia -- Fukuyama muscular dystrophy -- Hemoglobin -- Huntington disease -- Anti-coagulant deficiency -- Auto-inflammatory disorders -- Cancer -- Marfan syndrome -- Human immunodeficiency virus infection -- Hepatitis virus C -- Cytomegalovirus infection (especially congenital infection) -- Addiction
    Type of Medium: Online Resource
    Pages: 1 Online-Ressource (XI, 349 p. 167 illus., 113 illus. in color)
    ISBN: 9789811329777
    Series Statement: Springer eBooks
    Language: English
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  • 2
    ISSN: 1546-1718
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] X-linked lymphoproliferative syndrome (XLP or Duncan disease) is characterized by extreme sensitivity to Epstein-Barr virus (EBV), resulting in a complex phenotype manifested by severe or fatal infectious mononucleosis, acquired hypogammaglobulinemia and malignant lymphoma. We have identified a ...
    Type of Medium: Electronic Resource
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  • 3
    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
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  • 4
    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
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  • 5
    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
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  • 6
    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
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