Adiponectin secretion from cardiomyocytes produces canonical multimers and partial co-localization with calsequestrin in junctional SR

Solarewicz, Joanna; Manly, Amanda; Kokoszka, Stephanie K.; Sleiman, Naama H.; Leff, Todd; Cala, Steven E.

doi:10.1007/s11010-019-03524-9

Cited by 7 publications

(7 citation statements)

References 41 publications

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“…In addition to abundant rabs, the rab associated protein PRA-1 (A SR = 25.0, 7 th highest ), and hedgehog acyltransferase-like protein (aka mitsugamin-56 [ 65 ]) were also enriched in SR (Online Resource 1). The possible close physical proximity of rabs to junctional SR sites is consistent with evidence of protein secretion in cultured cardiomyocytes emanating from sites close to junctional SR [ 66 ].…”

Section: Resultssupporting

confidence: 65%

Activation of Ca2+ transport in cardiac microsomes enriches functional sets of ER and SR proteins

et al. 2023

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The importance of sarcoplasmic reticulum (SR) Ca2+-handling in heart has led to detailed understanding of Ca2+-release and re-uptake protein complexes, while less is known about other endoplasmic reticulum (ER) functions in the heart. To more fully understand cardiac SR and ER functions, we analyzed cardiac microsomes based on their increased density through the actions of the SR Ca2+-ATPase (SERCA) and the ryanodine receptor that are highly active in cardiomyocytes. Crude cardiac microsomal vesicles loaded with Ca oxalate produced two higher density subfractions, MedSR and HighSR. Proteins from 20.0 μg of MV, MedSR, and HighSR protein were fractionated using SDS-PAGE, then trypsinized from 20 separate gel pieces, and analyzed by LC–MS/MS to determine protein content. From 62,000 individual peptide spectra obtained, we identified 1105 different proteins, of which 354 were enriched ≥ 2.0-fold in SR fractions compared to the crude membrane preparation. Previously studied SR proteins were all enriched, as were proteins associated with canonical ER functions. Contractile, mitochondrial, and sarcolemmal proteins were not enriched. Comparing the levels of SERCA-positive SR proteins in MedSR versus HighSR vesicles produced a range of SR subfraction enrichments signifying differing levels of Ca2+ leak co-localized in the same membrane patch. All known junctional SR proteins were more enriched in MedSR, while canonical ER proteins were more enriched in HighSR membrane. Proteins constituting other putative ER/SR subdomains also exhibited average Esub enrichment values (mean ± S.D.) that spanned the range of possible Esub values, suggesting that functional sets of proteins are localized to the same areas of the ER/SR membrane. We conclude that active Ca2+ loading of cardiac microsomes, reflecting the combined activities of Ca2+ uptake by SERCA, and Ca2+ leak by RyR, permits evaluation of multiple functional ER/SR subdomains. Sets of proteins from these subdomains exhibited similar enrichment patterns across membrane subfractions, reflecting the relative levels of SERCA and RyR present within individual patches of cardiac ER and SR.

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Section: Resultssupporting

confidence: 65%

Activation of Ca2+ transport in cardiac microsomes enriches functional sets of ER and SR proteins

et al. 2023

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“…For example, sAnk1 is peptide (non-regulin family member) that acts to help target SERCA1 to longitudinal SR and to maintain the ultrastructure of longitudinal SR of mouse myofibers [121]; in addition, sAnk1 also acts as a regulin-like peptide inhibitor of SERCA1 activity in a heterologous expression system [11,70]. On the other hand, the SERCA2 protein contributes to targeting PLN to longitudinal SR of cardiomyocytes, via the newly-identified NEST pathway (nuclear ER to SR via T-tubule transit), as reported by Cala and Chen [122,123]. Similarly, SERCA1 contributes to targeting SLN peptides to endoplasmic reticulum of cultured human embryonic kidney cells [35,36,124].…”

Section: Potential Mechanisms To Control Sln Protein Expression and Serca Regulation In Horse Gluteal Musclementioning

confidence: 79%

Sarcolipin Exhibits Abundant RNA Transcription and Minimal Protein Expression in Horse Gluteal Muscle

Autry

Karim

Perumbakkam

et al. 2020

Veterinary Sciences

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Ca2+ regulation in equine muscle is important for horse performance, yet little is known about this species-specific regulation. We reported recently that horse encode unique gene and protein sequences for the sarcoplasmic reticulum (SR) Ca2+-transporting ATPase (SERCA) and the regulatory subunit sarcolipin (SLN). Here we quantified gene transcription and protein expression of SERCA and its inhibitory peptides in horse gluteus, as compared to commonly-studied rabbit skeletal muscle. RNA sequencing and protein immunoblotting determined that horse gluteus expresses the ATP2A1 gene (SERCA1) as the predominant SR Ca2+-ATPase isoform and the SLN gene as the most-abundant SERCA inhibitory peptide, as also found in rabbit skeletal muscle. Equine muscle expresses an insignificant level of phospholamban (PLN), another key SERCA inhibitory peptide expressed commonly in a variety of mammalian striated muscles. Surprisingly in horse, the RNA transcript ratio of SLN-to-ATP2A1 is an order of magnitude higher than in rabbit, while the corresponding protein expression ratio is an order of magnitude lower than in rabbit. Thus, SLN is not efficiently translated or maintained as a stable protein in horse muscle, suggesting a non-coding role for supra-abundant SLN mRNA. We propose that the lack of SLN and PLN inhibition of SERCA activity in equine muscle is an evolutionary adaptation that potentiates Ca2+ cycling and muscle contractility in a prey species domestically selected for speed.

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“…Finally, CM contain a large number of mitochondria, which maintain high levels of ATP required by the cells to promote the contraction and relaxation of the heart muscle [59,60]. CM produce and secrete several mediators such as adiponectin [61], regenerating islet-derived protein 3-β [62], TNF-α, interleukin-1β (IL-1β), interferon γ [63], transforming growth factor β (TGF-β) [64], IL-6 and IL-11 [65,66]. It has been shown that CM are also a source of angiogenic factors, such as angiopoietin 1 (ANGPT1), ANGPT2 [67,68] and mainly VEGF-A [69].…”

Section: Cardiomyocytesmentioning

confidence: 99%

“…CM produce and secrete several mediators such as adiponectin [ 61 ], regenerating islet-derived protein 3-β [ 62 ], TNF-α, interleukin-1β (IL-1β), interferon γ [ 63 ], transforming growth factor β (TGF-β) [ 64 ], IL-6 and IL-11 [ 65 , 66 ]. It has been shown that CM are also a source of angiogenic factors, such as angiopoietin 1 (ANGPT1), ANGPT2 [ 67 , 68 ] and mainly VEGF-A [ 69 ].…”

Section: Cardiomyocytesmentioning

confidence: 99%

VEGF-A in Cardiomyocytes and Heart Diseases

Braile

Marcella

Cristinziano

et al. 2020

IJMS

176

107

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The vascular endothelial growth factor (VEGF), a homodimeric vasoactive glycoprotein, is the key mediator of angiogenesis. Angiogenesis, the formation of new blood vessels, is responsible for a wide variety of physio/pathological processes, including cardiovascular diseases (CVD). Cardiomyocytes (CM), the main cell type present in the heart, are the source and target of VEGF-A and express its receptors, VEGFR1 and VEGFR2, on their cell surface. The relationship between VEGF-A and the heart is double-sided. On the one hand, VEGF-A activates CM, inducing morphogenesis, contractility and wound healing. On the other hand, VEGF-A is produced by CM during inflammation, mechanical stress and cytokine stimulation. Moreover, high concentrations of VEGF-A have been found in patients affected by different CVD, and are often correlated with an unfavorable prognosis and disease severity. In this review, we summarized the current knowledge about the expression and effects of VEGF-A on CM and the role of VEGF-A in CVD, which are the most important cause of disability and premature death worldwide. Based on clinical studies on angiogenesis therapy conducted to date, it is possible to think that the control of angiogenesis and VEGF-A can lead to better quality and span of life of patients with heart disease.

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Adiponectin secretion from cardiomyocytes produces canonical multimers and partial co-localization with calsequestrin in junctional SR

Cited by 7 publications

References 41 publications

Activation of Ca2+ transport in cardiac microsomes enriches functional sets of ER and SR proteins

Activation of Ca2+ transport in cardiac microsomes enriches functional sets of ER and SR proteins

Sarcolipin Exhibits Abundant RNA Transcription and Minimal Protein Expression in Horse Gluteal Muscle

VEGF-A in Cardiomyocytes and Heart Diseases

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