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  • 1985-1989  (31)
  • 1960-1964  (3)
  • Life and Medical Sciences  (31)
  • Genetics  (4)
  • α-l-fucosidase  (3)
  • 1
    ISSN: 1573-4927
    Keywords: α-l-fucosidase ; lymphoid cells ; fucosidosis ; serum polymorphism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract In humans, the quantity of α-l-fucosidase in serum is determined by heredity. The mechanism controlling levels of the enzyme in serum is unknown. Lymphoid cell lines derived from individuals with either low, intermediate, or high α-l-fucosidase in serum were established. Steady-state levels of intracellular and extracellular α-l-fucosidase as well as rates of synthesis and secretion of enzyme overlapped among the cell lines. Thus,vivo} serum phenotypes were not expressed in this system. No appreciable differences in the qualitative processing of newly made α-l-fucosidase were observed among these lymphoid cell lines. Cells pulse-labeled with35S-methionine from 0.25 to 2 hr had an intracellular form of enzyme with aM r=58,000. Cells pulsed for 1.5 hr and chased for 21 hr with unlabeled methionine had an intracellular form ofM r=60,000 and an extracellular form ofM r=62,000. All three enzyme forms were glycoproteins with a common polypeptide chain ofM r=52,000 but with different carbohydrate moieties. No evidence for a high molecular mass precursor form of α-l-fucosidase was found. Fucosidosis is a rare, inherited disease in which α-l-fucosidase activity in tissues and body fluids is low or absent. The mutations for fucosidosis and the serum polymorphism map separately. Lymphoid cells from two siblings with fucosidosis had 8-fold to 341-fold less intracellular α-l-fucosidase protein with 11-fold to 56-fold lower specific activities than control cells. Residual mutant enzyme was a glycoprotein with a polypeptide chain virtually the same size (M r=52,000) as control enzyme. However, residual mutant enzyme was hypoglycosylated and hypersecreted as compared to control enzyme.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-4927
    Keywords: α-l-fucosidase ; lymphoid cells ; fucosidosis ; serum polymorphism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract In humans, the quantity of α-l-fucosidase in serum is determined by heredity. The mechanism controlling levels of the enzyme in serum is unknown. Lymphoid cell lines derived from individuals with either low, intermediate, or high α-l-fucosidase in serum were established. Steady-state levels of intracellular and extracellular α-l-fucosidase as well as rates of synthesis and secretion of enzyme overlapped among the cell lines. Thus,vivo} serum phenotypes were not expressed in this system. No appreciable differences in the qualitative processing of newly made α-l-fucosidase were observed among these lymphoid cell lines. Cells pulse-labeled with35S-methionine from 0.25 to 2 hr had an intracellular form of enzyme with aM r=58,000. Cells pulsed for 1.5 hr and chased for 21 hr with unlabeled methionine had an intracellular form ofM r=60,000 and an extracellular form ofM r=62,000. All three enzyme forms were glycoproteins with a common polypeptide chain ofM r=52,000 but with different carbohydrate moieties. No evidence for a high molecular mass precursor form of α-l-fucosidase was found. Fucosidosis is a rare, inherited disease in which α-l-fucosidase activity in tissues and body fluids is low or absent. The mutations for fucosidosis and the serum polymorphism map separately. Lymphoid cells from two siblings with fucosidosis had 8-fold to 341-fold less intracellular α-l-fucosidase protein with 11-fold to 56-fold lower specific activities than control cells. Residual mutant enzyme was a glycoprotein with a polypeptide chain virtually the same size (M r=52,000) as control enzyme. However, residual mutant enzyme was hypoglycosylated and hypersecreted as compared to control enzyme.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-4927
    Keywords: specific activity ; α-l-fucosidase ; serum polymorphism ; fucosidosis ; enzyme-linked immunoabsorbent assay (ELISA)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The quantity of α-l-fucosidase activity in human serum is determined by heredity. An individual may inherit either low, intermediate, or high serum enzyme activity. An enzyme-linked immunoabsorbent assay has been developed that can detect 0.3 ng of α-l-fucosidase protein. Enzyme protein in serum of 102 individuals ranged from 20 to 835 ng/ml. The group included individuals with low, intermediate, and high enzyme activity. The specific activity of α-l-fucosidase within this group was statistically the same (mean±SD=11,002±1051 U/mg). Thus, individuals with low and intermediate enzyme activity in serum had lower amounts of enzyme protein with the same specific activity as in individuals with high enzyme activity. Fucosidosis is a rare inherited disease in which α-l-fucosidase activity in tissues and body fluids is low or absent. The concentrations of enzyme protein in sera of a fucosidosis patient and parents were 76, 565, and 604 ng/ml, respectively, and the specific activities of enzyme were 1316, 8938, and 8858 U/mg, respectively. Thus, the fucosidosis serum probably contained a structurally altered enzyme with reduced catalytic activity. The somewhat low specific activities in the parents suggested that their sera contained both structurally altered and normal protein.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Journal of Morphology 188 (1986), S. 15-28 
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Egg capsules of Syndisyrinx franciscanus, an intestinal parasite of sea urchins (Strongylocentrotus spp.), consist of a bulb, which contains the embryos, and a stalk-like filament. The wall of the bulb is about 12 μm thick and is composed of sclerotized proteins. The end of the bulb opposite the attachment of the filament bears a reticulum of hatching sutures. Transmission electron microscopy discloses that hatching sutures traverse the entire thickness of the capsule wall. The inner 9-10 μm of sutures are a uniform 20 nm in width and contain a trilaminar cementum. The outer 2-3 μm of sutures are 15 nm to more than 500 nm in width and contain an electron-lucent cementum. The latter may contain an irregular, median, electron-dense layer or, more commonly, electron-dense granules. The outside of some capsules is partially covered by a thin, electron-dense material.A previous study showed that sutures in intact capsules of Syndisyrinx franciscanus are not affected by host digestive fluids, but are severely weakened immediately prior to hatching owing to activities of the embryos. The hypothesis that the embryos secrete a hatching enzyme is supported by findings that sutures of intact capsules are not affected by externally applied trypsin, but become weakened when capsules are cut open and then incubated in trypsin. Scanning electron microscopy reveals that the outer parts of sutures often remain intact after hatching. We hypothesize that the ability of sutures to resist enzymatic attack from the outside, but not the inside, results from differences in the chemical properties of the cementums in outer and inner parts of sutures.
    Additional Material: 23 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Journal of Morphology 191 (1987), S. 131-144 
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Xenopus laevis froglet forelimbs normally respond to amputational injury by forming a heteromorphic cartilaginous rod-shaped outgrowth. However, partial denervation of a forelimb by ablation of the N. radialis or the N. ulnaris, followed in 2 days by amputation through the mid radius-ulna, results in a size deficiency of the regenerative outgrowth 14 and 21 days postamputation. The decreasing quantity of forelimb innervation, as a result of partial denervation by 55 or 45%, apparently has a graded effect on the cell population and on the extent of cartilage development in the outgrowth. As a consequence of amputational injury, a nerve independent response of the periosteum was also found. This response produced considerable thickening in the periosteum and was due to cell proliferation in both the control and denervated cases.
    Additional Material: 17 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 37 (1988), S. 269-284 
    ISSN: 0730-2312
    Keywords: membrane skeleton ; nonerythroid protein 4.1 homologues immunoreative isoforms ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Analogues of the human erythroid membrane skeletal component protein 4.1 have been identified in perfused rat tissues and human T and B lymphocyte cell lines, olyclonal antibodies were used which are specific for all domains of protein 4.1, the spectrin-actin-promoting 8-Kd peptide, the membrane-binding 30-Kd domain, and the 50-Kd domain. Antibody reactivity, by Western blotting of tissue homogenates, shows reactivity with proteins varying in molecular weight from 175 Kd to 30 Kd. Further, these protein 4.1 analogues appear to be expressed in a tissue-specific fashion. Of the analogues detected there appear to be at least three classes: analogues containing all erythroid protein 4.1 domains, analogues containing all domains but with modified antigenic epitopes, and analogues containing only some domains. Chemical cleavage at cysteine linkages indicates that in analogues containing the 30-Kd region the location of cysteine is highly conserved. This datum suggests that in nonerythroid 4.1 isoforms of higher molecular weight the additional protein mass is added to the amino terminal end (30 Kd end).
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 40 (1989), S. 133-145 
    ISSN: 0730-2312
    Keywords: calcium-binding ; cDNA sequence ; PKC substrate ; phosphorylation ; P47 ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Activation of protein kinase C (PKC) in platelets causes the immediate phosphorylation of pleckstrin, an apparent Mr 40-47,000 protein previously called 40K or P47. Pleckstrin presumably plays an important but as yet unknown role in mediating cellular responses evoked by agonist-induced phosphoinositide turnover. We have cloned the cDNA for pleckstrin from the HL-60 human promyelocytic leukemia cell line by immunological screening of a λgt11 expression library (Tyers et al.: Nature 333:470-473, 1988) and now report further analysis of the pleckstrin sequence. Pleckstrin has a deduced Mr of 40,087 and is encoded by a 1,050-bp open reading frame which is preceded by a short open reading frame that terminates before the correct initiator methionine. A single polymorphic site was found in the coding region. An unusual pattern of sequence heterogeneity occurred about a poly(A) tract in the 3′ untranslated region. The 3.0-kb pleckstrin mRNA induced upon differentiation of HL-60 cells apparently has heterogeneous 5′ ends which undergo differential regulation during HL-60 cell maturation. Analysis by multiple sequence alignment with known PKC substrates identified a strong candidate site for phosphorylation by PKC and a potential Ca2+-binding EF-hand motif. No other similarities to proteins in current databases were found.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 214 (1986), S. 289-293 
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Left forelimbs of postmetamorphic Xenopus laevis froglets were repeatedly denervated prior to and following amputation. Amputations were performed 14, 21, 28, or 42 days after the original denervation. A tissue-regenerative response resulting in the formation of a spike-shaped, heteromorphic outgrowth was found in the sham-denervated and control animals, but dedifferentiation of the stump tissues was not apparent. Tissue-regenerative outgrowths were not observed in the denervated cases; instead, dermal wound healing and stump and scar formation occurred. In both control and experimental cases, however, a periosteal proliferative response to amputation injury led to the development of a greatly thickened periosteum the length of the amputated radius-ulna as well as a cap of cartilage at the distal end of these bones. We conclude from these results that forelimbs of postmetamorphic froglets are incapable of adjusting to a prolonged nerveless state sufficient to allow the normal tissue-regenerative response of spike outgrowth formation.
    Additional Material: 6 Ill.
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 222 (1988), S. 95-102 
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: By dissection of thiocholine-stained orbital preparations, it has been determined that three different nerve pathways link the pterygopalatine ganglion and the eye in cats. (1) Nerves from the proximal half of the ganglion join a plexus of nerves and ganglion cells in the rete mirabile of the maxillary artery. Branches of the internal carotid nerve also supply this plexus. Fine nerves from the plexus travel to the optic nerve and then to the eye, accompanying both the nasociliary nerve that passes through the rete and the ciliary arteries that arise from the rete. (2) One or more nerves from the nerve of the pterygoid canal and from a prominent accessory ganglion near the orbital apex course to the inferior optic nerve surface at the optic foramen; these then run distally along the optic nerve to fuse with ciliary nerves or to accompany ciliary arteries entering the eye. (3) Other nerves from the pterygopalatine ganglion travel medially around the extraocular muscle cone to join the ethmoidal and infratrochlear branches of the nasociliary nerve; some nerves from the ganglion then take a retrograde course to the optic nerve, where they join ciliary nerves or arteries to the eye. All three pathways may transmit sympathetic, parasympathetic and somatic sensory nerve fibers.
    Additional Material: 9 Ill.
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  • 10
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
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