Immunohistological analysis on distribution of smooth muscle tissues in livers of various vertebrates with attention to different liver architectures

To determine the cellular site for uptake and degradation of circulating prostaglandins (PGs) by the lung, the metabolism of PGA1 and PGF2 alpha was studied in pig lung slices, smooth muscle preparations, and pulmonary valves, as well as in isolated and cultured endothelial cells and cultured fibroblasts. Formation of 15-keto metabolites of both PGA1 and PGF2 alpha by lung slices was confirmed. No evidence of PGF2 alpha degradation could be found in any of the remaining preparations. For PGA1, however, 15-hydroxyprostaglandin dehydrogenase activity was detected in the three smooth muscle preparations studied (trachea, aorta, pulmonary artery) and found to be similar to that measured in lung slices. But the inhibitory effect of diphloretin phosphate and bromcresol green was much more marked in smooth muscle tissues than in lung slices, which suggested that PGA1 metabolism by the lung was not due to smooth muscle cells. Endothelial cells, freshly isolated and cultured, originating from the pulmonary artery and from the aorta, formed a PGA1-glutathione adduct, poorly extractable in ethyl acetate. This reaction, also present in cultured fibroblasts, was inhibited by ethacrynic acid. The cellular site responsible for the pulmonary degradation of circulating PGs remains undetermined.

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The Appendix as a Viable Source of Neural Progenitor Cells to Functionally Innervate Bioengineered Gastrointestinal Smooth Muscle Tissues

Stem Cells Translational Medicine ◽

10.5966/sctm.2014-0238 ◽

2015 ◽

Vol 4 (6) ◽

pp. 548-554 ◽

Cited By ~ 7

Author(s):

Elie Zakhem ◽

Stephen L. Rego ◽

Shreya Raghavan ◽

Khalil N. Bitar

Keyword(s):

Smooth Muscle ◽

Progenitor Cells ◽

Neural Progenitor Cells ◽

Neural Progenitor ◽

Gastrointestinal Smooth Muscle ◽

Muscle Tissues

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Molecular cloning of chicken calcyclin (S100A6) and identification of putative isoforms

Biochemistry and Cell Biology ◽

10.1139/o97-068 ◽

1997 ◽

Vol 75 (6) ◽

pp. 733-738 ◽

Cited By ~ 4

Author(s):

Bruce G Allen ◽

Jacquelyn E Andrea ◽

Cindy Sutherland ◽

Brett O Schönekess ◽

Michael P Walsh

Keyword(s):

Smooth Muscle ◽

Amino Acid ◽

Anion Exchange Chromatography ◽

Exchange Chromatography ◽

Chain Reaction ◽

Proteolytic Fragment ◽

Chicken Gizzard ◽

Muscle Tissues ◽

Bona Fide ◽

Polymerase Chain

A full-length cDNA encoding smooth muscle calcyclin (S100A6) was cloned from chicken gizzard, using reverse transcription - polymerase chain reaction techniques. The deduced amino acid sequence contains 92 residues with 12 substitutions and a 2 amino acid C-terminal extension when compared with human calcyclin. Calcyclin was purified from chicken gizzard by Ca2+-dependent hydrophobic chromatography, heat treatment, and anion-exchange chromatography. N-terminal sequencing of two CNBr peptides confirmed its identity as calcyclin. Two isoforms of calcyclin (A and B), which differ with respect to the presence or absence of a C-terminal lysine, were identified and the native protein was shown to exist as noncovalently associated homodimers (AA and BB) and heterodimers (AB). Incubation of purified calcyclin AA with an extract of chicken gizzard did not result in degradation of calcyclin A or appearance of calcyclin B, suggesting that calcyclin B is a bona fide isoform rather than a proteolytic fragment generated during purification. Western blotting of chicken tissues with anti-(gizzard calcyclin) indicated abundant expression of calcyclin in smooth muscle tissues, including esophagus, large intestine, and trachea, with lower levels in lung, heart, kidney, and brain, and none detectable in liver or skeletal muscle.Key words: Ca2+-binding proteins, calcyclin, smooth muscle, cDNA cloning, isoforms.

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