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  • 1
    Electronic Resource
    Electronic Resource
    Photoaffinity labeling of the DDT1 MF-2 cell α1-adrenergic receptor (1985)
    Springer
    Molecular and cellular biochemistry 67 (1985), S. 47-53 
    Details
    ISSN: 1573-4919
    Keywords: α1-adrenergic receptor ; membrane ; photoaffinity ; smooth muscle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary In this study, we have used an α1-adrenergic receptor photoaffinity ligand, 2-[4-(4-azido-3-iodo-benzoyl)-piperazin-1-yl]-4-amino-6, 7-dimethoxyquinazoline (125I-APD), to label covalently the α1-adrenergic receptor in a smooth muscle cell line. Our results indicate that in the absence of light, (125I)APD binds reversibly to a site in the DDT1 MF-2 cell membranes having pharmacological characteristics of an α1-adrenergic receptor. Following incorporation of (125I)ADP into partially purified membranes a single labeled band of protein with a Mr of 81 000 was visualized by autoradiography following sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Incorporation of (125I)-APD into this band was affected by adrenergic agonists and antagonists in a manner consistent with an α1-adrenergic interaction. Prazosin (α1-selective) blocked incorporation of the label into the Mr = 81 000 protein while yohimbine (α2-selective) did not. Of the adrenergic agonists, (−)-epinephrine and (−)-norepinephrine but not (−)-isoproterenol blocked labeling of the Mr − 81 000 protein. We conclude that the ligand binding site of the DDT1 MF-2 cell α1-adrenergic receptor resides in a Mr = 81 000 protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00220985
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  • 2
    Electronic Resource
    Electronic Resource
    Glucocorticoid induction of β-adrenergic receptors in the DDT1 MF-2 smooth muscle cell line involves synthesis of new receptor (1987)
    Springer
    Molecular and cellular biochemistry 74 (1987), S. 21-27 
    Details
    ISSN: 1573-4919
    Keywords: glucocorticoid receptor ; β-adrenergic receptor regulation ; smooth muscle ; adenylate cyclase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract We have shown that glucocorticoids induce the appearance of β2-adrenergic receptors in membranes of the ductus deferens smooth muscle cell line (DDT1 MF-2). A concomitant increase in isoproterenol stimulated adenylate cyclase activity in the absence of exogenously applied GTP was observed as was a significantly increased (p 〈 0.05) sensitivity of the adenylate cyclase system to exogenously applied GTP. However, no significant difference in the maximal velocity of adenylate cyclase between control and steroid treatment was measurable in the presence of sodium fluoride. Induction of β2-adrenergic receptors in DDT1 MF-2 cells is correlated with the presence of steroid receptors (androgen and glucocorticoid) in the cells since estrogens and progesterones had no effect on receptor levels. Finally, utilizing dense amino acid labeling of cells to measure old versus newly synthesized receptor sites by a density shift method, we have documented that glucocorticoid induction of β2-adrenergic receptors involves synthesis of new receptor protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00221909
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  • 3
    Electronic Resource
    Electronic Resource
    Mitotic activity in the hemopoietic cortical zone of the liver of urodele larvaeSupported by Research grant no. 8147 from the U.S.P.H.S., N.I.H. (1964)
    New York, NY : Wiley-Blackwell
    Journal of Morphology 114 (1964), S. 361-371 
    Details
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmor.1051140211
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  • 4
    Electronic Resource
    Electronic Resource
    Morphological basis of the feeding mechanics in the shingle-back lizard Trachydosaurus rugosus (Scincidae, Reptilia) (1984)
    New York, NY : Wiley-Blackwell
    Journal of Morphology 181 (1984), S. 271-295 
    Details
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: This report details certain morphological aspects of the feeding system of the lizard Trachydosaurus rugosus, an opportunistic omnivore, as a first step toward a functional characterization of its masticatory system. The skull is relatively solid and internally well braced; its anterodorsal elements are tightly tied to the integument and covering osteoderms. There is potential for intracranial kinesis and streptostyly. At small gapes, mandibular movements seem to be restricted to relatively simple, hingelike actions by a series of mechanical stops. The dentition features a progression of smaller to larger teeth posteriorly along the tooth row. The jaw adductor musculature is massive; other jaw muscles are relatively simple. The external adductor mass is particularly noteworthy in that it is subdivided into four mechanical units by a complex internal tendon tract (the coronoid aponeurosis). The internal adductor is composed of two separate gross muscles, pseudotemporalis (PST) and pterygoideus (PT). Each of these is subdivided into two main units by aponeurotic sheets, the PST by parts of the coronoid aponeurosis and the PT by a separate series. The form of the aponeurotic system in Trachydosaurus confounds the separation and identification of the adductor muscles and their component parts along the lines of traditional nomenclature, and underscores the need for separating criteria based on homology from those reflecting morphological and possibly functional divisions.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmor.1051810303
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  • 5
    Electronic Resource
    Electronic Resource
    Facial morphology and vibrissal movement in the golden hamster (1985)
    New York, NY : Wiley-Blackwell
    Journal of Morphology 183 (1985), S. 199-217 
    Details
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The major cranial vibrissae in the golden hamster can be moved in complex ways that suggest they are served by a finely controlled motor system. Movements are hypothesized to be the products of (1) differential blood flow and pressure regulation in the sinus surrounding each vibrissal follicle, (2) contractions of the striated facial muscles, and (3) elastic rebound in the connective tissues. The vasculature contributes hydrostatic forces that (a) erect the vibrissae slightly and distort their connective tissue bedding, (b) rigidify the vibrissal capsules, thus forming firm bases of attachment for certain facial muscles, and (c) theoretically provide a pressure plate around the follicle, important in lowering the firing thresholds of receptor endings. The facial muscles supply the major forces in erection and protraction of the vibrissae by acting on both the capsules and the connective tissue bedding. The connective tissues are organized into capsular and extracapsular systems that serve to stabilize the vibrissae and return them to initial rest positions.The slight movements of the genal vibrissa are the effects of vascular and connective tissue dynamics, the musculature being uninvolved. Wide angle movements of the supraorbital vibrissae are products of the vasculature and connective tissues, plus contractions of the Mm. orbicularis oculi and frontalis. Mystacial vibrissal movement is quite complex. The vasculature supplies a small degree of capsular erection and mystacial pad distortion, but primarily rigidifies the capsules. The bulk of erection and protraction is produced by the M. nasolabialis profundus (NLP) and the vibrissal capsular muscles (VCM). The NLP distorts the mystacial pad; the VCM tilt the capsules relative to the pad. Retraction is mainly accomplished by elastic rebound in the pad, this being aided in its extreme degrees by the Mm. nasolabialis and maxillolabialis. The Mm. nasolabialis superficialis and buccinator pars orbicularis oris help to spread the vibrissae into a dorsoventral fan and stabilize the mystacial pad during whisking.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmor.1051830208
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  • 6
    Electronic Resource
    Electronic Resource
    Differential induction of glucose-regulated and heat shock proteins: Effects of pH and sulfhydryl-reducing agents on chicken embryo cells (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 125 (1985), S. 251-258 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Glucose-regulated and heat shock proteins are two subsets of eukaryotic stress proteins that can be induced differentially, simultaneously, and reciprocally. Two new inducers, low extracellular pH and 2-mercaptoethanol, that stimulate chicken embryo cells to synthesize glucose-regulated proteins rapidly were found. Two classes of cellular targets for mercaptoethanol were defined operationally, one dependent on and the other independent of protein synthesis. A new inducer of heat shock proteins, high extracellular pH, was found as well. Inductions by low and high extracellular pH were inhibited by actinomycin D but were insensitive to cycloheximide. Inductions of glucose-regulated and heat shock proteins are discussed in terms of changes in intracellular pH and sulfhydryl oxidation states.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041250212
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  • 7
    Electronic Resource
    Electronic Resource
    Phosphorylation of the T cell antigen receptor: Multiple signal transduction pathways (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 133 (1987), S. 49-51 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: In our previous description of the murine T cell antigen receptor complex (Samelson et al., 1985a), we demonstrated that the clonotypic α-β heterodimer is associated with four additional polypeptides. These include the 26 kd δ chain, the 25 kd ε chain, a 21 kd glycoprotein probably homologous with the human T3 γ chain, and a 16 kd homodimer, the {chain. These polypeptides are co-immunoprecipitated from T cell clones and normal peripheral T cells with monoclonal antibodies that bind the α-β heterodimer or with antisera that bind the δ chain (Samelson et al., 1986b) or the { chain (Weissman et al., 1986). All of these murine polypeptides have counterparts on human T cells. These results indicated that the T cell antigen receptor is a seven-chain complex.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041330410
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  • 8
    Electronic Resource
    Electronic Resource
    Selective release from cultured mammalian cells of heat-shock (stress) proteins that resemble glia-axon transfer proteins (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 138 (1989), S. 257-266 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Cultured rat embryo cells were stimulated to rapidly release a small group of proteins that included several heat-shock proteins (hsp110, hsp71, hscp73) and nonmuscle actin. The extracellular proteins were analyzed by two-dimensional polyacrylamide gel electrophoresis. Heat-shocked cells released the same set of proteins as control cells with the addition of the stress-inducible hspllO and hsp71. Release of these proteins was not blocked by either monensin or colchicine, inhibitors ofthe common secretory pathway. A small amount of the glucose-regulated protein grp78 was externalized by this pathway. The extracel-lular accumulation of these proteins was inhibited after they were synthesized in the presence of the lysine analogue aminoethyl cysteine. It is likely that the analogue-substituted proteins were misfolded and could not be released from cells, supporting our conclusion that a selective release mechanism is involved. Remarkably, actin and the squid heat-shock proteins homologous to rat hsp71 and hsp110 are also among a select group of proteins transferred from glial cells to the squid giant axon, where they have been implicated in neuronal stress responses (Tytell et al.:Brain Res., 363:161-164, 1986). Based in part on the similarities between these two sets of proteins, we hypothesized that these proteins were released from labile cortical regions of animal cells in response to perturbations of homeostasis in cells as evolutionarily distinct as cultured rat embryo cells and squid glial cells.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041380206
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  • 9
    Electronic Resource
    Electronic Resource
    Induction of stress proteins in chicken embryo cells by low-level zinc contamination in amino acid-free media (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 122 (1985), S. 205-209 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: It has been reported that chicken embryo cells deprived of exogenous amino acids for 4 hours synthesize stress (heat-shock) proteins. Herein, we show that amino acid deprivation is not sufficient to cause induction of stress proteins. Zinc contaminating a component of commercial cell culture medium used to prepare amino acid-free medium was an inducer in our cultures. In the absence of exogenous amino acids, the concentration of zinc ions needed for half-maximal induction of stress proteins was an order of magnitude lower than the dose required for cells in complete medium. Histidine and cystine, which have high affinities for zinc ions, were the amino acids most effective in blocking the induction of stress proteins by zinc. Problems posed by heavy metal ions in culture media and biologic fluids for searches for in vivo inducers of the cellular stress (heat shock) response are discussed.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041220207
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  • 10
    Electronic Resource
    Electronic Resource
    The 73 kilodalton heat shock cognate protein purified from rat brain contains nonesterified palmitic and stearic acids (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 128 (1986), S. 239-245 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A protein related to the 71 kilodalton inducible rat heat shock protein was purified to electrophoretic homogeneity in milligram amounts from brain tissue of nonheat-stressed rats. The protein has been designated as a stress cognate protein based on previous studies and data presented herein that this protein cross-reacted with a monoclonal antibody originally raised against the Drosophila 70 kilodalton heat shock protein. The purified protein had an apparent molecular mass of 73 kilodaltons when analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis and an apparent mass of 150 kilodaltons as determined by nondissociative gel chromatography, suggesting that the purified protein is a homodimer. The purified protein had isoelectric points of 5.0 under nondissociative conditions and 5.6 when exposed to protein denaturants, suggesting loss of bound anionic molecules and/or net exposure of basic residues upon denaturation. Chloroform/methanol extraction of the purified protein and subsequent analyses by thin layer and gas-liquid chromatography resulted in the identification of palmitic and stearic acids noncovalently bound to the protein. Approximately four molecules of fatty acids were bound per dimer with palmitic and stearic acids present in a one-to-one ratio. The purified protein did not bind exogenously added radio-active palmitate, indicating that the fatty acid-binding sites of the cognate protein were fully occupied and that the associated fatty acids were too tightly bound to exchange readily. The possible significance of the fatty acids associated with the 73 kilodalton stress cognate protein is discussed.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041280215
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