Localization of Annexin V in the Adult and Neonatal Heart

Luckcuck, Tracy; Trotter, Patrick J.; Walker, John H.

doi:10.1006/bbrc.1997.7350

Cited by 16 publications

(13 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Taken together, our results indicated that annexin V was present in sarcolemma, and intercalated discs, and in the T-tubules connected to the terminal cisternae of sarcoplasmic reticulum -the complex in which the excitation-contraction coupling took place. Therefore, labeling of annexin V in human heart was similar to that of other species (Doubell et al, 1993;Jans et al, 1995;Luckcuck et al, 1997;Trouvé et al, 1999;Van Bilsen et al, 1992;Wang et al, 1995). Interestingly, immunofluorescence of annexin V in failing hearts (Fig.…”

Section: Annexins In Failing Human Heartsupporting

confidence: 65%

“…Annexin V is able to form voltage-gated Ca 2ϩ channels (Pollard et al, 1992) and to modulate activity of protein kinase C and phospholipase A 2 Mira et al, 1998;Van Bilsen et al, 1992). In myocardium, the localization of annexin V is not clearly established: the presence of annexin V was first reported in endothelium and fibroblasts (Van Bilsen et al, 1992), then in myocytes in which it has been detected either in cytosol (Jans et al, 1995), in membranes (Luckcuck et al, 1997;Trouvé et al, 1999), or associated with Z-lines (Trouvé et al, 1999;Wang et al, 1995). Annexin VI has been localized in rat, bovine, and guinea pig hearts mainly in sarcolemma and intercalated discs of cardiomyocytes (Doubell et al, 1993;Iida et al, 1992;Luckcuck et al, 1997;Trouvé et al, 1999).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Expression and Localization of the Annexins II, V, and VI in Myocardium from Patients with End-Stage Heart Failure

Benevolensky

Belikova

Mohammadzadeh

et al. 2000

Laboratory Investigation

View full text Add to dashboard Cite

SUMMARY:Annexins II, V, and VI belong to a family of Ca 2ϩ -dependent phospholipid-binding proteins that have been involved mainly in signal transduction, differentiation, membrane trafficking events, or binding to the extracellular matrix, or that might be effective as Ca 2ϩ -channels. They are abundant in the mammalian myocardium and might play a role in ventricular remodeling and altered calcium handling during heart failure. To test this hypothesis, we compared the expression and distribution of these annexins in nonfailing (n ϭ 9) and failing human hearts with idiopathic dilated cardiomyopathy (n ϭ 11). Northern blot and slot blot analysis were used to determine the annexin mRNA levels and Western blots were used to quantify the amounts of annexin proteins. Distribution of annexins was studied by immunohistofluorescence labeling and compared with that of a sarcolemmal marker (Na ϩ /K ϩ -ATPase) and of a myofibrillar protein (␣-actinin). We showed that nonfailing hearts contained a higher amount of annexin VI than of annexin V or II (13.5 Ϯ 1.8, 3.7 Ϯ 0.2, and 2.5 Ϯ 0.5 g/mg protein, respectively). In failing hearts, there was a parallel increase in both mRNA and protein levels of annexin II (146% and 132%, p Ͻ 0.05, respectively) and annexin V (152%, p Ͻ 0.01, 147%, p Ͻ 0.005, respectively); the protein level of annexin VI was also increased (117%, p Ͻ 0.05), whereas the increase of its mRNA level was statistically insignificant. We observed a predominant localization of annexin II in interstitium, and of annexins V and VI in cardiomyocytes at the level of the sarcolemma, T-tubules, and intercalated disks in nonfailing hearts, whereas in failing hearts enlarged interstitium contained all three annexins. Furthermore, annexin V staining at the level of cardiomyocytes almost disappeared. In conclusion, we showed that heart failure is accompanied by marked overexpression of annexins II and V, as well as translocation of annexin V from cardiomyocytes to interstitial tissue. The data suggest that annexins may contribute to ventricular remodeling and annexin V to impaired Ca 2ϩ handling in failing heart. (Lab Invest 2000, 80:123-133).

show abstract

Section: Annexins In Failing Human Heartsupporting

confidence: 65%

mentioning

confidence: 99%

Expression and Localization of the Annexins II, V, and VI in Myocardium from Patients with End-Stage Heart Failure

Benevolensky

Belikova

Mohammadzadeh

et al. 2000

Laboratory Investigation

View full text Add to dashboard Cite

show abstract

“…In normal myocardium, we and others have previously shown that annexin A5 was found in cardiomyocytes, at the level of sarcolemma, intercalated discs and T-tubules [17][18][19][20]. However, in failing myocardium, a pathological situation associated with increased cardiomyocyte apoptosis, we have reported an increased expression and a translocation of endogenous annexin A5 to the interstitial tissue [20].…”

Section: Introductionmentioning

confidence: 57%

Externalization of endogenous annexin A5 participates in apoptosis of rat cardiomyocytes

Monceau

Belikova

Kratassiouk

et al. 2004

Cardiovascular Research

View full text Add to dashboard Cite

show abstract

“…They can be co-expressed in the same cell type but with their own localization. Endothelial cells expressed annexins A1, A2, A5 and A6 [34], smooth muscle cells expressed mainly annexins A2 and A6 [35], whereas cardiomyocytes expressed mainly annexins A4, A5, A6 and A7 [36][37][38][39]. The overall cellular [Ca 2+ ] i and the very high submembranous local [Ca 2+ ] in cardiomyocytes [40] should allow annexins to be present in or to rapidly translocate to SL and SR membranes.…”

Section: Myocardial Annexinsmentioning

confidence: 99%

Annexins and Ca handling in the heart

Camors

Monceau

Charlemagne

2005

Cardiovascular Research

View full text Add to dashboard Cite

Annexins are a family of 13 proteins known to bind phospholipids (PL) in a Ca(2+)-dependent way. They are ubiquitous proteins and share a similar structure characterized by a conserved C-terminal domain with Ca(2+) binding sites and a variable N-terminal domain. Depending on Ca(2+) concentration, they have been reported to participate in a variety of membrane-related events such as exocytosis, endocytosis, apoptosis and binding to cytoskeletal proteins. They have also been reported to regulate protein activities. This review will focus on annexins in the heart, and particularly on annexins A2, A5, A6 and A7. Annexin A2 has been found in endothelial cells and reported to play a central role in control of plasmin-mediated processes. Annexin A5 is mainly localized in cardiomyocytes. However, it could be relocated to interstitial tissue in ischemic and failing hearts or it could be externalized and exhibit a proapoptotic effect in cardiomyocytes. Annexin A6 is the most abundant annexin in the heart, and has been localized in various cell types including myocytes. Overexpression of annexin A6 has underlined physiological alterations in contractile mechanics leading to dilated cardiomyopathy, whereas knockout has been found to induce faster changes in Ca(2+) transient and increased contractility, suggesting a negative inotropic role for annexin A6. Annexin A7 is expressed in heart and skeletal muscle. In annexin A7 null mutant mice decreases in the force-frequency relationship were observed in adult cardiomyocytes, consistent with regulation of Ca(2+) handling. In conclusion, while annexin A2 was involved in regulation of fibrin homeostasis, alterations in expression and activity of annexins A5, A6 and A7 have been associated with regulation of Ca(2+) handling in the heart, but the target of each annexin has not yet been identified.

show abstract

Localization of Annexin V in the Adult and Neonatal Heart

Cited by 16 publications

References 38 publications

Expression and Localization of the Annexins II, V, and VI in Myocardium from Patients with End-Stage Heart Failure

Expression and Localization of the Annexins II, V, and VI in Myocardium from Patients with End-Stage Heart Failure

Externalization of endogenous annexin A5 participates in apoptosis of rat cardiomyocytes

Annexins and Ca handling in the heart

Contact Info

Product

Resources

About