The Median Tentacle of the Larva of Lingula Anatina (Brachiopoda) From Queensland, Australia

1996 ◽  
Vol 44 (4) ◽  
pp. 355 ◽  
Author(s):  
C Lüter
Keyword(s):  
Extracellular Matrix ◽  
Nervous System ◽  
Contact Region ◽  
Single Cells ◽  
Muscle Cells ◽  
Proximal Part ◽  
Sensory Organ ◽  
Continuous Transition ◽  
Apical Ganglion

The median tentacle of the larvae of Lingula anatina has been investigated in order to obtain information about the morphological implications of its function and its relation to the paired tentacles of the larval lophophore. The median tentacle is a larval sensory organ with apical, intraepidermal collar receptors and a basiepidermal nervous system (apical ganglion). The monociliated muscle cells in the median tentacle form a compact musculature; where cilia emanate from the single cells, small compartments surrounded by three epithelial muscle cells can be observed. The number of cavities corresponds with the number of muscle cells. In the proximal part of the median tentacle these muscle cells build a continuous transition to the muscle cells in the paired tentacles; an extracellular matrix could not be found in the contact-region between both muscular systems. Because of this continuity the muscle cells in the median tentacle must be regarded as part of the mesosome. The unpaired median tentacle is restricted to the larvae of all species of the Lingulida and Discinida within the inarticulate brachiopods and is lacking in all other brachiopod larvae. Because it is also unknown in Phoronida, it could be regarded as a synapomorphic characteristic of the supraspecific taxa Lingulida and Discinida.

Polarization, migration and homotypical interactions among prostatic smooth muscle cells in a laminin 111‐rich extracellular matrix

2020 ◽  
Author(s):  
Daniel Andrés Osório ◽  
Silvio Roberto Consonni ◽  
Aline Mara dos Santos ◽  
Hernandes F. Carvalho
Keyword(s):  
Extracellular Matrix ◽  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Muscle Cells

scholarly journals A Gain-of-Function Screen for Genes That Affect the Development of the Drosophila Adult External Sensory Organ

Genetics ◽  
2000 ◽  
Vol 155 (2) ◽  
pp. 733-752 ◽  
Author(s):  
Salim Abdelilah-Seyfried ◽  
Yee-Ming Chan ◽  
Chaoyang Zeng ◽  
Nicholas J Justice ◽  
Susan Younger-Shepherd ◽  
...  
Keyword(s):  
Nervous System ◽  
Peripheral Nervous System ◽  
Cell Fate ◽  
P Element ◽  
External Support ◽  
Sensory Organ ◽  
Sensory Organs ◽  
Gain Of Function ◽  
Asymmetric Cell Divisions ◽  
Single Precursor

Abstract The Drosophila adult external sensory organ, comprising a neuron and its support cells, is derived from a single precursor cell via several asymmetric cell divisions. To identify molecules involved in sensory organ development, we conducted a tissue-specific gain-of-function screen. We screened 2293 independent P-element lines established by P. Rørth and identified 105 lines, carrying insertions at 78 distinct loci, that produced misexpression phenotypes with changes in number, fate, or morphology of cells of the adult external sensory organ. On the basis of the gain-of-function phenotypes of both internal and external support cells, we subdivided the candidate lines into three classes. The first class (52 lines, 40 loci) exhibits partial or complete loss of adult external sensory organs. The second class (38 lines, 28 loci) is associated with increased numbers of entire adult external sensory organs or subsets of sensory organ cells. The third class (15 lines, 10 loci) results in potential cell fate transformations. Genetic and molecular characterization of these candidate lines reveals that some loci identified in this screen correspond to genes known to function in the formation of the peripheral nervous system, such as big brain, extra macrochaetae, and numb. Also emerging from the screen are a large group of previously uncharacterized genes and several known genes that have not yet been implicated in the development of the peripheral nervous system.

Abnormal Deposition of Extracellular Matrix Proteins by Cultured Smooth Muscle Cells from Human Varicose Veins

1998 ◽  
Vol 35 (2) ◽  
pp. 115-123 ◽  
Author(s):  
Patricia Sansilvestri-Morel ◽  
Isabelle Nonotte ◽  
Marie-Pierre Fournet-Bourguignon ◽  
Alain Rupin ◽  
Jean-Noël Fabiani ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Varicose Veins ◽  
Extracellular Matrix Proteins ◽  
Muscle Cells ◽  
Matrix Proteins ◽  
Cultured Smooth Muscle Cells

Initial characterization of anosmin-1, a putative extracellular matrix protein synthesized by definite neuronal cell populations in the central nervous system

1996 ◽  
Vol 109 (7) ◽  
pp. 1749-1757 ◽  
Author(s):  
N. Soussi-Yanicostas ◽  
J.P. Hardelin ◽  
M.M. Arroyo-Jimenez ◽  
O. Ardouin ◽  
R. Legouis ◽  
...  
Keyword(s):  
Central Nervous System ◽  
Extracellular Matrix ◽  
Nervous System ◽  
Cell Membrane ◽  
Heparan Sulfate ◽  
Matrix Protein ◽  
Neuronal Cell ◽  
Extracellular Matrix Protein ◽  
Cell Populations

The KAL gene is responsible for the X-chromosome linked form of Kallmann's syndrome in humans. Upon transfection of CHO cells with a human KAL cDNA, the corresponding encoded protein, KALc, was produced. This protein is N-glycosylated, secreted in the cell culture medium, and is localized at the cell surface. Several lines of evidence indicate that heparan-sulfate chains of proteoglycan(s) are involved in the binding of KALc to the cell membrane. Polyclonal and monoclonal antibodies to the purified KALc were generated. They allowed us to detect and characterize the protein encoded by the KAL gene in the chicken central nervous system at late stages of embryonic development. This protein is synthesized by definite neuronal cell populations including Purkinje cells in the cerebellum, mitral cells in the olfactory bulbs and several subpopulations in the optic tectum and the striatum. The protein, with an approximate molecular mass of 100 kDa, was named anosmin-1 in reference to the deficiency of the sense of smell which characterizes the human disease. Anosmin-1 is likely to be an extracellular matrix component. Since heparin treatment of cell membrane fractions from cerebellum and tectum resulted in the release of the protein, we suggest that one or several heparan-sulfate proteoglycans are involved in the binding of anosmin-1 to the membranes in vivo.

Metabolic modulation of hexokinase association with mitochondria in living smooth muscle cells

1996 ◽  
Vol 270 (2) ◽  
pp. C488-C499 ◽  
Author(s):  
R. M. Lynch ◽  
W. Carrington ◽  
K. E. Fogarty ◽  
F. S. Fay
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Energy State ◽  
Single Cells ◽  
Inverse Correlation ◽  
Muscle Cells ◽  
Cell Types ◽  
Differential Sensitivity ◽  
Similar Distribution ◽  
Apparent Difference

Hexokinase isoform I binds to mitochondria of many cell types. It has been hypothesized that this association is regulated by changes in the concentrations of specific cellular metabolites. To study the distribution of hexokinase in living cells, fluorophore-labeled functional hexokinase I was prepared. After microinjection into A7r5 smooth muscle cells, hexokinase localized to distinct structures identified as mitochondria. The endogenous hexokinase demonstrated a similar distribution with the use of immunocytochemistry. 2-Deoxyglucose elicited an increase in glucose 6-phosphate (G-6-P) and a decrease in ATP levels and diminished hexokinase binding to mitochondria in single cells. 3-O-methylglucose elicited slowly developing decreases in all three parameters. In contrast, cyanide elicited a rapid decrease in both ATP and hexokinase binding. Analyses of changes in metabolite levels and hexokinase binding indicate a positive correlation between binding and cell energy state as monitored by ATP. On the other hand, only in the presence of 2-deoxyglucose was the predicted inverse correlation between binding and G-6-P observed. Unlike the relatively large changes in distribution observed with the fluorescent-injected hexokinase, cyanide caused only a small decrease in the localization of endogenous hexokinase with mitochondria. These findings suggest that changes in the concentrations of specific metabolites can alter the binding of hexokinase I to specific sites on mitochondria. Moreover, the apparent difference in sensitivity of injected and endogenous hexokinase to changes in metabolites may reflect the presence of at least two classes of binding mechanisms for hexokinase, with differential sensitivity to metabolites.

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