Expression of alpha 1 integrin, a laminin-collagen receptor, during myogenesis and neurogenesis in the avian embryo

Development ◽  
1992 ◽  
Vol 116 (3) ◽  
pp. 585-600 ◽  
Author(s):  
J.L. Duband ◽  
A.M. Belkin ◽  
J. Syfrig ◽  
J.P. Thiery ◽  
V.E. Koteliansky
Keyword(s):  
Skeletal Muscle ◽  
Endothelial Cells ◽  
Smooth Muscle ◽  
Smooth Muscles ◽  
Collagen Iv ◽  
Integrin Subunit ◽  
Avian Embryo ◽  
Subunit Expression ◽  
Capillary Endothelial Cells ◽  
Collagen Receptor

In this study, we have examined the spatiotemporal distribution of the alpha 1 integrin subunit, a putative laminin and collagen receptor, in avian embryos, using immunofluorescence microscopy and immunoblotting techniques. We used an antibody raised against a gizzard 175 × 10(3) M(r) membrane protein which was described previously and which we found to be immunologically identical to the chicken alpha 1 integrin subunit. In adult avian tissues, alpha 1 integrin exhibited a very restricted pattern of expression; it was detected only in smooth muscle and in capillary endothelial cells. In the developing embryo, alpha 1 integrin subunit expression was discovered in addition to smooth muscle and capillary endothelial cells, transiently, in both central and peripheral nervous systems and in striated muscles, in association with laminin and collagen IV. alpha 1 integrin was practically absent from most epithelial tissues, including the liver, pancreas and kidney tubules, and was weakly expressed by tissues that were not associated with laminin and collagen IV. In the nervous system, alpha 1 integrin subunit expression occurred predominantly at the time of early neuronal differentiation. During skeletal muscle development, alpha 1 integrin was expressed on myogenic precursors, during myoblast migration, and in differentiating myotubes. alpha 1 integrin disappeared from skeletal muscle cells as they became contractile. In visceral and vascular smooth muscles, alpha 1 integrin appeared specifically during early smooth muscle cell differentiation and, later, was permanently expressed after cell maturation. These results indicate that (i) the expression pattern of alpha 1 integrin is consistent with a function as a laminin/collagen IV receptor; (ii) during avian development, expression of the alpha 1 integrin subunit is spatially and temporally regulated; (iii) during myogenesis and neurogenesis, expression of alpha 1 integrin is transient and correlates with cell migration and differentiation.

Endothelial cell integrin alpha5beta1 expression is modulated by cytokines and during migration in vitro

1999 ◽  
Vol 112 (4) ◽  
pp. 569-578 ◽  
Author(s):  
G. Collo ◽  
M.S. Pepper
Keyword(s):  
Endothelial Cells ◽  
Endothelial Cell ◽  
Growth Factor ◽  
Transforming Growth Factor ◽  
Integrin Subunit ◽  
Subunit Expression ◽  
Synergistic Induction ◽  
Co Addition ◽  
Extracellular Matrix Interactions

Alterations in endothelial cell-extracellular matrix interactions are central to the process of angiogenesis. We have investigated the effect of wound-induced two-dimensional migration, basic fibroblast growth factor (bFGF), transforming growth factor-beta1 (TGF-beta1) and leukemia inhibitory factor (LIF) on expression of the alpha5beta1 integrin in endothelial cells. In multiple-wounded monolayers of bovine microvascular endothelial (BME) cells, an increase in mRNA and total protein for both alpha5 and beta1 subunits was observed, and this could be correlated with a reduction in cell density but not proliferation, both of which are induced following wounding. Although as previously reported, the alpha5 subunit was increased when cells were exposed to TGF-beta1 alone, co-addition of bFGF and TGF-beta1 resulted in a striking synergistic induction of alpha5, with no significant changes in the expression of beta1. In contrast, the alpha5 subunit was decreased by LIF in bovine aortic endothelial but not in BME cells. These findings suggest that quantitative alterations in alpha5 and beta1 integrin subunit expression modulate the adhesive and migratory properties of endothelial cells during angiogenesis.

Molecular diversity of KVα- and β-subunit expression in canine gastrointestinal smooth muscles

1999 ◽  
Vol 277 (1) ◽  
pp. G127-G136 ◽  
Author(s):  
Anne Epperson ◽  
Helena P. Bonner ◽  
Sean M. Ward ◽  
William J. Hatton ◽  
Karri K. Bradley ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Smooth Muscles ◽  
Muscle Cells ◽  
Pcr Analysis ◽  
Transcriptional Level ◽  
Gi Tract ◽  
Excitable Cells ◽  
Subunit Expression ◽  
Molecular Components

Voltage-activated K+(KV) channels play an important role in regulating the membrane potential in excitable cells. In gastrointestinal (GI) smooth muscles, these channels are particularly important in modulating spontaneous electrical activities. The purpose of this study was to identify the molecular components that may be responsible for the KV currents found in the canine GI tract. In this report, we have examined the qualitative expression of eighteen different KV channel genes in canine GI smooth muscle cells at the transcriptional level using RT-PCR analysis. Our results demonstrate the expression of KV1.4, KV1.5, KV1.6, KV2.2, and KV4.3 transcripts in all regions of the GI tract examined. Transcripts encoding KV1.2, KVβ1.1, and KVβ1.2 subunits were differentially expressed. KV1.1, KV1.3, KV2.1, KV3.1, KV3.2, KV3.4, KV4.1, KV4.2, and KVβ2.1 transcripts were not detected in any GI smooth muscle cells. We have also determined the protein expression for a subset of these KV channel subunits using specific antibodies by immunoblotting and immunohistochemistry. Immunoblotting and immunohistochemistry demonstrated that KV1.2, KV1.4, KV1.5, and KV2.2 are expressed at the protein level in GI tissues and smooth muscle cells. KV2.1 was not detected in any regions of the GI tract examined. These results suggest that the wide array of electrical activity found in different regions of the canine GI tract may be due in part to the differential expression of KV channel subunits.

Proteins of interstitial cells of Cajal and intestinal smooth muscle, colocalized with caveolin-1

2005 ◽  
Vol 288 (3) ◽  
pp. G571-G585 ◽  
Author(s):  
Woo Jung Cho ◽  
E. E. Daniel
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Gap Junction ◽  
Interstitial Cells Of Cajal ◽  
Smooth Muscles ◽  
Circular Muscle ◽  
Interstitial Cells ◽  
Caveolin 1 ◽  
Cells Of Cajal ◽  
Junction Proteins

The murine jejunum and lower esophageal sphincter (LES) were examined to determine the locations of various signaling molecules and their colocalization with caveolin-1 and one another. Caveolin-1 was present in punctate sites of the plasma membranes (PM) of all smooth muscles and diffusely in all classes of interstitial cells of Cajal (ICC; identified by c-kit immunoreactivity), ICC-myenteric plexus (MP), ICC-deep muscular plexus (DMP), ICC-serosa (ICC-S), and ICC-intramuscularis (IM). In general, all ICC also contained the L-type Ca2+ (L-Ca2+) channel, the PM Ca2+ pump, and the Na+/Ca2+ exchanger-1 localized with caveolin-1. ICC in various sites also contained Ca2+-sequestering molecules such as calreticulin and calsequestrin. Calreticulin was present also in smooth muscle, frequently in the cytosol, whereas calsequestrin was present in skeletal muscle of the esophagus. Gap junction proteins connexin-43 and -40 were present in circular muscle of jejunum but not in longitudinal muscle or in LES. In some cases, these proteins were associated with ICC-DMP. The large-conductance Ca2+-activated K+ channel was present in smooth muscle and skeletal muscle of esophagus and some ICC but was not colocalized with caveolin-1. These findings suggest that all ICC have several Ca2+-handling and -sequestering molecules, although the functions of only the L-Ca2+ channel are currently known. They also suggest that gap junction proteins are located at sites where ultrastructural gap junctions are know to exist in circular muscle of intestine but not in other smooth muscles. These findings also point to the need to evaluate the function of Ca2+ sequestration in ICC.

scholarly journals A novel pressure-jump apparatus for the microvolume analysis of protein–ligand and protein–protein interactions: its application to nucleotide binding to skeletal-muscle and smooth-muscle myosin subfragment-1

2002 ◽  
Vol 366 (2) ◽  
pp. 643-651 ◽  
Author(s):  
David S. PEARSON ◽  
Georg HOLTERMANN ◽  
Patricia ELLISON ◽  
Christine CREMO ◽  
Michael A. GEEVES
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Protein Interactions ◽  
Muscle Protein ◽  
Smooth Muscles ◽  
High Volume ◽  
Pressure Jump ◽  
Original Design ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1

Reactions involving proteins frequently involve large changes in volume, which allows the equilibrium position to be perturbed by changes in pressure. Rapid changes in pressure can thus be used to initiate relaxation in pressure; however, this approach is seldom used, because it requires specialized equipment. We have built a microvolume (50μl) pressure-jump apparatus, powered by a piezoelectric actuator, based on the original design of Clegg and Maxfield [(1976) Rev. Sci. Instrum. 47, 1383–1393]. This equipment can apply pressure changes of ±20MPa (maximally) in time periods as short as 80μs and follow the resulting change in fluorescence signals. The system is relatively simple to use with fast (approx. 1min) exchange of samples. In the present study, we show that this system can perturb the binding of 2′(3′)-O-(N-methylanthraniloyl)-ADP to myosin subfragment-1(S1) from skeletal and smooth muscles. The kinetic data are consistent with previous work, and in addition show that, although 2′(3′)-O-(N-methylanthraniloyl)-ADP binds with a similar affinity to both proteins, the increase in molar volume for the skeletal-muscle S1 binding to ADP is half of that for the smooth-muscle protein. This high-volume change for smooth-muscle S1 may be related to the ability of ADP to induce a 23° tilt in the tail of S1 bound to actin.

scholarly journals Troponin C-like proteins (calmodulins) from mammalian smooth muscle and other tissues

1979 ◽  
Vol 177 (2) ◽  
pp. 521-529 ◽  
Author(s):  
R J Grand ◽  
S V Perry ◽  
R A Weeks
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Troponin I ◽  
Smooth Muscles ◽  
Bovine Brain ◽  
Troponin C ◽  
Rabbit Skeletal Muscle ◽  
Polyacrylamide Gels ◽  
Rabbit Lung ◽  
Chicken Gizzard

1. An acidic protein with properties similar to those of troponin C from rabbit skeletal muscle has been shown to be present in bovine and rabbit smooth muscles, chicken gizzard and rabbit liver, kidney and lung. 2. A simple new method involving the use of organic solvents is described for the purification of the troponin C-like proteins from various tissues. 3. The troponin C-like proteins can be distinguished from rabbit skeletal-muscle toponin C by their electrophoretic behaviour on polyacrylamide gels at pH 8.3 in the presence and absence of Ca2+. The troponin C-like proteins have been shown to form complexes with rabbit skeletal-muscle troponin I that migrate on electrophoresis in polyacrylamide gels. 4. Behaviour on electrophoresis, amino acid analysis and the patterns of CNBr digests on polyacrylamide gels indicate that the troponin C-like proteins from bovine uterus and aorta, rabbit uterus, and liver and chicken gizzard are very similar to, if not identical with, bovine brain modulator protein. 5. With bovine cardiac muscle the organic-solvent method yields a preparation consisting of roughly similar amounts of troponin C and troponin C-like protein. 6. By the isotope-dilution technique, troponin C-like protein has been shown to represent 0.42% of the total protein in rabbit uterus. 7. In homogenates of smooth muscle, rabbit lung, kidney and brain, the troponin C-like proteins form a complex with other protein (or proteins) that requires Ca2+ for its formation and that is not dissociated in 9M-urea.

scholarly journals Localization of xanthine dehydrogenase mRNA in horse skeletal muscle by in situ hybridization with digoxigenin-labelled probe

1993 ◽  
Vol 292 (3) ◽  
pp. 639-641 ◽  
Author(s):  
L A Räsänen ◽  
U Karvonen ◽  
A R Pösö
Keyword(s):  
Skeletal Muscle ◽  
Endothelial Cells ◽  
In Situ Hybridization ◽  
Northern Blot ◽  
Cdna Sequence ◽  
Muscle Cells ◽  
Xanthine Dehydrogenase ◽  
Capillary Endothelial Cells

In situ hybridization was used to localize xanthine dehydrogenase (XDH) mRNA in horse skeletal muscle. Capillary endothelial cells were found to express XDH, but muscle cells did not give any signal. The digoxigenin-labelled probe was produced by PCR with primers based on the cDNA sequence of mouse XDH and horse lung cDNAs. A 4.3 kb mRNA was detected in a Northern blot.

scholarly journals Apoptosis in capillary endothelial cells in ageing skeletal muscle

Aging Cell ◽  
2013 ◽  
Vol 13 (2) ◽  
pp. 254-262 ◽  
Author(s):  
Huijuan Wang ◽  
Anne Listrat ◽  
Bruno Meunier ◽  
Marine Gueugneau ◽  
Cécile Coudy‐Gandilhon ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Endothelial Cells ◽  
Capillary Endothelial Cells

scholarly journals Connexin expression and conducted vasodilation along arteriolar endothelium in mouse skeletal muscle

2004 ◽  
Vol 97 (3) ◽  
pp. 1152-1158 ◽  
Author(s):  
Robin C. Looft-Wilson ◽  
Geoffrey W. Payne ◽  
Steven S. Segal
Keyword(s):  
Skeletal Muscle ◽  
Endothelial Cells ◽  
Smooth Muscle ◽  
Gap Junction ◽  
Connexin Expression ◽  
Mouse Skeletal Muscle ◽  
Gap Junction Channels ◽  
Platelet Endothelial Cell Adhesion ◽  
Arteriolar Wall ◽  
Cell Layers

Functional hyperemia requires the coordination of smooth muscle cell relaxation along and between branches of the arteriolar network. Vasodilation is conducted from cell to cell along the arteriolar wall through gap junction channels composed of connexin protein subunits. Within skeletal muscle, it is unclear whether arteriolar endothelium, smooth muscle, or both cell layers provide the cellular pathway for conduction. Furthermore, the constitutive profile of connexin expression within the microcirculation is unknown. We tested the hypothesis that conducted vasodilation and connexin expression are intrinsic to the endothelium of arterioles (17 ± 1 μm diameter) that supply the skeletal muscle fibers in the cremaster of anesthetized C57BL/6 mice. ACh delivered to an arteriole (500 ms, 1-μA pulse; 1-μm micropipette) produced local dilation of 17 ± 1 μm; conducted vasodilation observed 1 mm upstream was 9 ± 1 μm ( n = 5). After light-dye treatment to selectively disrupt endothelium (250-μm segment centered 500 μm upstream, confirmed by loss of local response to ACh while constriction to phenylephrine and dilation to sodium nitroprusside remained intact), we found that conducted vasodilation was nearly abolished (2 ± 1 μm; P < 0.05). Whole-mount immunohistochemistry for connexins revealed punctate labeling at borders of arteriolar endothelial cells, with connexin40 and connexin37 in all branches and connexin43 only in the largest branches. Immunoreactivity for connexins was not apparent in smooth muscle or in capillary or venular endothelium, despite robust immunolabeling for α-actin and platelet endothelial cell adhesion molecule-1, respectively. We conclude that vasodilation is conducted along the endothelium of mouse skeletal muscle arterioles and that connexin40 and connexin37 are the primary connexins forming gap junction channels between arteriolar endothelial cells.

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