User:Morgane Crausaz/Sandbox - Revision history

Morgane Crausaz at 17:48, 26 January 2017

Morgane Crausaz — Thu, 26 Jan 2017 17:48:08 GMT

Morgane Crausaz at 17:36, 26 January 2017

Morgane Crausaz — Thu, 26 Jan 2017 17:36:19 GMT

←Older revision		Revision as of 17:36, 26 January 2017
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	[[Image:structure_secondaire.png \|1000px\|center\|thumb]]		[[Image:structure_secondaire.png \|1000px\|center\|thumb]]

-	The protein is divided into <scene name='75/750241/Domain/1'>three domains</scene>. First, the <scene name='75/750241/Membrane_binding_domain/2'>membrane binding domain</scene> from Leucine 18 to Proline 81, contains six beta strand and two alpha ~~helixes~~. The <scene name='75/750241/Cap_domain2/1'>cap domain</scene> from Glycine 198 to Threonine 288 then, from Glycine 301 to Glycine 324 presents five alpha helix and four beta strand. Finally, the <scene name='75/750241/Actif_domain/1'>hydrolase domain</scene> from Alanine 1 to Glutamine 17, from Glycine 82 to Glycine 197, from Methionine 289 to Threonine 300, then, from Aspartate 325 to the end of the protein.	+	The protein is divided into <scene name='75/750241/Domain/1'>three domains</scene>. First, the <scene name='75/750241/Membrane_binding_domain/2'>membrane binding domain</scene> from Leucine 18 to Proline 81, contains six beta strand and two alpha helices. The <scene name='75/750241/Cap_domain2/1'>cap domain</scene> from Glycine 198 to Threonine 288 then, from Glycine 301 to Glycine 324 presents five alpha helix and four beta strand. Finally, the <scene name='75/750241/Actif_domain/1'>hydrolase domain</scene> from Alanine 1 to Glutamine 17, from Glycine 82 to Glycine 197, from Methionine 289 to Threonine 300, then, from Aspartate 325 to the end of the protein.

	The lysosomal phospholipase A2 has a <scene name='75/750241/Catalytic_site/1'>catalytic triad</scene> in the alpha/beta hydrolase domain at conserved topological positions: Serine 165, Aspartate 327 and Histidine 359.		The lysosomal phospholipase A2 has a <scene name='75/750241/Catalytic_site/1'>catalytic triad</scene> in the alpha/beta hydrolase domain at conserved topological positions: Serine 165, Aspartate 327 and Histidine 359.
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	Lysosomal phospholipase A2 degrades glycerophospholipids by '''hydrolysis''', but also plays a role in cellular '''phospholipid homeostasis'''.		Lysosomal phospholipase A2 degrades glycerophospholipids by '''hydrolysis''', but also plays a role in cellular '''phospholipid homeostasis'''.

-	Tissue distribution:	+	'''Tissue distribution''':
	The highest level of lysosomal phospholipase A2 activity was found in alveolar macrophages.		The highest level of lysosomal phospholipase A2 activity was found in alveolar macrophages.
-	It was 40~~-fold~~ higher in alveolar macrophages than other tissues, ~~including~~ monocytes and peritoneal macrophages. <ref>PMID: 16880524</ref>	+	It was 40 times higher in alveolar macrophages than other tissues, such as monocytes and peritoneal macrophages. <ref>PMID: 16880524</ref>

	==Mechanism==		==Mechanism==

Morgane Crausaz at 17:26, 26 January 2017

Morgane Crausaz — Thu, 26 Jan 2017 17:26:40 GMT

←Older revision		Revision as of 17:26, 26 January 2017
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	The lysosome is a membrane-bound organelle which is present in animal cells. Those are acidic vesicles and contain more than fifty digestive enzymes such as proteases, nucleases, glycosidases, sulfatases, lipases, phosphatases phospholipases and esterases. The lumen’s pH of 4,5 is optimal for the hydrolytic enzymes. Indeed, ''acidic pH'' is important for the degradation of intracellular and extracellular compounds.<ref>PMID: 19356018</ref><ref>PMID:21638687</ref> <ref>DOI 10.1002/ijch.201300024</ref>		The lysosome is a membrane-bound organelle which is present in animal cells. Those are acidic vesicles and contain more than fifty digestive enzymes such as proteases, nucleases, glycosidases, sulfatases, lipases, phosphatases phospholipases and esterases. The lumen’s pH of 4,5 is optimal for the hydrolytic enzymes. Indeed, ''acidic pH'' is important for the degradation of intracellular and extracellular compounds.<ref>PMID: 19356018</ref><ref>PMID:21638687</ref> <ref>DOI 10.1002/ijch.201300024</ref>

-	Particularly, there are enzymes able to cleave phospholipids on a specific site: '''phospholipases'''. These phospholipases are classified into four types, ''phospholipase A1, A2, C and D'' depending on the specific cleavage site of the substrate. The Phospholipase A2 cleaves the acyl-ester bonds of '''sn-2 position of glycerophospholipids''' and they produce''' free fatty acids'''.<ref>PMID: 21074554</ref> <ref>ATCC: The Global Bioresource Center. Available at: https://www.lgcstandards-atcc.org/. (Accessed: 22nd January 2017)</ref>	+	Particularly, there are enzymes able to cleave phospholipids on a specific site: '''phospholipases'''. These phospholipases are classified into four types, ''phospholipase A1, A2, C and D'' depending on the specific cleavage site of the substrate. The Phospholipase A2 cleaves the acyl-ester bonds on '''sn-2 position of glycerophospholipids''' and they produce''' free fatty acids'''.<ref>PMID: 21074554</ref> <ref>ATCC: The Global Bioresource Center. Available at: https://www.lgcstandards-atcc.org/. (Accessed: 22nd January 2017)</ref>


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	[[Image:structure_secondaire.png \|1000px\|center\|thumb]]		[[Image:structure_secondaire.png \|1000px\|center\|thumb]]

-	The protein is divided in <scene name='75/750241/Domain/1'>three domains</scene>. First, the <scene name='75/750241/Membrane_binding_domain/2'>membrane binding domain</scene> from Leucine 18 to Proline 81, contains six beta strand and two alpha helixes. The <scene name='75/750241/Cap_domain2/1'>cap domain</scene> from Glycine 198 to Threonine 288 then, from Glycine 301 to Glycine 324 presents five alpha helix and four beta strand. Finally, the <scene name='75/750241/Actif_domain/1'>hydrolase domain</scene> from Alanine 1 to Glutamine 17, from Glycine 82 to Glycine 197, from Methionine 289 to Threonine 300, then, from Aspartate 325 to the end of the protein.	+	The protein is divided into <scene name='75/750241/Domain/1'>three domains</scene>. First, the <scene name='75/750241/Membrane_binding_domain/2'>membrane binding domain</scene> from Leucine 18 to Proline 81, contains six beta strand and two alpha helixes. The <scene name='75/750241/Cap_domain2/1'>cap domain</scene> from Glycine 198 to Threonine 288 then, from Glycine 301 to Glycine 324 presents five alpha helix and four beta strand. Finally, the <scene name='75/750241/Actif_domain/1'>hydrolase domain</scene> from Alanine 1 to Glutamine 17, from Glycine 82 to Glycine 197, from Methionine 289 to Threonine 300, then, from Aspartate 325 to the end of the protein.

	The lysosomal phospholipase A2 has a <scene name='75/750241/Catalytic_site/1'>catalytic triad</scene> in the alpha/beta hydrolase domain at conserved topological positions: Serine 165, Aspartate 327 and Histidine 359.		The lysosomal phospholipase A2 has a <scene name='75/750241/Catalytic_site/1'>catalytic triad</scene> in the alpha/beta hydrolase domain at conserved topological positions: Serine 165, Aspartate 327 and Histidine 359.

Morgane Crausaz at 17:19, 26 January 2017

Morgane Crausaz — Thu, 26 Jan 2017 17:19:23 GMT

←Older revision		Revision as of 17:19, 26 January 2017
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	The lysosome is a membrane-bound organelle which is present in animal cells. Those are acidic vesicles and contain more than fifty digestive enzymes such as proteases, nucleases, glycosidases, sulfatases, lipases, phosphatases phospholipases and esterases. The lumen’s pH of 4,5 is optimal for the hydrolytic enzymes. Indeed, ''acidic pH'' is important for the degradation of intracellular and extracellular compounds.<ref>PMID: 19356018</ref><ref>PMID:21638687</ref> <ref>DOI 10.1002/ijch.201300024</ref>		The lysosome is a membrane-bound organelle which is present in animal cells. Those are acidic vesicles and contain more than fifty digestive enzymes such as proteases, nucleases, glycosidases, sulfatases, lipases, phosphatases phospholipases and esterases. The lumen’s pH of 4,5 is optimal for the hydrolytic enzymes. Indeed, ''acidic pH'' is important for the degradation of intracellular and extracellular compounds.<ref>PMID: 19356018</ref><ref>PMID:21638687</ref> <ref>DOI 10.1002/ijch.201300024</ref>

-	Particularly, there are enzymes able to cleave phospholipids on a specific site~~: those enzymes are named~~: '''phospholipases'''. These phospholipases are classified into four types, ''phospholipase A1, A2, C and D'' depending on the specific cleavage site of the substrate. The Phospholipase A2 cleaves the acyl-ester bonds of '''sn-2 position of glycerophospholipids''' and they produce''' free fatty acids'''.<ref>PMID: 21074554</ref> <ref>ATCC: The Global Bioresource Center. Available at: https://www.lgcstandards-atcc.org/. (Accessed: 22nd January 2017)</ref>	+	Particularly, there are enzymes able to cleave phospholipids on a specific site: '''phospholipases'''. These phospholipases are classified into four types, ''phospholipase A1, A2, C and D'' depending on the specific cleavage site of the substrate. The Phospholipase A2 cleaves the acyl-ester bonds of '''sn-2 position of glycerophospholipids''' and they produce''' free fatty acids'''.<ref>PMID: 21074554</ref> <ref>ATCC: The Global Bioresource Center. Available at: https://www.lgcstandards-atcc.org/. (Accessed: 22nd January 2017)</ref>

Morgane Crausaz at 15:12, 26 January 2017

Morgane Crausaz — Thu, 26 Jan 2017 15:12:13 GMT

←Older revision		Revision as of 15:12, 26 January 2017
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	The lysosome is a membrane-bound organelle which is present in animal cells. Those are acidic vesicles and contain more than fifty digestive enzymes such as proteases, nucleases, glycosidases, sulfatases, lipases, phosphatases phospholipases and esterases. The lumen’s pH of 4,5 is optimal for the hydrolytic enzymes. Indeed, ''acidic pH'' is important for the degradation of intracellular and extracellular compounds.<ref>PMID: 19356018</ref><ref>PMID:21638687</ref> <ref>DOI 10.1002/ijch.201300024</ref>		The lysosome is a membrane-bound organelle which is present in animal cells. Those are acidic vesicles and contain more than fifty digestive enzymes such as proteases, nucleases, glycosidases, sulfatases, lipases, phosphatases phospholipases and esterases. The lumen’s pH of 4,5 is optimal for the hydrolytic enzymes. Indeed, ''acidic pH'' is important for the degradation of intracellular and extracellular compounds.<ref>PMID: 19356018</ref><ref>PMID:21638687</ref> <ref>DOI 10.1002/ijch.201300024</ref>

-	Particularly, there are enzymes able to cleave phospholipids on a specific site: those enzymes are named: '''phospholipases'''. These phospholipases are classified into four types, ''phospholipase A1, A2, C and D'' depending on the specific cleavage site of the substrate. Phospholipase A2 ~~cleave~~ the acyl-ester bonds of '''sn-2 position of glycerophospholipids''' and they produce''' free fatty acids'''.<ref>PMID: 21074554</ref> <ref>ATCC: The Global Bioresource Center. Available at: https://www.lgcstandards-atcc.org/. (Accessed: 22nd January 2017)</ref>	+	Particularly, there are enzymes able to cleave phospholipids on a specific site: those enzymes are named: '''phospholipases'''. These phospholipases are classified into four types, ''phospholipase A1, A2, C and D'' depending on the specific cleavage site of the substrate. The Phospholipase A2 cleaves the acyl-ester bonds of '''sn-2 position of glycerophospholipids''' and they produce''' free fatty acids'''.<ref>PMID: 21074554</ref> <ref>ATCC: The Global Bioresource Center. Available at: https://www.lgcstandards-atcc.org/. (Accessed: 22nd January 2017)</ref>

Morgane Crausaz at 15:05, 26 January 2017

Morgane Crausaz — Thu, 26 Jan 2017 15:05:19 GMT

←Older revision		Revision as of 15:05, 26 January 2017
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	==Introduction==		==Introduction==

-	The lysosome is a membrane-bound organelle which is present in animal cells. Those are acidic vesicles and contain more than fifty digestive enzymes such as proteases, nucleases, glycosidases, sulfatases, lipases, phosphatases phospholipases and esterases. The lumen’s pH of 4,5 is optimal for the hydrolytic enzymes. Indeed, acidic pH is important for the degradation of intracellular and extracellular compounds.<ref>PMID: 19356018</ref><ref>PMID:21638687</ref> <ref>DOI 10.1002/ijch.201300024</ref>	+	The lysosome is a membrane-bound organelle which is present in animal cells. Those are acidic vesicles and contain more than fifty digestive enzymes such as proteases, nucleases, glycosidases, sulfatases, lipases, phosphatases phospholipases and esterases. The lumen’s pH of 4,5 is optimal for the hydrolytic enzymes. Indeed, ''acidic pH'' is important for the degradation of intracellular and extracellular compounds.<ref>PMID: 19356018</ref><ref>PMID:21638687</ref> <ref>DOI 10.1002/ijch.201300024</ref>

	Particularly, there are enzymes able to cleave phospholipids on a specific site: those enzymes are named: '''phospholipases'''. These phospholipases are classified into four types, ''phospholipase A1, A2, C and D'' depending on the specific cleavage site of the substrate. Phospholipase A2 cleave the acyl-ester bonds of '''sn-2 position of glycerophospholipids''' and they produce''' free fatty acids'''.<ref>PMID: 21074554</ref> <ref>ATCC: The Global Bioresource Center. Available at: https://www.lgcstandards-atcc.org/. (Accessed: 22nd January 2017)</ref>		Particularly, there are enzymes able to cleave phospholipids on a specific site: those enzymes are named: '''phospholipases'''. These phospholipases are classified into four types, ''phospholipase A1, A2, C and D'' depending on the specific cleavage site of the substrate. Phospholipase A2 cleave the acyl-ester bonds of '''sn-2 position of glycerophospholipids''' and they produce''' free fatty acids'''.<ref>PMID: 21074554</ref> <ref>ATCC: The Global Bioresource Center. Available at: https://www.lgcstandards-atcc.org/. (Accessed: 22nd January 2017)</ref>

Morgane Crausaz at 14:59, 26 January 2017

Morgane Crausaz — Thu, 26 Jan 2017 14:59:42 GMT

←Older revision		Revision as of 14:59, 26 January 2017
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	Tissue distribution:		Tissue distribution:
	The highest level of lysosomal phospholipase A2 activity was found in alveolar macrophages.		The highest level of lysosomal phospholipase A2 activity was found in alveolar macrophages.
-	It was 40-fold higher in alveolar macrophages than other tissues, including monocytes and peritoneal macrophages. <ref>PMID: 16880524</ref>	+	It was 40-fold higher in alveolar macrophages than other tissues, including monocytes and peritoneal macrophages. <ref>PMID: 16880524</ref>

	==Mechanism==		==Mechanism==
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	-<scene name='75/750241/Cl/1'>Cl</scene> : Chloride are found at His347 (tyrosine kinase site), Gln348 and Gln294 (glycosylation site)		-<scene name='75/750241/Cl/1'>Cl</scene> : Chloride are found at His347 (tyrosine kinase site), Gln348 and Gln294 (glycosylation site)

		+	<ref>http://www.rcsb.org/pdb/explore.do?structureId=4x90</ref><ref>http://www.ebi.ac.uk/pdbe-site/pdbemotif/?tab=boundmolecule&pdb=4x90&ligandCode3letter=cl</ref>

	== Disease's treatment==		== Disease's treatment==

Morgane Crausaz at 14:29, 26 January 2017

Morgane Crausaz — Thu, 26 Jan 2017 14:29:07 GMT

←Older revision		Revision as of 14:29, 26 January 2017
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	-<scene name='75/750241/Mpd/1'>MPD</scene> : (4s)-2-methyl-2,4-pentanediol is found at Asp 13, Asp211 which are glycosylation sites, and Arg214		-<scene name='75/750241/Mpd/1'>MPD</scene> : (4s)-2-methyl-2,4-pentanediol is found at Asp 13, Asp211 which are glycosylation sites, and Arg214

-	-PO4 ~~ligand~~ : Phosphate, observed at His347, a tyrosine kinase phosphorylation site and Glu346, a glycosylation site	+	-PO4 : Phosphate, observed at His347, a tyrosine kinase phosphorylation site and Glu346, a glycosylation site

	-<scene name='75/750241/Cl/1'>Cl</scene> : Chloride are found at His347 (tyrosine kinase site), Gln348 and Gln294 (glycosylation site)		-<scene name='75/750241/Cl/1'>Cl</scene> : Chloride are found at His347 (tyrosine kinase site), Gln348 and Gln294 (glycosylation site)

Morgane Crausaz at 14:27, 26 January 2017

Morgane Crausaz — Thu, 26 Jan 2017 14:27:12 GMT

←Older revision		Revision as of 14:27, 26 January 2017
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	The highest level of lysosomal phospholipase A2 activity was found in alveolar macrophages.		The highest level of lysosomal phospholipase A2 activity was found in alveolar macrophages.
	It was 40-fold higher in alveolar macrophages than other tissues, including monocytes and peritoneal macrophages. <ref>PMID: 16880524</ref>		It was 40-fold higher in alveolar macrophages than other tissues, including monocytes and peritoneal macrophages. <ref>PMID: 16880524</ref>
-

	==Mechanism==		==Mechanism==
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	==Ligands==		==Ligands==

-	~~LPLA2~~ has 5 types of ligands :	+	Lysosomal phospholipase A2 has 5 types of <scene name='75/750241/Ligands/1'>ligands</scene> :

-	-'''NAG~~''' ligand~~ : N-acetylglucosamine sugars are observed at Asn66, Asn240, Asn256 and Asn365 (found on Asn-X-Ser/Thr motifs) and are N-glycosylation sites. NAG are useful for a post-translational modification : glycosylation	+	-<scene name='75/750241/Nag/1'>NAG</scene> : N-acetylglucosamine sugars are observed at Asn66, Asn240, Asn256 and Asn365 (found on Asn-X-Ser/Thr motifs) and are N-glycosylation sites. NAG are useful for a post-translational modification : glycosylation

-	-'''EPE~~''' ligand~~ : 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid (or HEPES) is observed at Ser33, a tyrosine kinase phosphorylation site. EPE is a zwitterion, its dissociation in water decreases as the heat decreases, allowing to maintain enzyme structure and function at low temperature	+	-<scene name='75/750241/Epe/1'>EPE</scene> : 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid (or HEPES) is observed at Ser33, a tyrosine kinase phosphorylation site. EPE is a zwitterion, its dissociation in water decreases as the heat decreases, allowing to maintain enzyme structure and function at low temperature

-	-'''MPD~~''' ligand~~ : (4s)-2-methyl-2,4-pentanediol is found at Asp 13, Asp211 which are glycosylation sites, and Arg214	+	-<scene name='75/750241/Mpd/1'>MPD</scene> : (4s)-2-methyl-2,4-pentanediol is found at Asp 13, Asp211 which are glycosylation sites, and Arg214

	-PO4 ligand : Phosphate, observed at His347, a tyrosine kinase phosphorylation site and Glu346, a glycosylation site		-PO4 ligand : Phosphate, observed at His347, a tyrosine kinase phosphorylation site and Glu346, a glycosylation site

-	-Cl ~~ligand~~ : Chloride are found at His347 (tyrosine kinase site), Gln348 and Gln294 (glycosylation site)	+	-<scene name='75/750241/Cl/1'>Cl</scene> : Chloride are found at His347 (tyrosine kinase site), Gln348 and Gln294 (glycosylation site)
-		+

Morgane Crausaz at 14:05, 26 January 2017

Morgane Crausaz — Thu, 26 Jan 2017 14:05:56 GMT

←Older revision		Revision as of 14:05, 26 January 2017
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	==Function==		==Function==
-	Lysosomal phospholipase A2 degrades glycerophospholipids by hydrolysis, but also plays a role in cellular phospholipid homeostasis.
-
-	[[LPLA2 tissue distribution]] :
-	The highest level of LPLA2 activity was found in alveolar macrophages. LPLA2 activity was 40-fold higher in alveolar macrophages than other tissues, including monocytes and peritoneal macrophages. <ref>PMID: 16880524</ref>

		+	Lysosomal phospholipase A2 degrades glycerophospholipids by '''hydrolysis''', but also plays a role in cellular '''phospholipid homeostasis'''.

		+	Tissue distribution:
		+	The highest level of lysosomal phospholipase A2 activity was found in alveolar macrophages.
		+	It was 40-fold higher in alveolar macrophages than other tissues, including monocytes and peritoneal macrophages. <ref>PMID: 16880524</ref>


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	The lysosomal phospholipase A2 activity is strongly dependent on pH, and is the highest at pH 4.5, a pH commonly found in lysosomes and in local inflammation events.		The lysosomal phospholipase A2 activity is strongly dependent on pH, and is the highest at pH 4.5, a pH commonly found in lysosomes and in local inflammation events.
-	Bis monoacylglycerol phosphate (BMP) inducing a negative charge on lysosomal membrane, the electrostatic repulsion is weakened between ~~LPLA2~~ and the membrane at low pH.	+	Bis monoacylglycerol phosphate (BMP) inducing a negative charge on lysosomal membrane, the electrostatic repulsion is weakened between lysosomal phospholipase A2 and the membrane at low pH.
-	The protein has a global basic electrostatic surface that is complementary of the acidic inner membrane of the lysosomal membrane. The structure shows a hydrophobic surface including Tyrosine 30, Leucine 31, Leucine 50 and Valine 52 on the membrane-binding domain which would be sufficient to bring the protein to the lipid bilayers.	+	The protein has a global '''basic electrostatic surface''' that is complementary of the acidic inner membrane of the lysosomal membrane. The structure shows a hydrophobic surface including Tyrosine 30, Leucine 31, Leucine 50 and Valine 52 on the membrane-binding domain which would be sufficient to bring the protein to the lipid bilayers.

-	After docking on membrane, a phospholipid, substrate of the enzyme, enters into the active site. The catalytic triad is located such a way to cleave the acyl group of the phospholipids. The serine is able to act as a nucleophile cleave the acyl-ester bonds. The histidine of the catalytic triad is placed to protonate the lysophospholipid after the cleavage.<ref>PMID: 25727495</ref>	+	After docking on membrane, a phospholipid, substrate of the enzyme, enters into the '''active site'''. The catalytic triad is located such a way to '''cleave''' the acyl group of the phospholipids. The serine is able to act as a nucleophile cleave the acyl-ester bonds. The histidine of the catalytic triad is placed to protonate the lysophospholipid after the cleavage.<ref>PMID: 25727495</ref>

	==Ligands==		==Ligands==

←Older revision		Revision as of 17:48, 26 January 2017
Line 36:		Line 36:
	==Mechanism==		==Mechanism==

-	The lysosomal phospholipase A2 activity is strongly dependent on pH, and is the highest at pH 4.5, a pH commonly found in lysosomes and in local inflammation events.	+	The lysosomal phospholipase A2 activity is strongly dependent on pH and is the highest at pH 4.5, a pH commonly found in lysosomes and in local inflammation events.
-	Bis ~~monoacylglycerol phosphate~~ (BMP) inducing a negative charge on lysosomal membrane, the electrostatic repulsion is weakened between lysosomal phospholipase A2 and the membrane at low pH.	+	Bis Monoacylglycerol Phosphate (BMP) inducing a negative charge on lysosomal membrane, the electrostatic repulsion is weakened between lysosomal phospholipase A2 and the membrane at low pH.
	The protein has a global '''basic electrostatic surface''' that is complementary of the acidic inner membrane of the lysosomal membrane. The structure shows a hydrophobic surface including Tyrosine 30, Leucine 31, Leucine 50 and Valine 52 on the membrane-binding domain which would be sufficient to bring the protein to the lipid bilayers.		The protein has a global '''basic electrostatic surface''' that is complementary of the acidic inner membrane of the lysosomal membrane. The structure shows a hydrophobic surface including Tyrosine 30, Leucine 31, Leucine 50 and Valine 52 on the membrane-binding domain which would be sufficient to bring the protein to the lipid bilayers.

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	Lysosomal phospholipase A2 has 5 types of <scene name='75/750241/Ligands/1'>ligands</scene> :		Lysosomal phospholipase A2 has 5 types of <scene name='75/750241/Ligands/1'>ligands</scene> :

-	-<scene name='75/750241/Nag/1'>NAG</scene> : N-acetylglucosamine sugars are observed at Asn66, Asn240, Asn256 and Asn365 (found on Asn-X-Ser/Thr motifs) and are N-glycosylation sites. NAG are useful for a post-translational modification : glycosylation	+	-<scene name='75/750241/Nag/1'>NAG</scene> : N-acetylglucosamine sugars are observed at Asn66, Asn240, Asn256 and Asn365 (found on Asn-X-Ser/Thr motifs) and are N-glycosylation sites. NAG are useful for a post-translational modification : glycosylation.

-	-<scene name='75/750241/Epe/1'>EPE</scene> : 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid (or HEPES) is observed at Ser33, a tyrosine kinase phosphorylation site. EPE is a zwitterion, its dissociation in water decreases as the heat decreases, allowing to maintain enzyme structure and function at low temperature	+	-<scene name='75/750241/Epe/1'>EPE</scene> : 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid (or HEPES) is observed at Ser33, a tyrosine kinase phosphorylation site. EPE is a zwitterion, its dissociation in water decreases as the heat decreases, allowing to maintain enzyme structure and function at low temperature.

	-<scene name='75/750241/Mpd/1'>MPD</scene> : (4s)-2-methyl-2,4-pentanediol is found at Asp 13, Asp211 which are glycosylation sites, and Arg214		-<scene name='75/750241/Mpd/1'>MPD</scene> : (4s)-2-methyl-2,4-pentanediol is found at Asp 13, Asp211 which are glycosylation sites, and Arg214

-	-PO4 : Phosphate, observed at His347, a tyrosine kinase phosphorylation site and Glu346, a glycosylation site	+	-PO4 : Phosphate, observed at His347, a tyrosine kinase phosphorylation site and Glu346, a glycosylation site.

-	-<scene name='75/750241/Cl/1'>Cl</scene> : Chloride are found at His347 (tyrosine kinase site), Gln348 and Gln294 (glycosylation site)	+	-<scene name='75/750241/Cl/1'>Cl</scene> : Chloride are found at His347 (tyrosine kinase site), Gln348 and Gln294 (glycosylation site).

	<ref>http://www.rcsb.org/pdb/explore.do?structureId=4x90</ref><ref>http://www.ebi.ac.uk/pdbe-site/pdbemotif/?tab=boundmolecule&pdb=4x90&ligandCode3letter=cl</ref>		<ref>http://www.rcsb.org/pdb/explore.do?structureId=4x90</ref><ref>http://www.ebi.ac.uk/pdbe-site/pdbemotif/?tab=boundmolecule&pdb=4x90&ligandCode3letter=cl</ref>
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	== Disease's treatment==		== Disease's treatment==

-	Implication of ~~the~~ lysosomal phospholipase A2 in ~~the~~ detoxification :	+	Implication of lysosomal phospholipase A2 in detoxification :

	Lipid oxidation products and in particular '''oxidized phospholipids (OxPL)''' are increasingly recognized as inducers of chronic inflammation characteristic of '''atherosclerosis'''. Atherosclerosis is a chronic inflammatory disease characterized by accumulation of monocytes and T-cells due to lipid abnormalities. Increased levels of phospholipids’ oxidation products have been detected in different organs and pathological states, including atherosclerotic vessels. They can integrate the lipid membranes of cells and lipoproteins, act as ligands and may cause local membrane disruption. Indeed, they stimulate production of chemokines and adhesion of monocytes to endothelial cells.		Lipid oxidation products and in particular '''oxidized phospholipids (OxPL)''' are increasingly recognized as inducers of chronic inflammation characteristic of '''atherosclerosis'''. Atherosclerosis is a chronic inflammatory disease characterized by accumulation of monocytes and T-cells due to lipid abnormalities. Increased levels of phospholipids’ oxidation products have been detected in different organs and pathological states, including atherosclerotic vessels. They can integrate the lipid membranes of cells and lipoproteins, act as ligands and may cause local membrane disruption. Indeed, they stimulate production of chemokines and adhesion of monocytes to endothelial cells.