Expression and epitopic conservation of calponin in different smooth muscles and during development

1996 ◽  
Vol 74 (2) ◽  
pp. 187-196 ◽  
Author(s):  
Jian-Ping Jin ◽  
Michael P. Walsh ◽  
Mary E. Resek ◽  
Gail A. McMartin
Keyword(s):  
Smooth Muscle ◽  
Thin Filament ◽  
Smooth Muscles ◽  
Constitutive Expression ◽  
Young Chick ◽  
Adult Chicken ◽  
Muscle Tissues ◽  
Highly Sensitive ◽  
Cnbr Cleavage ◽  
Low Levels

Calponin is a thin filament associated protein found in smooth muscle as a potential modulator of contraction. Five mouse monoclonal antibodies (mAbs CP1, CP3, CP4, CP7, and CP8) were prepared against chicken gizzard α-calponin. The CP1 epitopic structure is conserved in smooth muscles across vertebrate phyla and is highly sensitive to CNBr cleavage in contrast with the chicken-specific CP4 and the avian–mammalian-specific CP8 epitopes that are resistant to CNBr fragmentation. Using this panel of mAbs against multiple epitopes, only α-calponin was detected in adult chicken smooth muscles and throughout development of the gizzard. Western blotting showed that the calponin content varied among different smooth muscle tissues and correlated with that of h-caldesmon. In contrast with the constitutive expression of calponin in phasic smooth muscle of the digestive tract, very low levels of calponin were detected in adult avian tracheas and no calponin expression was detected in embryonic and young chick tracheas. These results provide information on the structural conservation of calponins and suggest a relationship between calponin expression and smooth muscle functional states.Key words: smooth muscle calponin, caldesmon, expression, development, chicken trachea.

scholarly journals Calcium-Activated Chloride Channels in Myometrial and Vascular Smooth Muscle

2021 ◽  
Vol 12 ◽  
Author(s):  
Susan Wray ◽  
Clodagh Prendergast ◽  
Sarah Arrowsmith
Keyword(s):  
Smooth Muscle ◽  
Chloride Channels ◽  
Smooth Muscles ◽  
Functional Results ◽  
Molecular Entity ◽  
Muscle Tissues ◽  
Channel Opening ◽  
Activation Mechanisms ◽  
Intracellular Ca ◽  
And Control

In smooth muscle tissues, calcium-activated chloride channels (CaCC) provide the major anionic channel. Opening of these channels leads to chloride efflux and depolarization of the myocyte membrane. In this way, activation of the channels by a rise of intracellular [Ca2+], from a variety of sources, produces increased excitability and can initiate action potentials and contraction or increased tone. We now have a good mechanistic understanding of how the channels are activated and regulated, due to identification of TMEM16A (ANO1) as the molecular entity of the channel, but key questions remain. In reviewing these channels and comparing two distinct smooth muscles, myometrial and vascular, we expose the differences that occur in their activation mechanisms, properties, and control. We find that the myometrium only expresses “classical,” Ca2+-activated, and voltage sensitive channels, whereas both tonic and phasic blood vessels express classical, and non-classical, cGMP-regulated CaCC, which are voltage insensitive. This translates to more complex activation and regulation in vascular smooth muscles, irrespective of whether they are tonic or phasic. We therefore tentatively conclude that although these channels are expressed and functionally important in all smooth muscles, they are probably not part of the mechanisms governing phasic activity. Recent knockdown studies have produced unexpected functional results, e.g. no effects on labour and delivery, and tone increasing in some but decreasing in other vascular beds, strongly suggesting that there is still much to be explored concerning CaCC in smooth muscle.

scholarly journals An abundant and novel protein of 22 kDa (SM22) is widely distributed in smooth muscles. Purification from bovine aorta

1987 ◽  
Vol 244 (3) ◽  
pp. 705-709 ◽  
Author(s):  
J P Lees-Miller ◽  
D H Heeley ◽  
L B Smillie
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscles ◽  
Chicken Breast ◽  
Antibody Preparation ◽  
Chicken Gizzard ◽  
Gradient Electrophoresis ◽  
Muscle Tissues ◽  
Rabbit Polyclonal Antibody ◽  
Similar Amino Acid ◽  
Novel Protein

Using a rabbit polyclonal-antibody preparation directed against the chicken gizzard protein, we demonstrated by immunoblotting the presence of the 22 kDa protein (SM22) in a variety of chicken smooth-muscle-containing organs, including uterus, intestine, gizzard, oesophagus and aorta. Protein SM22 was present in only trace amounts in brain, liver and heart, and could not be detected in chicken breast muscle. The antibody preparation did not cross-react with extracts of bovine aorta. However, the presence of SM22 as a major component in bovine aorta and pig carotid was demonstrated by its co-migration with the purified chicken gizzard protein on one- and two-dimensional polyacrylamide electrophoretic gels. Its molar abundance relative to actin was estimated to be 0.9:6.0 and 1.4:6.0 for bovine aorta and pig carotid respectively. Like the chicken gizzard protein, it separates on pH-gradient electrophoresis into at least three variants, alpha, beta and gamma, with similar apparent Mr. Purification of the aorta SM22 showed it to have a similar amino acid composition to the chicken gizzard protein. We conclude that SM22 is widely distributed and an abundant and unique protein component of smooth-muscle tissues of birds and mammals.

scholarly journals An invertebrate smooth muscle with striated muscle myosin filaments

2015 ◽  
Vol 112 (42) ◽  
pp. E5660-E5668 ◽  
Author(s):  
Guidenn Sulbarán ◽  
Lorenzo Alamo ◽  
Antonio Pinto ◽  
Gustavo Márquez ◽  
Franklin Méndez ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Actin Filaments ◽  
Striated Muscle ◽  
Smooth Muscles ◽  
Structural Similarity ◽  
Striated Muscles ◽  
Muscle Tissues ◽  
Myosin Filaments ◽  
Muscle Myosin ◽  
Surprising Finding

Muscle tissues are classically divided into two major types, depending on the presence or absence of striations. In striated muscles, the actin filaments are anchored at Z-lines and the myosin and actin filaments are in register, whereas in smooth muscles, the actin filaments are attached to dense bodies and the myosin and actin filaments are out of register. The structure of the filaments in smooth muscles is also different from that in striated muscles. Here we have studied the structure of myosin filaments from the smooth muscles of the human parasite Schistosoma mansoni. We find, surprisingly, that they are indistinguishable from those in an arthropod striated muscle. This structural similarity is supported by sequence comparison between the schistosome myosin II heavy chain and known striated muscle myosins. In contrast, the actin filaments of schistosomes are similar to those of smooth muscles, lacking troponin-dependent regulation. We conclude that schistosome muscles are hybrids, containing striated muscle-like myosin filaments and smooth muscle-like actin filaments in a smooth muscle architecture. This surprising finding has broad significance for understanding how muscles are built and how they evolved, and challenges the paradigm that smooth and striated muscles always have distinctly different components.

scholarly journals Caldesmon is a Ca2+-regulatory component of native smooth-muscle thin filaments

1985 ◽  
Vol 231 (3) ◽  
pp. 517-522 ◽  
Author(s):  
S B Marston ◽  
W Lehman
Keyword(s):  
Smooth Muscle ◽  
Thin Filament ◽  
Myosin Light Chain ◽  
Potent Inhibitor ◽  
Peptide Mapping ◽  
Smooth Muscles ◽  
Physiological Mechanism ◽  
Thin Filaments ◽  
Muscle Types ◽  
Mgatpase Activity

Thin-filament preparations from four smooth muscle types (gizzard, stomach, trachea, aorta) all activate myosin MgATPase activity, are regulated by Ca2+, and contain actin, tropomyosin and a 120000-140000-Mr protein in the molar proportions 1:1/7:1/26. The 120000-140000-Mr protein from all sources is a potent inhibitor of actomyosin ATPase activity. Peptide-mapping and immunological evidence is presented showing that it is identical with caldesmon. Quantitative immunological data suggest that caldesmon is a component of all the thin filaments and that the thin-filament-bound caldesmon accounts for all the caldesmon in intact tissue. The myosin light-chain kinase content of thin-filament preparations was found to be negligible. We propose that caldesmon-based thin-filament Ca2+ regulation is a physiological mechanism in all smooth muscles.

Occurrence of anti-gizzard P34K antibody cross-reactive components in bovine smooth muscles and non-smooth muscle tissues

Life Sciences ◽  
1987 ◽  
Vol 41 (3) ◽  
pp. 291-296 ◽  
Author(s):  
Katsuhito Takahashi ◽  
Kunio Hiwada ◽  
Tatsuo Kokubu
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscles ◽  
Muscle Tissues

scholarly journals Hypoxic conditioning in blood vessels and smooth muscle tissues: effects on function, mechanisms, and unknowns

2018 ◽  
Vol 315 (4) ◽  
pp. H756-H770 ◽  
Author(s):  
Asmaa M. Almohanna ◽  
Susan Wray
Keyword(s):  
Smooth Muscle ◽  
Blood Vessels ◽  
Contractile Activity ◽  
Smooth Muscles ◽  
Cell Types ◽  
Hypoxic Preconditioning ◽  
Visceral Organs ◽  
Muscle Tissues ◽  
Force Increase ◽  
Liver And Kidney

Hypoxic preconditioning, the protective effect of brief, intermittent hypoxic or ischemic episodes on subsequent more severe hypoxic episodes, has been known for 30 yr from studies on cardiac muscle. The concept of hypoxic preconditioning has expanded; excitingly, organs beyond the heart, including the brain, liver, and kidney, also benefit. Preconditioning of vascular and visceral smooth muscles has received less attention despite their obvious importance to health. In addition, there has been no attempt to synthesize the literature in this field. Therefore, in addition to overviewing the current understanding of hypoxic conditioning, in the present review, we consider the role of blood vessels in conditioning and explore evidence for conditioning in other smooth muscles. Where possible, we have distinguished effects on myocytes from other cell types in the visceral organs. We found evidence of a pivotal role for blood vessels in conditioning and for conditioning in other smooth muscle, including the bladder, vascular myocytes, and gastrointestinal tract, and a novel response in the uterus of a hypoxic-induced force increase, which helps maintain contractions during labor. To date, however, there are insufficient data to provide a comprehensive or unifying mechanism for smooth muscles or visceral organs and the effects of conditioning on their function. This also means that no firm conclusions can be drawn as to how differences between smooth muscles in metabolic and contractile activity may contribute to conditioning. Therefore, we have suggested what may be general mechanisms of conditioning occurring in all smooth muscles and tabulated tissue-specific mechanistic findings and suggested ideas for further progress.

Smooth muscle protein kinase C

1994 ◽  
Vol 72 (11) ◽  
pp. 1392-1399 ◽  
Author(s):  
Michael P. Walsh ◽  
Jacquelyn E. Andrea ◽  
Bruce G. Allen ◽  
Odile Clément-Chomienne ◽  
Elizabeth M. Collins ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Thin Filament ◽  
Muscle Protein ◽  
Smooth Muscles ◽  
Proteolytic Fragment ◽  
Cross Bridge ◽  
Kinase C ◽  
Substrate Peptide

Protein kinase C (PKC) was first implicated in the regulation of smooth muscle contraction with the observation that phorbol esters induce slowly developing, sustained contractions. In some vascular smooth muscles, e.g., ferret aorta, phorbol ester induced contractions occur without an increase in sarcoplasmic free-Ca2+ concentration ([Ca]i) or myosin light chain phosphorylation. This response appears to be mediated by a Ca2+-independent isoenzyme of PKC (probably PKCε), since saponin-permeabilized single ferret aortic smooth muscle cells, which retain receptor coupling, developed force in response to phenylephrine at low free [Ca2+] (pCa 7.0–8.6) and the constitutively active proteolytic fragment of PKC (PKM) elicited a contraction at pCa 7 comparable with the phenylephrine-induced contraction. Both contractions were reversed by a pseudo-substrate peptide inhibitor of PKC. These observations suggest a mechanism whereby α-adrenergic agonists may elicit a contractile response without a Ca2+ signal: α-adrenergic stimulation of phosphatidylcholine-specific phosphoiipase C or D (the latter in conjunction with phosphatidate phosphohydrolase) generates diacylglycerol. In the absence of an increase in [Ca2+]i, diacylglycerol specifically activates so-called novel PKCs, of which ε is the only isoenzyme known to be expressed in vascular smooth muscle. Recent evidence suggests that PKC may trigger a cascade of phosphorylation reactions, resulting in activation of mitogen-activated protein kinase and phosphorylation of the thin filament associated protein caldesmon. Alternatively, or additionally, PKC may directly phosphorylate calponin, another thin filament associated protein. These phosphorylations are predicted to alleviate inhibition of the cross-bridge cycling rate by these thin-filament proteins. The slow development of force would then result from a slow rate of cross-bridge cycling due to the low basal level of myosin phosphorylation.Key words: protein kinase C, smooth muscle, calcium, caldesmon, calponin.

scholarly journals Expression of endoplasmic-reticulum Ca2+-pump isoforms and of phospholamban in pig smooth-muscle tissues

1990 ◽  
Vol 271 (3) ◽  
pp. 649-653 ◽  
Author(s):  
J A Eggermont ◽  
F Wuytack ◽  
J Verbist ◽  
R Casteels
Keyword(s):  
Endoplasmic Reticulum ◽  
Smooth Muscle ◽  
Pulmonary Artery ◽  
Western Blot ◽  
Mrna Levels ◽  
Protection Assay ◽  
Western Blots ◽  
Specific Antibodies ◽  
Muscle Tissues ◽  
Low Levels

The expression of the gene 2 sarcoplasmic/endoplasmic-reticulum Ca2(+)-pump isoforms (SERCA2a and SERCA2b) and of phospholamban was studied in pig smooth muscle of the stomach, longitudinal ileum, pulmonary artery and aorta. mRNA levels were determined using an RNAase protection assay. The SERCA2 isoforms and phospholamban were tested on Western blots with a panel of antibodies, some of which were isoform-specific. The pig smooth-muscle tissues all contained comparable SERCA2 mRNA levels, but these levels were 10-20-fold lower than SERCA2 mRNA levels in cardiac muscle. Of the SERCA2 mRNAs in smooth muscle, 72-81% encoded the non-muscle isoform (SERCA2b), and Western blot analysis with isoform-specific antibodies confirmed that the SERCA2b isoform is the predominant endoplasmic-reticulum Ca2(+)-pump in smooth muscle. In contrast with SERCA2 mRNA levels, phospholamban mRNA levels varied by 12-fold between the different pig smooth-muscle tissues, with low and very low levels in the pig pulmonary artery and the pig aorta respectively. The differential expression of phospholamban was also confirmed on Western blots. The finding that the phospholamban content varied between the different smooth-muscle tissues whereas the SERCA2 expression remained rather constant indicates that, in pig smooth muscle, the expression of phospholamban is not coupled with that of SERCA2.

scholarly journals Detecting the Multiomics Signatures of Factor-Specific Inflammatory Effects on Airway Smooth Muscles

2021 ◽  
Vol 11 ◽  
Author(s):  
Yu-Hang Zhang ◽  
Zhandong Li ◽  
Tao Zeng ◽  
Lei Chen ◽  
Hao Li ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Airway Smooth Muscle ◽  
Smooth Muscles ◽  
Inflammatory Factors ◽  
Airway Smooth Muscle Cells ◽  
Biological Mechanisms ◽  
Unique Type ◽  
Muscle Tissues ◽  
Specific Muscle ◽  
Contraction And Relaxation

Smooth muscles are a specific muscle subtype that is widely identified in the tissues of internal passageways. This muscle subtype has the capacity for controlled or regulated contraction and relaxation. Airway smooth muscles are a unique type of smooth muscles that constitute the effective, adjustable, and reactive wall that covers most areas of the entire airway from the trachea to lung tissues. Infection with SARS-CoV-2, which caused the world-wide COVID-19 pandemic, involves airway smooth muscles and their surrounding inflammatory environment. Therefore, airway smooth muscles and related inflammatory factors may play an irreplaceable role in the initiation and progression of several severe diseases. Many previous studies have attempted to reveal the potential relationships between interleukins and airway smooth muscle cells only on the omics level, and the continued existence of numerous false-positive optimal genes/transcripts cannot reflect the actual effective biological mechanisms underlying interleukin-based activation effects on airway smooth muscles. Here, on the basis of newly presented machine learning-based computational approaches, we identified specific regulatory factors and a series of rules that contribute to the activation and stimulation of airway smooth muscles by IL-13, IL-17, or the combination of both interleukins on the epigenetic and/or transcriptional levels. The detected discriminative factors (genes) and rules can contribute to the identification of potential regulatory mechanisms linking airway smooth muscle tissues and inflammatory factors and help reveal specific pathological factors for diseases associated with airway smooth muscle inflammation on multiomics levels.

scholarly journals Changes in the Contractile Activity and Reactivity to 5-HT of Smooth Muscles of Rats Following Total Body Irradiation with Accelerated Electrons

Folia Medica ◽  
2019 ◽  
Vol 61 (3) ◽  
pp. 411-418 ◽  
Author(s):  
Xenodochidis A. Charilaos ◽  
Raina G. Ardasheva ◽  
Veselin G. Popov ◽  
Natalia A. Prissadova ◽  
Valentin I. Turiyski ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Total Body Irradiation ◽  
Serotonin Receptors ◽  
Contractile Activity ◽  
Smooth Muscles ◽  
Control Group ◽  
Gi Tract ◽  
Circular Smooth Muscle ◽  
Muscle Tissues ◽  
Total Body

Background: Besides its “classical” neurotransmitter function in the central and peripheral nervous systems, serotonin, or 5-hydroxytryptamine (5-HT) is also a local hormone in a number of tissues, including those of the GI tract. Radiation is known to be able to disrupt certain functions of the tract, modulated by 5-HT-signaling pathways, or the serotonin receptors themselves. Aim: The present investigation focused on clarifying the nature and extent of influence of an accelerated electron beam with energy of 9 MeV on the serotonergic mediation of healthy smooth muscle gastric tissue of rats following total body irradiation of the animals. Materials and methods: The study involved a control group and two experimental groups of animals exposed to 1 and 5 Gy, respectively, using Siemens Primus S/N 3561. Circular smooth muscle tissues were isolated from rats 1 hour and 18 hours after they were exposed to 1 and 5 Gy and also 5 days after irradiation from the rats that received a dose of 5 Gy in order to investigate the action of exogenous serotonin at increasing concentrations from 10-8 to 10-4 mol/l. The contractile reactivity of each group SM preparations was registered isometrically. Results: Electron beams with energy of 9 MeV did not damage the contractile apparatus of gastric SM of rats and had a stimulating effect on contractility resulting from rapidly developing processes (1 hour) or later occurring once (5 days). Conclusions: Difference was observed in the importance of the factors of received dose, lapse of time from irradiation to investigation of SM tissues, and exogenous 5-HT concentration for the changes in SM reactivity in serotonin-induced tonic and phasic responses.

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